Full text data of FLAD1
FLAD1
[Confidence: low (only semi-automatic identification from reviews)]
FAD synthase; 2.7.7.2 (FAD pyrophosphorylase; FMN adenylyltransferase; Flavin adenine dinucleotide synthase; Molybdenum cofactor biosynthesis protein-like region; FAD synthase region; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
FAD synthase; 2.7.7.2 (FAD pyrophosphorylase; FMN adenylyltransferase; Flavin adenine dinucleotide synthase; Molybdenum cofactor biosynthesis protein-like region; FAD synthase region; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8NFF5
ID FAD1_HUMAN Reviewed; 587 AA.
AC Q8NFF5; Q8N5J1; Q8N686; Q8WU93; Q8WUJ4; Q96CR8; Q99764; Q9HBN6;
read moreDT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=FAD synthase;
DE EC=2.7.7.2;
DE AltName: Full=FAD pyrophosphorylase;
DE AltName: Full=FMN adenylyltransferase;
DE AltName: Full=Flavin adenine dinucleotide synthase;
DE Includes:
DE RecName: Full=Molybdenum cofactor biosynthesis protein-like region;
DE Includes:
DE RecName: Full=FAD synthase region;
DE Flags: Precursor;
GN Name=FLAD1; ORFNames=PP591;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM
RP 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC TISSUE=Skin;
RX PubMed=16643857; DOI=10.1016/j.bbrc.2006.04.003;
RA Brizio C., Galluccio M., Wait R., Torchetti E.M., Bafunno V.,
RA Accardi R., Gianazza E., Indiveri C., Barile M.;
RT "Over-expression in Escherichia coli and characterization of two
RT recombinant isoforms of human FAD synthetase.";
RL Biochem. Biophys. Res. Commun. 344:1008-1016(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Fischer M.J., Kempter K., Bacher A.;
RT "Cloning, expression and characterization of a human FAD synthetase.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RA Chen X.G., Li Y.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 10-587 (ISOFORM 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 256-587 (ISOFORM 1).
RC TISSUE=Brain, Colon, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-587 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=17049878; DOI=10.1016/j.pep.2006.09.002;
RA Galluccio M., Brizio C., Torchetti E.M., Ferranti P., Gianazza E.,
RA Indiveri C., Barile M.;
RT "Over-expression in Escherichia coli, purification and
RT characterization of isoform 2 of human FAD synthetase.";
RL Protein Expr. Purif. 52:175-181(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-563, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20060505; DOI=10.1016/j.mito.2009.12.149;
RA Torchetti E.M., Brizio C., Colella M., Galluccio M., Giancaspero T.A.,
RA Indiveri C., Roberti M., Barile M.;
RT "Mitochondrial localization of human FAD synthetase isoform 1.";
RL Mitochondrion 10:263-273(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN)
CC to form flavin adenine dinucleotide (FAD) coenzyme.
CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for FMN (PubMed:16643857);
CC KM=0.36 uM for FMN (isoform 2) (PubMed:17049878);
CC Vmax=6.1 nmol/min/mg enzyme (PubMed:16643857);
CC Vmax=3.9 nmol/min/mg enzyme (isoform 2) (PubMed:17049878);
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN:
CC step 1/1.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8NFF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFF5-2; Sequence=VSP_027947;
CC Name=3;
CC IsoId=Q8NFF5-3; Sequence=VSP_027947, VSP_027954;
CC Name=4;
CC IsoId=Q8NFF5-4; Sequence=VSP_027948, VSP_027949, VSP_027951,
CC VSP_027952;
CC Name=5;
CC IsoId=Q8NFF5-5; Sequence=VSP_027948, VSP_027949, VSP_027950,
CC VSP_027953;
CC -!- DOMAIN: The molybdenum cofactor biosynthesis protein-like region
CC may not be functional.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PAPS
CC reductase family. FAD1 subfamily.
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DR EMBL; DQ458779; ABE65383.1; -; mRNA.
DR EMBL; AF481877; AAO49318.1; -; mRNA.
DR EMBL; AF520568; AAM77338.1; -; mRNA.
DR EMBL; AF218022; AAG17264.1; -; mRNA.
DR EMBL; AL451085; CAI13259.1; -; Genomic_DNA.
DR EMBL; AL451085; CAI13260.1; -; Genomic_DNA.
DR EMBL; AL451085; CAI13261.1; -; Genomic_DNA.
DR EMBL; AL451085; CAI13262.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53154.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53155.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53158.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53159.1; -; Genomic_DNA.
DR EMBL; BC011378; AAH11378.1; -; mRNA.
DR EMBL; BC014012; AAH14012.2; -; mRNA.
DR EMBL; BC020253; AAH20253.1; -; mRNA.
DR EMBL; BC021096; AAH21096.2; -; mRNA.
DR EMBL; BC032323; AAH32323.1; -; mRNA.
DR EMBL; U79241; AAB50199.1; -; mRNA.
DR RefSeq; NP_001171820.1; NM_001184891.1.
DR RefSeq; NP_001171821.1; NM_001184892.1.
DR RefSeq; NP_079483.3; NM_025207.4.
DR RefSeq; NP_958800.1; NM_201398.2.
DR RefSeq; XP_005245558.1; XM_005245501.1.
DR UniGene; Hs.118666; -.
DR ProteinModelPortal; Q8NFF5; -.
DR SMR; Q8NFF5; 113-269, 349-560.
DR IntAct; Q8NFF5; 12.
DR MINT; MINT-3042841; -.
DR STRING; 9606.ENSP00000292180; -.
DR PhosphoSite; Q8NFF5; -.
DR DMDM; 74751275; -.
DR PaxDb; Q8NFF5; -.
DR PRIDE; Q8NFF5; -.
DR DNASU; 80308; -.
DR Ensembl; ENST00000292180; ENSP00000292180; ENSG00000160688.
DR Ensembl; ENST00000315144; ENSP00000317296; ENSG00000160688.
DR Ensembl; ENST00000368431; ENSP00000357416; ENSG00000160688.
DR Ensembl; ENST00000368432; ENSP00000357417; ENSG00000160688.
DR Ensembl; ENST00000405236; ENSP00000384323; ENSG00000160688.
DR GeneID; 80308; -.
DR KEGG; hsa:80308; -.
DR UCSC; uc001fgd.2; human.
DR CTD; 80308; -.
DR GeneCards; GC01P154955; -.
DR HGNC; HGNC:24671; FLAD1.
DR HPA; HPA028476; -.
DR HPA; HPA028486; -.
DR HPA; HPA028563; -.
DR MIM; 610595; gene.
DR neXtProt; NX_Q8NFF5; -.
DR PharmGKB; PA142671759; -.
DR eggNOG; COG0175; -.
DR HOVERGEN; HBG058211; -.
DR InParanoid; Q8NFF5; -.
DR KO; K00953; -.
DR OMA; AIAVEIS; -.
DR OrthoDB; EOG7C5M9F; -.
DR PhylomeDB; Q8NFF5; -.
DR BioCyc; MetaCyc:HS08520-MONOMER; -.
DR BRENDA; 2.7.7.2; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q8NFF5; -.
DR UniPathway; UPA00277; UER00407.
DR ChiTaRS; FLAD1; human.
DR GenomeRNAi; 80308; -.
DR NextBio; 70783; -.
DR PRO; PR:Q8NFF5; -.
DR ArrayExpress; Q8NFF5; -.
DR Bgee; Q8NFF5; -.
DR CleanEx; HS_FLAD1; -.
DR Genevestigator; Q8NFF5; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR012183; FAD_synth_Mopterin-bd.
DR InterPro; IPR001453; Mopterin-bd_dom.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF01507; PAPS_reduct; 2.
DR PIRSF; PIRSF036620; MPTbdFAD; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; FAD; Flavoprotein; FMN; Mitochondrion; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1 17 Mitochondrion (Potential).
FT CHAIN 18 587 FAD synthase.
FT /FTId=PRO_0000302737.
FT REGION 114 205 Molybdenum cofactor biosynthesis protein-
FT like.
FT REGION 398 555 FAD synthase.
FT MOD_RES 106 106 Phosphoserine.
FT MOD_RES 378 378 N6-acetyllysine (By similarity).
FT MOD_RES 563 563 Phosphoserine.
FT VAR_SEQ 1 97 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_027947.
FT VAR_SEQ 1 30 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_027948.
FT VAR_SEQ 31 124 LEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAG
FT PPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVT
FT AGIIIVGDEILK -> MQPSSSTPPLHPYSTDGLIFPFNPQ
FT (in isoform 4 and isoform 5).
FT /FTId=VSP_027949.
FT VAR_SEQ 374 437 SSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLH
FT LFHAAVQRKLPDVPNPLQILYIR -> NYLMFQTPSRSCIS
FT AASPLSLSWNSFYRTLSREQAIPENQIASPPSEAKGAEEPW
FT MGPFPGQQG (in isoform 5).
FT /FTId=VSP_027950.
FT VAR_SEQ 374 393 SSLGKKVAGALQTIETSLAQ -> RDLMEEGHYAQSHWWHP
FT RSQ (in isoform 4).
FT /FTId=VSP_027951.
FT VAR_SEQ 394 587 Missing (in isoform 4).
FT /FTId=VSP_027952.
FT VAR_SEQ 438 587 Missing (in isoform 5).
FT /FTId=VSP_027953.
FT VAR_SEQ 544 587 Missing (in isoform 3).
FT /FTId=VSP_027954.
SQ SEQUENCE 587 AA; 65266 MW; F95918B15D9D8106 CRC64;
MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV PSTQDPLFPG
YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS RASELSPGRS VTAGIIIVGD
EILKGHTQDT NTFFLCRTLR SLGVQVCRVS VVPDEVATIA AEVTSFSNRF THVLTAGGIG
PTHDDVTFEA VAQAFGDELK PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP
FRFPLVSVRN VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA
QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS LVPYMPNAVE
QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC VGFNGGKDCT ALLHLFHAAV
QRKLPDVPNP LQILYIRSIS PFPELEQFLQ DTIKRYNLQM LEAEGSMKQA LGELQARHPQ
LEAVLMGTRR TDPYSCSLCP FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY
DRGYTSLGSR ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT
//
ID FAD1_HUMAN Reviewed; 587 AA.
AC Q8NFF5; Q8N5J1; Q8N686; Q8WU93; Q8WUJ4; Q96CR8; Q99764; Q9HBN6;
read moreDT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=FAD synthase;
DE EC=2.7.7.2;
DE AltName: Full=FAD pyrophosphorylase;
DE AltName: Full=FMN adenylyltransferase;
DE AltName: Full=Flavin adenine dinucleotide synthase;
DE Includes:
DE RecName: Full=Molybdenum cofactor biosynthesis protein-like region;
DE Includes:
DE RecName: Full=FAD synthase region;
DE Flags: Precursor;
GN Name=FLAD1; ORFNames=PP591;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM
RP 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC TISSUE=Skin;
RX PubMed=16643857; DOI=10.1016/j.bbrc.2006.04.003;
RA Brizio C., Galluccio M., Wait R., Torchetti E.M., Bafunno V.,
RA Accardi R., Gianazza E., Indiveri C., Barile M.;
RT "Over-expression in Escherichia coli and characterization of two
RT recombinant isoforms of human FAD synthetase.";
RL Biochem. Biophys. Res. Commun. 344:1008-1016(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Fischer M.J., Kempter K., Bacher A.;
RT "Cloning, expression and characterization of a human FAD synthetase.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RA Chen X.G., Li Y.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 10-587 (ISOFORM 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 256-587 (ISOFORM 1).
RC TISSUE=Brain, Colon, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-587 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=17049878; DOI=10.1016/j.pep.2006.09.002;
RA Galluccio M., Brizio C., Torchetti E.M., Ferranti P., Gianazza E.,
RA Indiveri C., Barile M.;
RT "Over-expression in Escherichia coli, purification and
RT characterization of isoform 2 of human FAD synthetase.";
RL Protein Expr. Purif. 52:175-181(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-563, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20060505; DOI=10.1016/j.mito.2009.12.149;
RA Torchetti E.M., Brizio C., Colella M., Galluccio M., Giancaspero T.A.,
RA Indiveri C., Roberti M., Barile M.;
RT "Mitochondrial localization of human FAD synthetase isoform 1.";
RL Mitochondrion 10:263-273(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN)
CC to form flavin adenine dinucleotide (FAD) coenzyme.
CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for FMN (PubMed:16643857);
CC KM=0.36 uM for FMN (isoform 2) (PubMed:17049878);
CC Vmax=6.1 nmol/min/mg enzyme (PubMed:16643857);
CC Vmax=3.9 nmol/min/mg enzyme (isoform 2) (PubMed:17049878);
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN:
CC step 1/1.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8NFF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFF5-2; Sequence=VSP_027947;
CC Name=3;
CC IsoId=Q8NFF5-3; Sequence=VSP_027947, VSP_027954;
CC Name=4;
CC IsoId=Q8NFF5-4; Sequence=VSP_027948, VSP_027949, VSP_027951,
CC VSP_027952;
CC Name=5;
CC IsoId=Q8NFF5-5; Sequence=VSP_027948, VSP_027949, VSP_027950,
CC VSP_027953;
CC -!- DOMAIN: The molybdenum cofactor biosynthesis protein-like region
CC may not be functional.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PAPS
CC reductase family. FAD1 subfamily.
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DR EMBL; DQ458779; ABE65383.1; -; mRNA.
DR EMBL; AF481877; AAO49318.1; -; mRNA.
DR EMBL; AF520568; AAM77338.1; -; mRNA.
DR EMBL; AF218022; AAG17264.1; -; mRNA.
DR EMBL; AL451085; CAI13259.1; -; Genomic_DNA.
DR EMBL; AL451085; CAI13260.1; -; Genomic_DNA.
DR EMBL; AL451085; CAI13261.1; -; Genomic_DNA.
DR EMBL; AL451085; CAI13262.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53154.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53155.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53158.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53159.1; -; Genomic_DNA.
DR EMBL; BC011378; AAH11378.1; -; mRNA.
DR EMBL; BC014012; AAH14012.2; -; mRNA.
DR EMBL; BC020253; AAH20253.1; -; mRNA.
DR EMBL; BC021096; AAH21096.2; -; mRNA.
DR EMBL; BC032323; AAH32323.1; -; mRNA.
DR EMBL; U79241; AAB50199.1; -; mRNA.
DR RefSeq; NP_001171820.1; NM_001184891.1.
DR RefSeq; NP_001171821.1; NM_001184892.1.
DR RefSeq; NP_079483.3; NM_025207.4.
DR RefSeq; NP_958800.1; NM_201398.2.
DR RefSeq; XP_005245558.1; XM_005245501.1.
DR UniGene; Hs.118666; -.
DR ProteinModelPortal; Q8NFF5; -.
DR SMR; Q8NFF5; 113-269, 349-560.
DR IntAct; Q8NFF5; 12.
DR MINT; MINT-3042841; -.
DR STRING; 9606.ENSP00000292180; -.
DR PhosphoSite; Q8NFF5; -.
DR DMDM; 74751275; -.
DR PaxDb; Q8NFF5; -.
DR PRIDE; Q8NFF5; -.
DR DNASU; 80308; -.
DR Ensembl; ENST00000292180; ENSP00000292180; ENSG00000160688.
DR Ensembl; ENST00000315144; ENSP00000317296; ENSG00000160688.
DR Ensembl; ENST00000368431; ENSP00000357416; ENSG00000160688.
DR Ensembl; ENST00000368432; ENSP00000357417; ENSG00000160688.
DR Ensembl; ENST00000405236; ENSP00000384323; ENSG00000160688.
DR GeneID; 80308; -.
DR KEGG; hsa:80308; -.
DR UCSC; uc001fgd.2; human.
DR CTD; 80308; -.
DR GeneCards; GC01P154955; -.
DR HGNC; HGNC:24671; FLAD1.
DR HPA; HPA028476; -.
DR HPA; HPA028486; -.
DR HPA; HPA028563; -.
DR MIM; 610595; gene.
DR neXtProt; NX_Q8NFF5; -.
DR PharmGKB; PA142671759; -.
DR eggNOG; COG0175; -.
DR HOVERGEN; HBG058211; -.
DR InParanoid; Q8NFF5; -.
DR KO; K00953; -.
DR OMA; AIAVEIS; -.
DR OrthoDB; EOG7C5M9F; -.
DR PhylomeDB; Q8NFF5; -.
DR BioCyc; MetaCyc:HS08520-MONOMER; -.
DR BRENDA; 2.7.7.2; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q8NFF5; -.
DR UniPathway; UPA00277; UER00407.
DR ChiTaRS; FLAD1; human.
DR GenomeRNAi; 80308; -.
DR NextBio; 70783; -.
DR PRO; PR:Q8NFF5; -.
DR ArrayExpress; Q8NFF5; -.
DR Bgee; Q8NFF5; -.
DR CleanEx; HS_FLAD1; -.
DR Genevestigator; Q8NFF5; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR012183; FAD_synth_Mopterin-bd.
DR InterPro; IPR001453; Mopterin-bd_dom.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF01507; PAPS_reduct; 2.
DR PIRSF; PIRSF036620; MPTbdFAD; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; FAD; Flavoprotein; FMN; Mitochondrion; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1 17 Mitochondrion (Potential).
FT CHAIN 18 587 FAD synthase.
FT /FTId=PRO_0000302737.
FT REGION 114 205 Molybdenum cofactor biosynthesis protein-
FT like.
FT REGION 398 555 FAD synthase.
FT MOD_RES 106 106 Phosphoserine.
FT MOD_RES 378 378 N6-acetyllysine (By similarity).
FT MOD_RES 563 563 Phosphoserine.
FT VAR_SEQ 1 97 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_027947.
FT VAR_SEQ 1 30 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_027948.
FT VAR_SEQ 31 124 LEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAG
FT PPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVT
FT AGIIIVGDEILK -> MQPSSSTPPLHPYSTDGLIFPFNPQ
FT (in isoform 4 and isoform 5).
FT /FTId=VSP_027949.
FT VAR_SEQ 374 437 SSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLH
FT LFHAAVQRKLPDVPNPLQILYIR -> NYLMFQTPSRSCIS
FT AASPLSLSWNSFYRTLSREQAIPENQIASPPSEAKGAEEPW
FT MGPFPGQQG (in isoform 5).
FT /FTId=VSP_027950.
FT VAR_SEQ 374 393 SSLGKKVAGALQTIETSLAQ -> RDLMEEGHYAQSHWWHP
FT RSQ (in isoform 4).
FT /FTId=VSP_027951.
FT VAR_SEQ 394 587 Missing (in isoform 4).
FT /FTId=VSP_027952.
FT VAR_SEQ 438 587 Missing (in isoform 5).
FT /FTId=VSP_027953.
FT VAR_SEQ 544 587 Missing (in isoform 3).
FT /FTId=VSP_027954.
SQ SEQUENCE 587 AA; 65266 MW; F95918B15D9D8106 CRC64;
MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV PSTQDPLFPG
YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS RASELSPGRS VTAGIIIVGD
EILKGHTQDT NTFFLCRTLR SLGVQVCRVS VVPDEVATIA AEVTSFSNRF THVLTAGGIG
PTHDDVTFEA VAQAFGDELK PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP
FRFPLVSVRN VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA
QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS LVPYMPNAVE
QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC VGFNGGKDCT ALLHLFHAAV
QRKLPDVPNP LQILYIRSIS PFPELEQFLQ DTIKRYNLQM LEAEGSMKQA LGELQARHPQ
LEAVLMGTRR TDPYSCSLCP FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY
DRGYTSLGSR ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT
//
MIM
610595
*RECORD*
*FIELD* NO
610595
*FIELD* TI
*610595 FLAVIN ADENINE DINUCLEOTIDE SYNTHETASE, S. CEREVISIAE, HOMOLOG OF;
FLAD1
;;FAD1, S. CEREVISIAE, HOMOLOG OF;;
read moreFAD SYNTHETASE; FADS;;
FMN ADENYLYLTRANSFERASE
*FIELD* TX
DESCRIPTION
FAD synthetase (EC 2.7.7.2) catalyzes the adenylation of flavin
mononucleotide (FMN) into the redox cofactor FAD.
CLONING
Wu et al. (1995) cloned the gene for FAD synthetase, which they
designated Fad1, in S. cerevisiae. By database analysis with yeast Fad1
as query, Brizio et al. (2006) identified the human homolog, FLAD1.
FLAD1 encodes 2 alternatively spliced transcripts, which the authors
named FADS1 and FADS2. FADS1 encodes a 587-amino acid protein with a
predicted molecular mass of 65.3 kD, and FADS2 encodes a 490-amino acid
protein with a predicted molecular mass of 54.2 kD. FADS2 uses a
downstream start codon and thus lacks an N-terminal region present in
FADS1. Analysis using protein prediction programs showed that both FLAD1
isoforms have a predicted cytoplasmic location, although FADS1 also
contains an N-terminal mitochondrial targeting sequence.
GENE FUNCTION
Using spectrophotometric and chromatographic measurements of in vitro
enzymatic assays of recombinant FLAD1 proteins, Brizio et al. (2006)
showed that both FLAD1 isoforms possess MgCl2-dependent FAD synthetase
activity.
MAPPING
By genomic sequence analysis, Brizio et al. (2006) mapped the FLAD1 gene
to chromosome 1.
*FIELD* RF
1. Brizio, C.; Galluccio, M.; Wait, R.; Torchetti, E. M.; Bafunno,
V.; Accardi, R.; Gianazza, E.; Indiveri, C.; Barile, M.: Over-expression
in Escherichia coli and characterization of two recombinant isoforms
of human FAD synthetase. Biochem. Biophys. Res. Commun. 344: 1008-1016,
2006.
2. Wu, M.; Repetto, B.; Glerum, D. M.; Tzagoloff, A.: Cloning and
characterization of FAD1, the structural gene for flavin adenine dinucleotide
synthetase of Saccharomyces cerevisiae. Molec. Cell. Biol. 15: 264-271,
1995.
*FIELD* CD
Laura L. Baxter: 11/22/2006
*FIELD* ED
carol: 11/22/2006
*RECORD*
*FIELD* NO
610595
*FIELD* TI
*610595 FLAVIN ADENINE DINUCLEOTIDE SYNTHETASE, S. CEREVISIAE, HOMOLOG OF;
FLAD1
;;FAD1, S. CEREVISIAE, HOMOLOG OF;;
read moreFAD SYNTHETASE; FADS;;
FMN ADENYLYLTRANSFERASE
*FIELD* TX
DESCRIPTION
FAD synthetase (EC 2.7.7.2) catalyzes the adenylation of flavin
mononucleotide (FMN) into the redox cofactor FAD.
CLONING
Wu et al. (1995) cloned the gene for FAD synthetase, which they
designated Fad1, in S. cerevisiae. By database analysis with yeast Fad1
as query, Brizio et al. (2006) identified the human homolog, FLAD1.
FLAD1 encodes 2 alternatively spliced transcripts, which the authors
named FADS1 and FADS2. FADS1 encodes a 587-amino acid protein with a
predicted molecular mass of 65.3 kD, and FADS2 encodes a 490-amino acid
protein with a predicted molecular mass of 54.2 kD. FADS2 uses a
downstream start codon and thus lacks an N-terminal region present in
FADS1. Analysis using protein prediction programs showed that both FLAD1
isoforms have a predicted cytoplasmic location, although FADS1 also
contains an N-terminal mitochondrial targeting sequence.
GENE FUNCTION
Using spectrophotometric and chromatographic measurements of in vitro
enzymatic assays of recombinant FLAD1 proteins, Brizio et al. (2006)
showed that both FLAD1 isoforms possess MgCl2-dependent FAD synthetase
activity.
MAPPING
By genomic sequence analysis, Brizio et al. (2006) mapped the FLAD1 gene
to chromosome 1.
*FIELD* RF
1. Brizio, C.; Galluccio, M.; Wait, R.; Torchetti, E. M.; Bafunno,
V.; Accardi, R.; Gianazza, E.; Indiveri, C.; Barile, M.: Over-expression
in Escherichia coli and characterization of two recombinant isoforms
of human FAD synthetase. Biochem. Biophys. Res. Commun. 344: 1008-1016,
2006.
2. Wu, M.; Repetto, B.; Glerum, D. M.; Tzagoloff, A.: Cloning and
characterization of FAD1, the structural gene for flavin adenine dinucleotide
synthetase of Saccharomyces cerevisiae. Molec. Cell. Biol. 15: 264-271,
1995.
*FIELD* CD
Laura L. Baxter: 11/22/2006
*FIELD* ED
carol: 11/22/2006