Full text data of SRM
SRM
(SPS1, SRML1)
[Confidence: low (only semi-automatic identification from reviews)]
Spermidine synthase; SPDSY; 2.5.1.16 (Putrescine aminopropyltransferase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Spermidine synthase; SPDSY; 2.5.1.16 (Putrescine aminopropyltransferase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P19623
ID SPEE_HUMAN Reviewed; 302 AA.
AC P19623; B1AKP9; Q15511;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1991, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Spermidine synthase;
DE Short=SPDSY;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase;
GN Name=SRM; Synonyms=SPS1, SRML1;
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].
RX PubMed=2344393; DOI=10.1089/dna.1990.9.103;
RA Wahlfors J., Alhonen L., Kauppinen L., Hyvoenen T., Jaenne J.,
RA Eloranta T.;
RT "Human spermidine synthase: cloning and primary structure.";
RL DNA Cell Biol. 9:103-110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2069720; DOI=10.1089/dna.1991.10.467;
RA Myoehaenen S., Kauppinen L., Wahlfors J., Alhonen L., Jaenne J.;
RT "Human spermidine synthase gene: structure and chromosomal
RT localization.";
RL DNA Cell Biol. 10:467-474(1991).
RN [3]
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEXES WITH SPERMIDINE;
RP PUTRESCINE; MTA AND S-ADENOSYLMETHIONINAMINE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17585781; DOI=10.1021/bi602498k;
RA Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E.,
RA Plotnikov A.N.;
RT "Structure and mechanism of spermidine synthases.";
RL Biochemistry 46:8331-8339(2007).
CC -!- FUNCTION: Catalyzes the production of spermidine from putrescine
CC and decarboxylated S-adenosylmethionine (dcSAM). Has a strong
CC preference for putrescine as substrate, and has very low activity
CC towards 1,3-diaminopropane. Has extremely low activity towards
CC spermidine.
CC -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
CC putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
CC -!- ENZYME REGULATION: The activity is thought to be regulated mainly
CC by the availability of decarboxylated S-adenosylmethionine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for putrescine;
CC KM=0.9 uM for S-adenosylmethioninamine;
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine
CC biosynthesis; spermidine from putrescine: step 1/1.
CC -!- SUBUNIT: Homodimer or homotetramer.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC -!- SIMILARITY: Contains 1 PABS (polyamine biosynthesis) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M34338; AAA36633.1; -; mRNA.
DR EMBL; M64231; AAA60574.1; -; Genomic_DNA.
DR EMBL; AL109811; CAI22104.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71675.1; -; Genomic_DNA.
DR EMBL; BC000309; AAH00309.1; -; mRNA.
DR EMBL; BC033106; AAH33106.1; -; mRNA.
DR PIR; A32610; A32610.
DR RefSeq; NP_003123.2; NM_003132.2.
DR UniGene; Hs.76244; -.
DR PDB; 2O05; X-ray; 2.00 A; A/B=1-302.
DR PDB; 2O06; X-ray; 2.00 A; A/B=1-302.
DR PDB; 2O07; X-ray; 1.89 A; A/B=1-302.
DR PDB; 2O0L; X-ray; 1.99 A; A/B=1-302.
DR PDB; 3RW9; X-ray; 2.00 A; A/B=1-302.
DR PDBsum; 2O05; -.
DR PDBsum; 2O06; -.
DR PDBsum; 2O07; -.
DR PDBsum; 2O0L; -.
DR PDBsum; 3RW9; -.
DR ProteinModelPortal; P19623; -.
DR SMR; P19623; 15-299.
DR IntAct; P19623; 4.
DR STRING; 9606.ENSP00000366156; -.
DR BindingDB; P19623; -.
DR ChEMBL; CHEMBL4232; -.
DR DrugBank; DB00118; S-Adenosylmethionine.
DR DrugBank; DB00127; Spermine.
DR PhosphoSite; P19623; -.
DR DMDM; 134811; -.
DR PaxDb; P19623; -.
DR PeptideAtlas; P19623; -.
DR PRIDE; P19623; -.
DR DNASU; 6723; -.
DR Ensembl; ENST00000376957; ENSP00000366156; ENSG00000116649.
DR GeneID; 6723; -.
DR KEGG; hsa:6723; -.
DR UCSC; uc001arz.1; human.
DR CTD; 6723; -.
DR GeneCards; GC01M011114; -.
DR HGNC; HGNC:11296; SRM.
DR HPA; HPA015746; -.
DR HPA; HPA029528; -.
DR MIM; 182891; gene.
DR neXtProt; NX_P19623; -.
DR PharmGKB; PA36120; -.
DR eggNOG; COG0421; -.
DR HOGENOM; HOG000256147; -.
DR HOVERGEN; HBG000834; -.
DR InParanoid; P19623; -.
DR KO; K00797; -.
DR OMA; ELWYTEK; -.
DR OrthoDB; EOG78D7KS; -.
DR PhylomeDB; P19623; -.
DR BioCyc; MetaCyc:HS04027-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P19623; -.
DR UniPathway; UPA00248; UER00314.
DR ChiTaRS; SRM; human.
DR EvolutionaryTrace; P19623; -.
DR GenomeRNAi; 6723; -.
DR NextBio; 26226; -.
DR PRO; PR:P19623; -.
DR ArrayExpress; P19623; -.
DR Bgee; P19623; -.
DR CleanEx; HS_SRM; -.
DR Genevestigator; P19623; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004766; F:spermidine synthase activity; IDA:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR001045; Spermidine/spermine_synthase.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Polyamine biosynthesis;
KW Polymorphism; Reference proteome; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1 302 Spermidine synthase.
FT /FTId=PRO_0000156445.
FT DOMAIN 18 253 PABS.
FT REGION 155 156 S-adenosylmethioninamine binding.
FT REGION 173 176 Putrescine binding.
FT ACT_SITE 173 173 Proton acceptor (By similarity).
FT BINDING 49 49 S-adenosylmethioninamine.
FT BINDING 79 79 Putrescine.
FT BINDING 80 80 S-adenosylmethioninamine.
FT BINDING 104 104 S-adenosylmethioninamine.
FT BINDING 124 124 S-adenosylmethioninamine.
FT BINDING 173 173 S-adenosylmethioninamine.
FT BINDING 241 241 Putrescine.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 149 149 L -> V (in dbSNP:rs1049932).
FT /FTId=VAR_011807.
FT CONFLICT 210 210 Q -> E (in Ref. 1; AAA36633).
FT STRAND 20 23
FT STRAND 31 45
FT STRAND 47 59
FT STRAND 61 65
FT STRAND 68 72
FT TURN 73 76
FT HELIX 77 88
FT STRAND 91 93
FT STRAND 96 101
FT HELIX 106 111
FT STRAND 119 125
FT HELIX 127 136
FT HELIX 138 141
FT HELIX 142 145
FT STRAND 149 154
FT HELIX 156 161
FT STRAND 167 173
FT TURN 177 179
FT HELIX 180 185
FT HELIX 188 196
FT STRAND 197 208
FT TURN 210 212
FT HELIX 214 227
FT STRAND 229 237
FT HELIX 242 244
FT STRAND 245 254
FT STRAND 259 261
FT HELIX 268 273
FT HELIX 281 286
FT HELIX 292 299
SQ SEQUENCE 302 AA; 33825 MW; 3EF454D886F6425D CRC64;
MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG
NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV
VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP
AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT
YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND
VS
//
ID SPEE_HUMAN Reviewed; 302 AA.
AC P19623; B1AKP9; Q15511;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1991, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Spermidine synthase;
DE Short=SPDSY;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase;
GN Name=SRM; Synonyms=SPS1, SRML1;
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].
RX PubMed=2344393; DOI=10.1089/dna.1990.9.103;
RA Wahlfors J., Alhonen L., Kauppinen L., Hyvoenen T., Jaenne J.,
RA Eloranta T.;
RT "Human spermidine synthase: cloning and primary structure.";
RL DNA Cell Biol. 9:103-110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2069720; DOI=10.1089/dna.1991.10.467;
RA Myoehaenen S., Kauppinen L., Wahlfors J., Alhonen L., Jaenne J.;
RT "Human spermidine synthase gene: structure and chromosomal
RT localization.";
RL DNA Cell Biol. 10:467-474(1991).
RN [3]
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEXES WITH SPERMIDINE;
RP PUTRESCINE; MTA AND S-ADENOSYLMETHIONINAMINE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17585781; DOI=10.1021/bi602498k;
RA Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E.,
RA Plotnikov A.N.;
RT "Structure and mechanism of spermidine synthases.";
RL Biochemistry 46:8331-8339(2007).
CC -!- FUNCTION: Catalyzes the production of spermidine from putrescine
CC and decarboxylated S-adenosylmethionine (dcSAM). Has a strong
CC preference for putrescine as substrate, and has very low activity
CC towards 1,3-diaminopropane. Has extremely low activity towards
CC spermidine.
CC -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
CC putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
CC -!- ENZYME REGULATION: The activity is thought to be regulated mainly
CC by the availability of decarboxylated S-adenosylmethionine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for putrescine;
CC KM=0.9 uM for S-adenosylmethioninamine;
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine
CC biosynthesis; spermidine from putrescine: step 1/1.
CC -!- SUBUNIT: Homodimer or homotetramer.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC -!- SIMILARITY: Contains 1 PABS (polyamine biosynthesis) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M34338; AAA36633.1; -; mRNA.
DR EMBL; M64231; AAA60574.1; -; Genomic_DNA.
DR EMBL; AL109811; CAI22104.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71675.1; -; Genomic_DNA.
DR EMBL; BC000309; AAH00309.1; -; mRNA.
DR EMBL; BC033106; AAH33106.1; -; mRNA.
DR PIR; A32610; A32610.
DR RefSeq; NP_003123.2; NM_003132.2.
DR UniGene; Hs.76244; -.
DR PDB; 2O05; X-ray; 2.00 A; A/B=1-302.
DR PDB; 2O06; X-ray; 2.00 A; A/B=1-302.
DR PDB; 2O07; X-ray; 1.89 A; A/B=1-302.
DR PDB; 2O0L; X-ray; 1.99 A; A/B=1-302.
DR PDB; 3RW9; X-ray; 2.00 A; A/B=1-302.
DR PDBsum; 2O05; -.
DR PDBsum; 2O06; -.
DR PDBsum; 2O07; -.
DR PDBsum; 2O0L; -.
DR PDBsum; 3RW9; -.
DR ProteinModelPortal; P19623; -.
DR SMR; P19623; 15-299.
DR IntAct; P19623; 4.
DR STRING; 9606.ENSP00000366156; -.
DR BindingDB; P19623; -.
DR ChEMBL; CHEMBL4232; -.
DR DrugBank; DB00118; S-Adenosylmethionine.
DR DrugBank; DB00127; Spermine.
DR PhosphoSite; P19623; -.
DR DMDM; 134811; -.
DR PaxDb; P19623; -.
DR PeptideAtlas; P19623; -.
DR PRIDE; P19623; -.
DR DNASU; 6723; -.
DR Ensembl; ENST00000376957; ENSP00000366156; ENSG00000116649.
DR GeneID; 6723; -.
DR KEGG; hsa:6723; -.
DR UCSC; uc001arz.1; human.
DR CTD; 6723; -.
DR GeneCards; GC01M011114; -.
DR HGNC; HGNC:11296; SRM.
DR HPA; HPA015746; -.
DR HPA; HPA029528; -.
DR MIM; 182891; gene.
DR neXtProt; NX_P19623; -.
DR PharmGKB; PA36120; -.
DR eggNOG; COG0421; -.
DR HOGENOM; HOG000256147; -.
DR HOVERGEN; HBG000834; -.
DR InParanoid; P19623; -.
DR KO; K00797; -.
DR OMA; ELWYTEK; -.
DR OrthoDB; EOG78D7KS; -.
DR PhylomeDB; P19623; -.
DR BioCyc; MetaCyc:HS04027-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P19623; -.
DR UniPathway; UPA00248; UER00314.
DR ChiTaRS; SRM; human.
DR EvolutionaryTrace; P19623; -.
DR GenomeRNAi; 6723; -.
DR NextBio; 26226; -.
DR PRO; PR:P19623; -.
DR ArrayExpress; P19623; -.
DR Bgee; P19623; -.
DR CleanEx; HS_SRM; -.
DR Genevestigator; P19623; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004766; F:spermidine synthase activity; IDA:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR001045; Spermidine/spermine_synthase.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Polyamine biosynthesis;
KW Polymorphism; Reference proteome; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1 302 Spermidine synthase.
FT /FTId=PRO_0000156445.
FT DOMAIN 18 253 PABS.
FT REGION 155 156 S-adenosylmethioninamine binding.
FT REGION 173 176 Putrescine binding.
FT ACT_SITE 173 173 Proton acceptor (By similarity).
FT BINDING 49 49 S-adenosylmethioninamine.
FT BINDING 79 79 Putrescine.
FT BINDING 80 80 S-adenosylmethioninamine.
FT BINDING 104 104 S-adenosylmethioninamine.
FT BINDING 124 124 S-adenosylmethioninamine.
FT BINDING 173 173 S-adenosylmethioninamine.
FT BINDING 241 241 Putrescine.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 149 149 L -> V (in dbSNP:rs1049932).
FT /FTId=VAR_011807.
FT CONFLICT 210 210 Q -> E (in Ref. 1; AAA36633).
FT STRAND 20 23
FT STRAND 31 45
FT STRAND 47 59
FT STRAND 61 65
FT STRAND 68 72
FT TURN 73 76
FT HELIX 77 88
FT STRAND 91 93
FT STRAND 96 101
FT HELIX 106 111
FT STRAND 119 125
FT HELIX 127 136
FT HELIX 138 141
FT HELIX 142 145
FT STRAND 149 154
FT HELIX 156 161
FT STRAND 167 173
FT TURN 177 179
FT HELIX 180 185
FT HELIX 188 196
FT STRAND 197 208
FT TURN 210 212
FT HELIX 214 227
FT STRAND 229 237
FT HELIX 242 244
FT STRAND 245 254
FT STRAND 259 261
FT HELIX 268 273
FT HELIX 281 286
FT HELIX 292 299
SQ SEQUENCE 302 AA; 33825 MW; 3EF454D886F6425D CRC64;
MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG
NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV
VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP
AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT
YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND
VS
//
MIM
182891
*RECORD*
*FIELD* NO
182891
*FIELD* TI
*182891 SPERMIDINE SYNTHASE; SRM
;;SPS1
*FIELD* TX
CLONING
The biosynthesis of polyamines, which are universally essential for
read morecellular functions, takes place from arginine and methionine and
involves 4 distinct enzymes: spermidine synthase (EC 2.5.1.16),
ornithine decarboxylase (165640), S-adenosyl-L-methionine decarboxylase
(180980), and spermine synthase (300105). Wahlfors et al. (1990) cloned
a cDNA coding for the full-length subunit of spermidine synthase, using
a synthetic deoxyoligonucleotide mixture corresponding to a tryptic
peptide of the bovine enzyme and a human decidual cDNA library. An open
reading frame for a 302-amino acid polypeptide was found.
GENE STRUCTURE
Myohanen et al. (1991) isolated the SRM gene from a genomic library and
showed that it comprises 5,818 nucleotides from the cap site to the last
A of the putative polyadenylation signal with 8 exons.
MAPPING
Using Southern blot analysis of panels of human/rodent somatic cell
hybrids and chromosomal in situ hybridization, Winqvist et al. (1991)
assigned spermidine synthase DNA sequences to 1p36-p22 and 3p14-q21. As
determined from the intensity of the hybridization signal observed in
analysis of DNA from somatic cell hybrids, it seemed likely that the
functional gene is located at the former site.
By PCR analysis of DNA obtained from human/hamster somatic cell hybrids,
Myohanen et al. (1991) mapped the SRM gene to chromosome 1.
*FIELD* RF
1. Myohanen, S.; Kauppinen, L.; Wahlfors, J.; Alhonen, L.; Janne,
J.: Human spermidine synthase gene: structure and chromosomal localization. DNA
Cell Biol. 10: 467-474, 1991.
2. Wahlfors, J.; Alhonen, L.; Kauppinen, L.; Hyvonen, T.; Janne, J.;
Eloranta, T. O.: Human spermidine synthase: cloning and primary structure. DNA
Cell Biol. 9: 103-110, 1990. Note: Erratum: DNA Cell Biol. 9: 543
only, 1990.
3. Winqvist, R.; Alanen, L.; Grzeschik, K.-H.; Janne, J.; Eloranta,
T.: Mapping of DNA sequences for spermidine synthase to human chromosome
1p36-p22 and chromosome 3p14-q21. (Abstract) Cytogenet. Cell Genet. 58:
1865 only, 1991.
*FIELD* CD
Victor A. McKusick: 6/11/1990
*FIELD* ED
carol: 12/17/2012
dkim: 9/11/1998
mark: 11/6/1997
supermim: 3/16/1992
carol: 2/23/1992
carol: 12/12/1991
carol: 11/6/1991
carol: 8/6/1991
carol: 6/11/1990
*RECORD*
*FIELD* NO
182891
*FIELD* TI
*182891 SPERMIDINE SYNTHASE; SRM
;;SPS1
*FIELD* TX
CLONING
The biosynthesis of polyamines, which are universally essential for
read morecellular functions, takes place from arginine and methionine and
involves 4 distinct enzymes: spermidine synthase (EC 2.5.1.16),
ornithine decarboxylase (165640), S-adenosyl-L-methionine decarboxylase
(180980), and spermine synthase (300105). Wahlfors et al. (1990) cloned
a cDNA coding for the full-length subunit of spermidine synthase, using
a synthetic deoxyoligonucleotide mixture corresponding to a tryptic
peptide of the bovine enzyme and a human decidual cDNA library. An open
reading frame for a 302-amino acid polypeptide was found.
GENE STRUCTURE
Myohanen et al. (1991) isolated the SRM gene from a genomic library and
showed that it comprises 5,818 nucleotides from the cap site to the last
A of the putative polyadenylation signal with 8 exons.
MAPPING
Using Southern blot analysis of panels of human/rodent somatic cell
hybrids and chromosomal in situ hybridization, Winqvist et al. (1991)
assigned spermidine synthase DNA sequences to 1p36-p22 and 3p14-q21. As
determined from the intensity of the hybridization signal observed in
analysis of DNA from somatic cell hybrids, it seemed likely that the
functional gene is located at the former site.
By PCR analysis of DNA obtained from human/hamster somatic cell hybrids,
Myohanen et al. (1991) mapped the SRM gene to chromosome 1.
*FIELD* RF
1. Myohanen, S.; Kauppinen, L.; Wahlfors, J.; Alhonen, L.; Janne,
J.: Human spermidine synthase gene: structure and chromosomal localization. DNA
Cell Biol. 10: 467-474, 1991.
2. Wahlfors, J.; Alhonen, L.; Kauppinen, L.; Hyvonen, T.; Janne, J.;
Eloranta, T. O.: Human spermidine synthase: cloning and primary structure. DNA
Cell Biol. 9: 103-110, 1990. Note: Erratum: DNA Cell Biol. 9: 543
only, 1990.
3. Winqvist, R.; Alanen, L.; Grzeschik, K.-H.; Janne, J.; Eloranta,
T.: Mapping of DNA sequences for spermidine synthase to human chromosome
1p36-p22 and chromosome 3p14-q21. (Abstract) Cytogenet. Cell Genet. 58:
1865 only, 1991.
*FIELD* CD
Victor A. McKusick: 6/11/1990
*FIELD* ED
carol: 12/17/2012
dkim: 9/11/1998
mark: 11/6/1997
supermim: 3/16/1992
carol: 2/23/1992
carol: 12/12/1991
carol: 11/6/1991
carol: 8/6/1991
carol: 6/11/1990