Full text data of ENOPH1
ENOPH1
(MASA)
[Confidence: low (only semi-automatic identification from reviews)]
Enolase-phosphatase E1; 3.1.3.77 (2,3-diketo-5-methylthio-1-phosphopentane phosphatase; MASA homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Enolase-phosphatase E1; 3.1.3.77 (2,3-diketo-5-methylthio-1-phosphopentane phosphatase; MASA homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UHY7
ID ENOPH_HUMAN Reviewed; 261 AA.
AC Q9UHY7; Q7Z4C5; Q9BVC2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Enolase-phosphatase E1;
DE EC=3.1.3.77;
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
DE AltName: Full=MASA homolog;
GN Name=ENOPH1; Synonyms=MASA; ORFNames=MSTP145;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 72-261 (ISOFORM 1).
RC TISSUE=Aorta;
RA Qin B.M., Sheng H., Liu B., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
RA Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP SUBSTRATE ANALOG, FUNCTION, AND SUBUNIT.
RX PubMed=15843022; DOI=10.1016/j.jmb.2005.01.072;
RA Wang H., Pang H., Bartlam M., Rao Z.;
RT "Crystal structure of human E1 enzyme and its complex with a substrate
RT analog reveals the mechanism of its phosphatase/enolase activity.";
RL J. Mol. Biol. 348:917-926(2005).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of
CC 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
CC (HK-MTPenyl-1-P), which is then dephosphorylated to form the
CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-
CC MTPene).
CC -!- CATALYTIC ACTIVITY: 5-(methylthio)-2,3-dioxopentyl phosphate +
CC H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC 1-phosphate: step 3/6.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC 1-phosphate: step 4/6.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHY7-2; Sequence=VSP_021160;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC MasA/MtnC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13671.1; Type=Frameshift; Positions=235;
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; AF113125; AAF14866.1; -; mRNA.
DR EMBL; AK022656; BAB14160.1; -; mRNA.
DR EMBL; CR457141; CAG33422.1; -; mRNA.
DR EMBL; BC001317; AAH01317.1; -; mRNA.
DR EMBL; BC065815; AAH65815.1; -; mRNA.
DR EMBL; AF177286; AAQ13671.1; ALT_SEQ; mRNA.
DR RefSeq; NP_067027.1; NM_021204.3.
DR UniGene; Hs.18442; -.
DR PDB; 1YNS; X-ray; 1.70 A; A=1-261.
DR PDB; 1ZS9; X-ray; 1.70 A; A=1-261.
DR PDBsum; 1YNS; -.
DR PDBsum; 1ZS9; -.
DR ProteinModelPortal; Q9UHY7; -.
DR SMR; Q9UHY7; 4-257.
DR IntAct; Q9UHY7; 2.
DR MINT; MINT-1415620; -.
DR STRING; 9606.ENSP00000273920; -.
DR DMDM; 74735024; -.
DR PaxDb; Q9UHY7; -.
DR PRIDE; Q9UHY7; -.
DR Ensembl; ENST00000273920; ENSP00000273920; ENSG00000145293.
DR Ensembl; ENST00000505846; ENSP00000427209; ENSG00000145293.
DR GeneID; 58478; -.
DR KEGG; hsa:58478; -.
DR UCSC; uc003hmv.3; human.
DR CTD; 58478; -.
DR GeneCards; GC04P083351; -.
DR HGNC; HGNC:24599; ENOPH1.
DR HPA; CAB004985; -.
DR HPA; HPA044607; -.
DR neXtProt; NX_Q9UHY7; -.
DR PharmGKB; PA162385052; -.
DR eggNOG; COG4229; -.
DR HOGENOM; HOG000237286; -.
DR HOVERGEN; HBG054539; -.
DR InParanoid; Q9UHY7; -.
DR KO; K09880; -.
DR OMA; DTHVGHK; -.
DR OrthoDB; EOG7BP83J; -.
DR PhylomeDB; Q9UHY7; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR EvolutionaryTrace; Q9UHY7; -.
DR GenomeRNAi; 58478; -.
DR NextBio; 64922; -.
DR PRO; PR:Q9UHY7; -.
DR ArrayExpress; Q9UHY7; -.
DR Bgee; Q9UHY7; -.
DR CleanEx; HS_ENOPH1; -.
DR Genevestigator; Q9UHY7; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043874; F:acireductone synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:UniProtKB.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_03117; Salvage_MtnC_euk; 1; -.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR027511; ENOPH1_eukaryotes.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis;
KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Nucleus; Reference proteome.
FT CHAIN 1 261 Enolase-phosphatase E1.
FT /FTId=PRO_0000254007.
FT REGION 153 154 Substrate binding.
FT METAL 16 16 Magnesium.
FT METAL 18 18 Magnesium; via carbonyl oxygen.
FT METAL 212 212 Magnesium.
FT BINDING 187 187 Substrate.
FT VAR_SEQ 1 146 Missing (in isoform 2).
FT /FTId=VSP_021160.
FT STRAND 12 15
FT TURN 19 21
FT HELIX 24 29
FT HELIX 31 46
FT HELIX 50 65
FT TURN 66 68
FT HELIX 83 103
FT HELIX 108 123
FT HELIX 135 144
FT STRAND 148 152
FT HELIX 157 165
FT HELIX 173 175
FT STRAND 177 180
FT HELIX 182 184
FT HELIX 190 200
FT HELIX 204 206
FT STRAND 207 212
FT HELIX 214 222
FT STRAND 226 230
FT HELIX 240 245
FT STRAND 248 251
FT HELIX 252 254
SQ SEQUENCE 261 AA; 28933 MW; 12B3F73463907E2C CRC64;
MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR
KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA
AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF
DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD
DEKTYYSLIT SFSELYLPSS T
//
ID ENOPH_HUMAN Reviewed; 261 AA.
AC Q9UHY7; Q7Z4C5; Q9BVC2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Enolase-phosphatase E1;
DE EC=3.1.3.77;
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
DE AltName: Full=MASA homolog;
GN Name=ENOPH1; Synonyms=MASA; ORFNames=MSTP145;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 72-261 (ISOFORM 1).
RC TISSUE=Aorta;
RA Qin B.M., Sheng H., Liu B., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
RA Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP SUBSTRATE ANALOG, FUNCTION, AND SUBUNIT.
RX PubMed=15843022; DOI=10.1016/j.jmb.2005.01.072;
RA Wang H., Pang H., Bartlam M., Rao Z.;
RT "Crystal structure of human E1 enzyme and its complex with a substrate
RT analog reveals the mechanism of its phosphatase/enolase activity.";
RL J. Mol. Biol. 348:917-926(2005).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of
CC 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
CC (HK-MTPenyl-1-P), which is then dephosphorylated to form the
CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-
CC MTPene).
CC -!- CATALYTIC ACTIVITY: 5-(methylthio)-2,3-dioxopentyl phosphate +
CC H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC 1-phosphate: step 3/6.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC 1-phosphate: step 4/6.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHY7-2; Sequence=VSP_021160;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC MasA/MtnC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13671.1; Type=Frameshift; Positions=235;
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; AF113125; AAF14866.1; -; mRNA.
DR EMBL; AK022656; BAB14160.1; -; mRNA.
DR EMBL; CR457141; CAG33422.1; -; mRNA.
DR EMBL; BC001317; AAH01317.1; -; mRNA.
DR EMBL; BC065815; AAH65815.1; -; mRNA.
DR EMBL; AF177286; AAQ13671.1; ALT_SEQ; mRNA.
DR RefSeq; NP_067027.1; NM_021204.3.
DR UniGene; Hs.18442; -.
DR PDB; 1YNS; X-ray; 1.70 A; A=1-261.
DR PDB; 1ZS9; X-ray; 1.70 A; A=1-261.
DR PDBsum; 1YNS; -.
DR PDBsum; 1ZS9; -.
DR ProteinModelPortal; Q9UHY7; -.
DR SMR; Q9UHY7; 4-257.
DR IntAct; Q9UHY7; 2.
DR MINT; MINT-1415620; -.
DR STRING; 9606.ENSP00000273920; -.
DR DMDM; 74735024; -.
DR PaxDb; Q9UHY7; -.
DR PRIDE; Q9UHY7; -.
DR Ensembl; ENST00000273920; ENSP00000273920; ENSG00000145293.
DR Ensembl; ENST00000505846; ENSP00000427209; ENSG00000145293.
DR GeneID; 58478; -.
DR KEGG; hsa:58478; -.
DR UCSC; uc003hmv.3; human.
DR CTD; 58478; -.
DR GeneCards; GC04P083351; -.
DR HGNC; HGNC:24599; ENOPH1.
DR HPA; CAB004985; -.
DR HPA; HPA044607; -.
DR neXtProt; NX_Q9UHY7; -.
DR PharmGKB; PA162385052; -.
DR eggNOG; COG4229; -.
DR HOGENOM; HOG000237286; -.
DR HOVERGEN; HBG054539; -.
DR InParanoid; Q9UHY7; -.
DR KO; K09880; -.
DR OMA; DTHVGHK; -.
DR OrthoDB; EOG7BP83J; -.
DR PhylomeDB; Q9UHY7; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR EvolutionaryTrace; Q9UHY7; -.
DR GenomeRNAi; 58478; -.
DR NextBio; 64922; -.
DR PRO; PR:Q9UHY7; -.
DR ArrayExpress; Q9UHY7; -.
DR Bgee; Q9UHY7; -.
DR CleanEx; HS_ENOPH1; -.
DR Genevestigator; Q9UHY7; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043874; F:acireductone synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:UniProtKB.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_03117; Salvage_MtnC_euk; 1; -.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR027511; ENOPH1_eukaryotes.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis;
KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Nucleus; Reference proteome.
FT CHAIN 1 261 Enolase-phosphatase E1.
FT /FTId=PRO_0000254007.
FT REGION 153 154 Substrate binding.
FT METAL 16 16 Magnesium.
FT METAL 18 18 Magnesium; via carbonyl oxygen.
FT METAL 212 212 Magnesium.
FT BINDING 187 187 Substrate.
FT VAR_SEQ 1 146 Missing (in isoform 2).
FT /FTId=VSP_021160.
FT STRAND 12 15
FT TURN 19 21
FT HELIX 24 29
FT HELIX 31 46
FT HELIX 50 65
FT TURN 66 68
FT HELIX 83 103
FT HELIX 108 123
FT HELIX 135 144
FT STRAND 148 152
FT HELIX 157 165
FT HELIX 173 175
FT STRAND 177 180
FT HELIX 182 184
FT HELIX 190 200
FT HELIX 204 206
FT STRAND 207 212
FT HELIX 214 222
FT STRAND 226 230
FT HELIX 240 245
FT STRAND 248 251
FT HELIX 252 254
SQ SEQUENCE 261 AA; 28933 MW; 12B3F73463907E2C CRC64;
MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR
KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA
AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF
DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD
DEKTYYSLIT SFSELYLPSS T
//