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Enolase-phosphatase E1 (EC 3 1 3 77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (MASA homolog)

 ENOPH_HUMAN             Reviewed;         261 AA.
Q9UHY7; Q7Z4C5; Q9BVC2;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
26-FEB-2020, entry version 161.
RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03117};
EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_03117};
AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_03117};
AltName: Full=MASA homolog {ECO:0000255|HAMAP-Rule:MF_03117};
Name=ENOPH1 {ECO:0000255|HAMAP-Rule:MF_03117};
Synonyms=MASA {ECO:0000255|HAMAP-Rule:MF_03117}; ORFNames=MSTP145;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hypothalamus;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 72-261 (ISOFORM 1).
TISSUE=Aorta;
Qin B.M., Sheng H., Liu B., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
SUBSTRATE ANALOG, FUNCTION, AND SUBUNIT.
PubMed=15843022; DOI=10.1016/j.jmb.2005.01.072;
Wang H., Pang H., Bartlam M., Rao Z.;
"Crystal structure of human E1 enzyme and its complex with a substrate
analog reveals the mechanism of its phosphatase/enolase activity.";
J. Mol. Biol. 348:917-926(2005).
-!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-
diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-
MTPenyl-1-P), which is then dephosphorylated to form the acireductone
1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
{ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:15843022}.
-!- CATALYTIC ACTIVITY:
Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
Evidence={ECO:0000255|HAMAP-Rule:MF_03117};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per subunit.;
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
step 3/6. {ECO:0000255|HAMAP-Rule:MF_03117}.
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
step 4/6. {ECO:0000255|HAMAP-Rule:MF_03117}.
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03117,
ECO:0000269|PubMed:15843022}.
-!- INTERACTION:
Q9H4P4:RNF41; NbExp=5; IntAct=EBI-726969, EBI-2130266;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}.
Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UHY7-1; Sequence=Displayed;
Name=2;
IsoId=Q9UHY7-2; Sequence=VSP_021160;
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
family. {ECO:0000255|HAMAP-Rule:MF_03117}.
-!- SEQUENCE CAUTION:
Sequence=AAQ13671.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AF113125; AAF14866.1; -; mRNA.
EMBL; AK022656; BAB14160.1; -; mRNA.
EMBL; CR457141; CAG33422.1; -; mRNA.
EMBL; BC001317; AAH01317.1; -; mRNA.
EMBL; BC065815; AAH65815.1; -; mRNA.
EMBL; AF177286; AAQ13671.1; ALT_SEQ; mRNA.
CCDS; CCDS3594.1; -. [Q9UHY7-1]
RefSeq; NP_001278946.1; NM_001292017.1.
RefSeq; NP_067027.1; NM_021204.4. [Q9UHY7-1]
PDB; 1YNS; X-ray; 1.70 A; A=1-261.
PDB; 1ZS9; X-ray; 1.70 A; A=1-261.
PDBsum; 1YNS; -.
PDBsum; 1ZS9; -.
SMR; Q9UHY7; -.
BioGrid; 121811; 27.
IntAct; Q9UHY7; 15.
MINT; Q9UHY7; -.
STRING; 9606.ENSP00000273920; -.
DrugBank; DB07912; 2-OXOHEPTYLPHOSPHONIC ACID.
DEPOD; Q9UHY7; -.
iPTMnet; Q9UHY7; -.
PhosphoSitePlus; Q9UHY7; -.
BioMuta; ENOPH1; -.
DMDM; 74735024; -.
EPD; Q9UHY7; -.
jPOST; Q9UHY7; -.
MassIVE; Q9UHY7; -.
PaxDb; Q9UHY7; -.
PeptideAtlas; Q9UHY7; -.
PRIDE; Q9UHY7; -.
ProteomicsDB; 84440; -. [Q9UHY7-1]
ProteomicsDB; 84441; -. [Q9UHY7-2]
Ensembl; ENST00000273920; ENSP00000273920; ENSG00000145293. [Q9UHY7-1]
Ensembl; ENST00000505846; ENSP00000427209; ENSG00000145293. [Q9UHY7-2]
GeneID; 58478; -.
KEGG; hsa:58478; -.
UCSC; uc003hmv.4; human. [Q9UHY7-1]
CTD; 58478; -.
DisGeNET; 58478; -.
GeneCards; ENOPH1; -.
HGNC; HGNC:24599; ENOPH1.
HPA; CAB004985; -.
HPA; HPA044607; -.
neXtProt; NX_Q9UHY7; -.
OpenTargets; ENSG00000145293; -.
PharmGKB; PA162385052; -.
eggNOG; KOG2630; Eukaryota.
eggNOG; COG4229; LUCA.
GeneTree; ENSGT00440000039914; -.
HOGENOM; CLU_023273_0_0_1; -.
InParanoid; Q9UHY7; -.
KO; K09880; -.
OMA; NRACPVH; -.
OrthoDB; 1475361at2759; -.
PhylomeDB; Q9UHY7; -.
TreeFam; TF105939; -.
BRENDA; 3.1.3.77; 2681.
Reactome; R-HSA-1237112; Methionine salvage pathway.
UniPathway; UPA00904; UER00876.
UniPathway; UPA00904; UER00877.
ChiTaRS; ENOPH1; human.
EvolutionaryTrace; Q9UHY7; -.
GenomeRNAi; 58478; -.
Pharos; Q9UHY7; Tbio.
PRO; PR:Q9UHY7; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; Q9UHY7; protein.
Bgee; ENSG00000145293; Expressed in C1 segment of cervical spinal cord and 224 other tissues.
ExpressionAtlas; Q9UHY7; baseline and differential.
Genevisible; Q9UHY7; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
GO; GO:0043874; F:acireductone synthase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:UniProtKB.
GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
CDD; cd01629; HAD_EP; 1.
Gene3D; 3.40.50.1000; -; 1.
HAMAP; MF_01681; Salvage_MtnC; 1.
HAMAP; MF_03117; Salvage_MtnC_euk; 1.
InterPro; IPR023943; Enolase-ppase_E1.
InterPro; IPR027511; ENOPH1_eukaryotes.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006439; HAD-SF_hydro_IA.
InterPro; IPR023214; HAD_sf.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01691; enolase-ppase; 1.
TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis; Cytoplasm;
Hydrolase; Magnesium; Metal-binding; Methionine biosynthesis; Nucleus;
Reference proteome.
CHAIN 1..261
/note="Enolase-phosphatase E1"
/id="PRO_0000254007"
REGION 153..154
/note="Substrate binding"
METAL 16
/note="Magnesium"
/evidence="ECO:0000255|HAMAP-Rule:MF_03117,
ECO:0000269|PubMed:15843022"
METAL 18
/note="Magnesium; via carbonyl oxygen"
/evidence="ECO:0000255|HAMAP-Rule:MF_03117,
ECO:0000269|PubMed:15843022"
METAL 212
/note="Magnesium"
/evidence="ECO:0000255|HAMAP-Rule:MF_03117,
ECO:0000269|PubMed:15843022"
BINDING 187
/note="Substrate"
VAR_SEQ 1..146
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_021160"
STRAND 12..15
/evidence="ECO:0000244|PDB:1YNS"
TURN 19..21
/evidence="ECO:0000244|PDB:1YNS"
HELIX 24..29
/evidence="ECO:0000244|PDB:1YNS"
HELIX 31..46
/evidence="ECO:0000244|PDB:1YNS"
HELIX 50..65
/evidence="ECO:0000244|PDB:1YNS"
TURN 66..68
/evidence="ECO:0000244|PDB:1YNS"
HELIX 83..103
/evidence="ECO:0000244|PDB:1YNS"
HELIX 108..123
/evidence="ECO:0000244|PDB:1YNS"
HELIX 135..144
/evidence="ECO:0000244|PDB:1YNS"
STRAND 148..152
/evidence="ECO:0000244|PDB:1YNS"
HELIX 157..165
/evidence="ECO:0000244|PDB:1YNS"
HELIX 173..175
/evidence="ECO:0000244|PDB:1YNS"
STRAND 177..180
/evidence="ECO:0000244|PDB:1YNS"
HELIX 182..184
/evidence="ECO:0000244|PDB:1YNS"
HELIX 190..200
/evidence="ECO:0000244|PDB:1YNS"
HELIX 204..206
/evidence="ECO:0000244|PDB:1YNS"
STRAND 207..212
/evidence="ECO:0000244|PDB:1YNS"
HELIX 214..222
/evidence="ECO:0000244|PDB:1YNS"
STRAND 226..230
/evidence="ECO:0000244|PDB:1YNS"
HELIX 240..245
/evidence="ECO:0000244|PDB:1YNS"
STRAND 248..251
/evidence="ECO:0000244|PDB:1YNS"
HELIX 252..254
/evidence="ECO:0000244|PDB:1YNS"
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


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