ENOPH_HUMAN
ID ENOPH_HUMAN Reviewed; 261 AA.
AC Q9UHY7; Q7Z4C5; Q9BVC2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03117};
DE EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_03117};
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_03117};
DE AltName: Full=MASA homolog {ECO:0000255|HAMAP-Rule:MF_03117};
GN Name=ENOPH1 {ECO:0000255|HAMAP-Rule:MF_03117};
GN Synonyms=MASA {ECO:0000255|HAMAP-Rule:MF_03117}; ORFNames=MSTP145;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 project:
RT 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., Buerckstuemmer T.,
RA 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 2,3-
CC diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-
CC MTPenyl-1-P), which is then dephosphorylated to form the acireductone
CC 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
CC {ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:15843022}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
CC dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03117};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 3/6. {ECO:0000255|HAMAP-Rule:MF_03117}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 4/6. {ECO:0000255|HAMAP-Rule:MF_03117}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03117,
CC ECO:0000269|PubMed:15843022}.
CC -!- INTERACTION:
CC Q9UHY7; Q9H4P4: RNF41; NbExp=7; IntAct=EBI-726969, EBI-2130266;
CC Q9UHY7; P59817: ZNF280A; NbExp=5; IntAct=EBI-726969, EBI-8489342;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}.
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. MasA/MtnC
CC family. {ECO:0000255|HAMAP-Rule:MF_03117}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13671.1; Type=Frameshift; Evidence={ECO:0000305};
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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 CCDS; CCDS3594.1; -. [Q9UHY7-1]
DR RefSeq; NP_001278946.1; NM_001292017.1.
DR RefSeq; NP_067027.1; NM_021204.4. [Q9UHY7-1]
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 AlphaFoldDB; Q9UHY7; -.
DR SMR; Q9UHY7; -.
DR BioGRID; 121811; 33.
DR IntAct; Q9UHY7; 16.
DR MINT; Q9UHY7; -.
DR STRING; 9606.ENSP00000273920; -.
DR DrugBank; DB07912; 2-OXOHEPTYLPHOSPHONIC ACID.
DR DrugBank; DB09325; Sodium fluoride.
DR DEPOD; ENOPH1; -.
DR GlyGen; Q9UHY7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHY7; -.
DR PhosphoSitePlus; Q9UHY7; -.
DR BioMuta; ENOPH1; -.
DR DMDM; 74735024; -.
DR EPD; Q9UHY7; -.
DR jPOST; Q9UHY7; -.
DR MassIVE; Q9UHY7; -.
DR MaxQB; Q9UHY7; -.
DR PaxDb; Q9UHY7; -.
DR PeptideAtlas; Q9UHY7; -.
DR PRIDE; Q9UHY7; -.
DR ProteomicsDB; 84440; -. [Q9UHY7-1]
DR ProteomicsDB; 84441; -. [Q9UHY7-2]
DR Antibodypedia; 25049; 170 antibodies from 24 providers.
DR DNASU; 58478; -.
DR Ensembl; ENST00000273920.8; ENSP00000273920.3; ENSG00000145293.17. [Q9UHY7-1]
DR Ensembl; ENST00000505846.5; ENSP00000427209.1; ENSG00000145293.17. [Q9UHY7-2]
DR GeneID; 58478; -.
DR KEGG; hsa:58478; -.
DR MANE-Select; ENST00000273920.8; ENSP00000273920.3; NM_021204.5; NP_067027.1.
DR UCSC; uc003hmv.4; human. [Q9UHY7-1]
DR CTD; 58478; -.
DR DisGeNET; 58478; -.
DR GeneCards; ENOPH1; -.
DR HGNC; HGNC:24599; ENOPH1.
DR HPA; ENSG00000145293; Low tissue specificity.
DR neXtProt; NX_Q9UHY7; -.
DR OpenTargets; ENSG00000145293; -.
DR PharmGKB; PA162385052; -.
DR VEuPathDB; HostDB:ENSG00000145293; -.
DR eggNOG; KOG2630; Eukaryota.
DR GeneTree; ENSGT00440000039914; -.
DR HOGENOM; CLU_023273_0_0_1; -.
DR InParanoid; Q9UHY7; -.
DR OMA; QLKGHVY; -.
DR OrthoDB; 1475361at2759; -.
DR PhylomeDB; Q9UHY7; -.
DR TreeFam; TF105939; -.
DR BRENDA; 3.1.3.77; 2681.
DR PathwayCommons; Q9UHY7; -.
DR Reactome; R-HSA-1237112; Methionine salvage pathway.
DR SignaLink; Q9UHY7; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR BioGRID-ORCS; 58478; 17 hits in 1089 CRISPR screens.
DR ChiTaRS; ENOPH1; human.
DR EvolutionaryTrace; Q9UHY7; -.
DR GenomeRNAi; 58478; -.
DR Pharos; Q9UHY7; Tbio.
DR PRO; PR:Q9UHY7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UHY7; protein.
DR Bgee; ENSG00000145293; Expressed in C1 segment of cervical spinal cord and 205 other tissues.
DR ExpressionAtlas; Q9UHY7; baseline and differential.
DR Genevisible; Q9UHY7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043874; F:acireductone synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:UniProtKB.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR CDD; cd01629; HAD_EP; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01681; Salvage_MtnC; 1.
DR HAMAP; MF_03117; Salvage_MtnC_euk; 1.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR027511; ENOPH1_eukaryotes.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR SFLD; SFLDF00044; enolase-phosphatase; 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; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Methionine biosynthesis; Nucleus;
KW Reference proteome.
FT CHAIN 1..261
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000254007"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117,
FT ECO:0000269|PubMed:15843022"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117,
FT ECO:0000269|PubMed:15843022"
FT BINDING 153..154
FT /ligand="substrate"
FT BINDING 187
FT /ligand="substrate"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117,
FT ECO:0000269|PubMed:15843022"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021160"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1YNS"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:1YNS"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 83..103
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1YNS"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1YNS"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1YNS"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:1YNS"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:1YNS"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1YNS"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1YNS"
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
