ID   ENOPH_MOUSE             Reviewed;         257 AA.
AC   Q8BGB7; Q3TGK8; Q3TXA2; Q3U8Y4; Q8VC92; Q9D6U4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 162.
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; Synonyms=Masa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow macrophage, Diencephalon, Embryonic kidney,
RC   Osteoclast, Placenta, Retina, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03117};
CC       Note=Binds 1 Mg(2+) ion per subunit. {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 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   -!- 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=Q8BGB7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGB7-2; Sequence=VSP_021161;
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC       family. {ECO:0000255|HAMAP-Rule:MF_03117}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE30883.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK009954; BAB26606.1; -; mRNA.
DR   EMBL; AK079062; BAC37520.1; -; mRNA.
DR   EMBL; AK080714; BAC37988.1; -; mRNA.
DR   EMBL; AK082747; BAC38597.1; -; mRNA.
DR   EMBL; AK152021; BAE30883.1; ALT_FRAME; mRNA.
DR   EMBL; AK159356; BAE35014.1; -; mRNA.
DR   EMBL; AK167575; BAE39638.1; -; mRNA.
DR   EMBL; AK168696; BAE40540.1; -; mRNA.
DR   EMBL; BC021429; AAH21429.1; -; mRNA.
DR   CCDS; CCDS39183.1; -. [Q8BGB7-1]
DR   RefSeq; NP_001156507.1; NM_001163035.1. [Q8BGB7-1]
DR   RefSeq; NP_080697.2; NM_026421.3. [Q8BGB7-1]
DR   AlphaFoldDB; Q8BGB7; -.
DR   SMR; Q8BGB7; -.
DR   BioGRID; 212497; 1.
DR   STRING; 10090.ENSMUSP00000129704; -.
DR   iPTMnet; Q8BGB7; -.
DR   PhosphoSitePlus; Q8BGB7; -.
DR   SwissPalm; Q8BGB7; -.
DR   EPD; Q8BGB7; -.
DR   MaxQB; Q8BGB7; -.
DR   PaxDb; 10090-ENSMUSP00000129704; -.
DR   PeptideAtlas; Q8BGB7; -.
DR   ProteomicsDB; 277791; -. [Q8BGB7-1]
DR   ProteomicsDB; 277792; -. [Q8BGB7-2]
DR   Pumba; Q8BGB7; -.
DR   Antibodypedia; 25049; 187 antibodies from 25 providers.
DR   DNASU; 67870; -.
DR   Ensembl; ENSMUST00000031268.8; ENSMUSP00000031268.7; ENSMUSG00000029326.14. [Q8BGB7-1]
DR   Ensembl; ENSMUST00000169390.8; ENSMUSP00000129704.2; ENSMUSG00000029326.14. [Q8BGB7-1]
DR   GeneID; 67870; -.
DR   KEGG; mmu:67870; -.
DR   UCSC; uc008yha.2; mouse. [Q8BGB7-1]
DR   AGR; MGI:1915120; -.
DR   CTD; 58478; -.
DR   MGI; MGI:1915120; Enoph1.
DR   VEuPathDB; HostDB:ENSMUSG00000029326; -.
DR   eggNOG; KOG2630; Eukaryota.
DR   GeneTree; ENSGT00440000039914; -.
DR   HOGENOM; CLU_023273_0_0_1; -.
DR   InParanoid; Q8BGB7; -.
DR   OMA; LQGMVWE; -.
DR   OrthoDB; 275419at2759; -.
DR   PhylomeDB; Q8BGB7; -.
DR   TreeFam; TF105939; -.
DR   Reactome; R-MMU-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   BioGRID-ORCS; 67870; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Enoph1; mouse.
DR   PRO; PR:Q8BGB7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8BGB7; Protein.
DR   Bgee; ENSMUSG00000029326; Expressed in condyle and 269 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:UniProtKB.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   CDD; cd01629; HAD_EP; 1.
DR   Gene3D; 1.10.720.60; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01691; enolase-ppase; 1.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   PANTHER; PTHR20371; ENOLASE-PHOSPHATASE E1; 1.
DR   PANTHER; PTHR20371:SF1; ENOLASE-PHOSPHATASE E1; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01133; C1.5.4:_Enolase-phosphatase_Li; 1.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   Genevisible; Q8BGB7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid biosynthesis; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding; Methionine biosynthesis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..257
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000254008"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         150..151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   VAR_SEQ         55..85
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021161"
FT   CONFLICT        56
FT                   /note="V -> I (in Ref. 2; AAH21429)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="P -> L (in Ref. 2; AAH21429)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="G -> R (in Ref. 1; BAB26606)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="T -> N (in Ref. 1; BAE35014)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   257 AA;  28600 MW;  AD64B1C70976C344 CRC64;
     MVVVSVPAEV TVILLDIEGT TTPIAFVKDV LFPYIKENVK EYLQTHWEEE ECQQDVSLLR
     KQAEEDAHLD GAVPIPVASG SDLQQMIQAV VDNVYWQMSH DRKTTALKQL QGHMWKAAFT
     AGRMKAEFFA DVVPAVRRWR EAGMKVYIYS SGSVEAQKLL FGHSTEGDIL ELIDGHFDTK
     IGHKVDSESY RKIADSIGCS TNNILFLTDV TVEASAAEEA DVHVAVVVRP GNAGLTDDEK
     TYYNLITSFS ELYLPST
//