ENOPH_MOUSE
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 03-AUG-2022, entry version 154.
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, Osteoclast,
RC 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 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;
CC Evidence={ECO:0000255|HAMAP-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 EPD; Q8BGB7; -.
DR MaxQB; Q8BGB7; -.
DR PaxDb; Q8BGB7; -.
DR PeptideAtlas; Q8BGB7; -.
DR PRIDE; Q8BGB7; -.
DR ProteomicsDB; 277791; -. [Q8BGB7-1]
DR ProteomicsDB; 277792; -. [Q8BGB7-2]
DR Antibodypedia; 25049; 170 antibodies from 24 providers.
DR DNASU; 67870; -.
DR Ensembl; ENSMUST00000031268; ENSMUSP00000031268; ENSMUSG00000029326. [Q8BGB7-1]
DR Ensembl; ENSMUST00000169390; ENSMUSP00000129704; ENSMUSG00000029326. [Q8BGB7-1]
DR GeneID; 67870; -.
DR KEGG; mmu:67870; -.
DR UCSC; uc008yha.2; mouse. [Q8BGB7-1]
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; QLKGHVY; -.
DR OrthoDB; 1475361at2759; -.
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 74 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 265 other tissues.
DR Genevisible; Q8BGB7; MM.
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; 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 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
