ENOPH_CAEBR
ID ENOPH_CAEBR Reviewed; 249 AA.
AC A8Y461;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN ORFNames=CBG23332;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC family. {ECO:0000255|HAMAP-Rule:MF_03117}.
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DR EMBL; HE601533; CAP39681.1; -; Genomic_DNA.
DR RefSeq; XP_002636628.1; XM_002636582.1.
DR AlphaFoldDB; A8Y461; -.
DR SMR; A8Y461; -.
DR STRING; 6238.CBG23332; -.
DR EnsemblMetazoa; CBG23332.1; CBG23332.1; WBGene00041706.
DR GeneID; 8578623; -.
DR KEGG; cbr:CBG_23332; -.
DR CTD; 8578623; -.
DR WormBase; CBG23332; CBP12398; WBGene00041706; -.
DR eggNOG; KOG2630; Eukaryota.
DR HOGENOM; CLU_023273_0_0_1; -.
DR InParanoid; A8Y461; -.
DR OMA; QLKGHVY; -.
DR OrthoDB; 1475361at2759; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000008549; Chromosome V.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Nucleus; Reference proteome.
FT CHAIN 1..249
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000393988"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 146..147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ SEQUENCE 249 AA; 28242 MW; 3EC1EEA07835CE0B CRC64;
MTNTTTIQFN ALLLDIEGTI TSISFVKDEL FPYAFENVGK YLEEHYDKPA TQIIIEDLRR
LAEQQLETDA DVVKIRERKQ ECIEDVTKNV RHWIKRDKKL TPMKALQGLI WEEAYQRGYV
KGHVYPDVLP ILKIIESRQI PIYIYSSGSV HAQKLLFANS VEGDMTKILY GYFDTNIGLK
GETSSYTKIS EQIGVPEKDI LFLTDVEAEA AAASKAGLQT RLVIRPGNAT LTQEAKNAYG
TIHTLEEIL
