位置:首页 > 蛋白库 > ENOPH_BOVIN
ENOPH_BOVIN
ID   ENOPH_BOVIN             Reviewed;         261 AA.
AC   Q0VD27;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC119871; AAI19872.1; -; mRNA.
DR   RefSeq; NP_001069343.1; NM_001075875.1.
DR   AlphaFoldDB; Q0VD27; -.
DR   SMR; Q0VD27; -.
DR   STRING; 9913.ENSBTAP00000019702; -.
DR   PaxDb; Q0VD27; -.
DR   PRIDE; Q0VD27; -.
DR   Ensembl; ENSBTAT00000019702; ENSBTAP00000019702; ENSBTAG00000014805.
DR   GeneID; 525563; -.
DR   KEGG; bta:525563; -.
DR   CTD; 58478; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014805; -.
DR   VGNC; VGNC:28500; ENOPH1.
DR   eggNOG; KOG2630; Eukaryota.
DR   GeneTree; ENSGT00440000039914; -.
DR   HOGENOM; CLU_023273_0_0_1; -.
DR   InParanoid; Q0VD27; -.
DR   OMA; QLKGHVY; -.
DR   OrthoDB; 1475361at2759; -.
DR   TreeFam; TF105939; -.
DR   Reactome; R-BTA-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000014805; Expressed in Ammon's horn and 105 other 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; 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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Nucleus; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000254006"
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         153..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ   SEQUENCE   261 AA;  28930 MW;  D6288757291FAC10 CRC64;
     MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYVKENVE EYLQAHWEEE ECQQDVRLLR
     KQAEEDSHLD GAVPIPAASG NGADDPQWMI QAVVDNVYWQ MSLDRKTTAL KQLQGHMWRA
     AFKAGHMKAE FFEDVVPAVR KWREAGMKVY VYSSGSVEAQ KLLFGHSTEG DILELVDGHF
     DTKIGHKVES ESYQKIASSI GCSTNNILFL TDVSREASAA EEAGVHVAVV VRPGNAGLTD
     DEKTHFSLIT SFSELYLPSS T
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024