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ENOPH_YEAS1
ID   ENOPH_YEAS1             Reviewed;         227 AA.
AC   B3LRX9;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 61.
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=Unknown transcript 4 protein {ECO:0000255|HAMAP-Rule:MF_03117};
GN   Name=UTR4 {ECO:0000255|HAMAP-Rule:MF_03117}; ORFNames=SCRG_04432;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) 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   -!- SEQUENCE CAUTION:
CC       Sequence=EDV08795.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH408052; EDV08795.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B3LRX9; -.
DR   SMR; B3LRX9; -.
DR   EnsemblFungi; EDV08795; EDV08795; SCRG_04432.
DR   HOGENOM; CLU_023273_1_1_1; -.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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_03117; Salvage_MtnC_euk; 1.
DR   InterPro; IPR023943; Enolase-ppase_E1.
DR   InterPro; IPR027511; ENOPH1_eukaryotes.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01691; enolase-ppase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Nucleus.
FT   CHAIN           1..227
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000377656"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         118..119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ   SEQUENCE   227 AA;  25208 MW;  E29DD481FD450D49 CRC64;
     MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TKKVPQLVQQ DTRDSPVSNI LSQFHIDDKE
     QLQAHILELV AKDVKDPILK QLQGYIWAQG YESGQIKAPV YADAIDFIKR KKRVFIYSSG
     SVKAQKLLFG YVQDPNAPAH DSLDLNSYID GYFDINTSGK KTETQSYANI LRDIGAKASE
     VLFLSDNPLE LDAAAGVGIA TGLASRPGNA PVPDGQKYQV YKDFETL
 
 
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