位置:首页 > 蛋白库 > ENOPH_DROAN
ENOPH_DROAN
ID   ENOPH_DROAN             Reviewed;         252 AA.
AC   B3M173;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=GF16066;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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; CH902617; EDV44343.1; -; Genomic_DNA.
DR   RefSeq; XP_001955782.1; XM_001955746.2.
DR   AlphaFoldDB; B3M173; -.
DR   SMR; B3M173; -.
DR   STRING; 7217.FBpp0119258; -.
DR   EnsemblMetazoa; FBtr0120766; FBpp0119258; FBgn0093088.
DR   GeneID; 6498863; -.
DR   KEGG; dan:6498863; -.
DR   eggNOG; KOG2630; Eukaryota.
DR   HOGENOM; CLU_023273_0_0_1; -.
DR   InParanoid; B3M173; -.
DR   OMA; QLKGHVY; -.
DR   OrthoDB; 1475361at2759; -.
DR   PhylomeDB; B3M173; -.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000007801; 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_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   PRINTS; PR00413; HADHALOGNASE.
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; Reference proteome.
FT   CHAIN           1..252
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000393976"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         142..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ   SEQUENCE   252 AA;  28142 MW;  D08CEF86E4B998D3 CRC64;
     MTAEKREAKV VLVDIEGTTT SISFVHQVLF PHAKENVEKY LKEYWENEET KQIVEDLQQV
     PQYADYQATL SAPPAVVDVK VIAGFVRYLI DKDLKVTPMK TLQGLIWACG YASGELKGHV
     YEDVPDAFRA WQKAGLRIAV YSSGSVDAQK LIFGYSVAGN LLPYLSDHFD THVGHKQEQQ
     SYVNISNSLR EKPQNILFLT DIPGEASAAL SAGLQTIILH RPGNGPLSDD QKSNYEVIPD
     FKSLYSLQLP QK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024