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MTBC2_VITVI
ID   MTBC2_VITVI             Reviewed;         531 AA.
AC   E0CTF3; F6H5E7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 2 {ECO:0000255|HAMAP-Rule:MF_03118};
DE   Includes:
DE     RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03118};
DE              Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03118};
DE              EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03118};
DE   Includes:
DE     RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03118};
DE              EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_03118};
DE     AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_03118};
GN   OrderedLocusNames=VIT_12s0028g03470;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024;
RX   PubMed=17721507; DOI=10.1038/nature06148;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC         dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
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_03118};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03118};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03118};
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 2/6. {ECO:0000255|HAMAP-Rule:MF_03118}.
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_03118}.
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_03118}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the aldolase class II
CC       family. MtnB subfamily. {ECO:0000255|HAMAP-Rule:MF_03118}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HAD-like
CC       hydrolase superfamily. MasA/MtnC family. {ECO:0000255|HAMAP-
CC       Rule:MF_03118}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCB47296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FN595235; CCB47296.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; FN597034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002274553.3; XM_002274517.4.
DR   AlphaFoldDB; E0CTF3; -.
DR   SMR; E0CTF3; -.
DR   STRING; 29760.VIT_12s0028g03470.t01; -.
DR   EnsemblPlants; Vitvi12g04066_t001; Vitvi12g04066_P001; Vitvi12g04066.
DR   GeneID; 100247253; -.
DR   Gramene; Vitvi12g04066_t001; Vitvi12g04066_P001; Vitvi12g04066.
DR   KEGG; vvi:100247253; -.
DR   eggNOG; KOG2630; Eukaryota.
DR   eggNOG; KOG2631; Eukaryota.
DR   HOGENOM; CLU_023273_3_1_1; -.
DR   InParanoid; E0CTF3; -.
DR   OrthoDB; 436252at2759; -.
DR   UniPathway; UPA00904; UER00875.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000009183; Chromosome 12.
DR   ExpressionAtlas; E0CTF3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc 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; 3.40.225.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR   HAMAP; MF_03118; Salvage_MtnBC; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR023943; Enolase-ppase_E1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR   InterPro; IPR027505; MtnB_viridiplantae.
DR   InterPro; IPR027514; Salvage_MtnB_euk.
DR   PANTHER; PTHR10640; PTHR10640; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Hydrolase; Lyase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Multifunctional enzyme; Reference proteome; Zinc.
FT   CHAIN           1..531
FT                   /note="Probable bifunctional methylthioribulose-1-phosphate
FT                   dehydratase/enolase-phosphatase E1 2"
FT                   /id="PRO_0000403961"
FT   REGION          1..248
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   REGION          292..531
FT                   /note="Enolase-phosphatase E1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   ACT_SITE        163
FT                   /note="Proton donor/acceptor; for methylthioribulose-1-
FT                   phosphate dehydratase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /ligand_label="1"
FT                   /ligand_note="for methylthioribulose-1-phosphate
FT                   dehydratase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         430..431
FT                   /ligand="substrate"
FT                   /ligand_label="2"
FT                   /ligand_note="for enolase-phosphatase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         464
FT                   /ligand="substrate"
FT                   /ligand_label="2"
FT                   /ligand_note="for enolase-phosphatase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT   BINDING         490
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
SQ   SEQUENCE   531 AA;  58661 MW;  239C9C74D8FD5672 CRC64;
     MGVPSEGAVG NVNGNEVGTT ASFAGYMETR GVREARVLAS ELCRHMYTLG WFSGTGGSIT
     IKVHDDSIPK PRQLVVISPS GVQKERMVPE DMYVLSSDGF ILSTPPLKPY PHKPPKCTDC
     TPLFMKVYEM RDAGAVIHSH GMESCIVTMI LPFSKEFRIT HMEMIKGIKG HGYHDELVVP
     IIENTAHEAE LVESLTEAIT AYPKTTAVLV RNHGVYVWGD SWISAKTQAE CYHYLFDAAI
     KLHQLGLDWS TPTHGPIRSI NGIWGCNGTM SRGLKVGGLS LDDMIEPSQR CILLDIEGTT
     TPISFVTDVL FPYAHANVGK HLAATFDSEE TQDDINLLRS QIQHDLEHGV VGAVPIPPDY
     VGKELVIASF VANVEAMIRA DRNITALKQL QGHIWKTGFQ SNELVGVVFD DVPEALERWH
     ASGIKVYIYS SGSREAQQLI FSNSNYGDLR KYFCGFFDTT MGNKKETHSY FEILRTVGID
     RPSDMLFVTD VFQEAVAARA AGLEVVISIR PGNGPLPENH GFRTIETFLE I
 
 
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