位置:首页 > 蛋白库 > YDIB_SHIDS
YDIB_SHIDS
ID   YDIB_SHIDS              Reviewed;         297 AA.
AC   Q32GE1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Quinate/shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01578};
DE            EC=1.1.1.282 {ECO:0000255|HAMAP-Rule:MF_01578};
DE   AltName: Full=NAD-dependent shikimate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01578};
GN   Name=ydiB {ECO:0000255|HAMAP-Rule:MF_01578}; OrderedLocusNames=SDY_1475;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: The actual biological function of YdiB remains unclear, nor
CC       is it known whether 3-dehydroshikimate or quinate represents the
CC       natural substrate. Catalyzes the reversible NAD-dependent reduction of
CC       both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate
CC       (SA) and quinate, respectively. It can use both NAD or NADP for
CC       catalysis, however it has higher catalytic efficiency with NAD.
CC       {ECO:0000255|HAMAP-Rule:MF_01578}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:18425, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000255|HAMAP-Rule:MF_01578}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01578}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01578}.
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; CP000034; ABB61614.1; -; Genomic_DNA.
DR   RefSeq; WP_000798754.1; NC_007606.1.
DR   RefSeq; YP_403105.1; NC_007606.1.
DR   AlphaFoldDB; Q32GE1; -.
DR   SMR; Q32GE1; -.
DR   STRING; 300267.SDY_1475; -.
DR   EnsemblBacteria; ABB61614; ABB61614; SDY_1475.
DR   KEGG; sdy:SDY_1475; -.
DR   PATRIC; fig|300267.13.peg.1759; -.
DR   HOGENOM; CLU_044063_4_4_6; -.
DR   OMA; SIFARND; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052733; F:quinate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0052734; F:shikimate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   HAMAP; MF_01578; Shikimate_DH_YdiB; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR022872; Quinate/Shikimate_DH.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   PANTHER; PTHR21089; PTHR21089; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..297
FT                   /note="Quinate/shikimate dehydrogenase"
FT                   /id="PRO_0000280776"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT   BINDING         141..144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT   BINDING         164..167
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT   BINDING         214
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT   BINDING         241..244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT   BINDING         264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
SQ   SEQUENCE   297 AA;  32390 MW;  88B8547CFBFE6D5B CRC64;
     MKNTCSTNWK HHPAKYELIG LMAYPIRHSL SPEMQNKALE KAGLPFTYMA FEVDNDSFPG
     AIEGLKALKM RGTGVSMPNK QLACEYVDEL TPAAKLVGAI NTIVNDDGYL RGYNTDGTGH
     IRAIKESGFD IKGKTMVLLG AGGASTAIGA QGAIEGLKEI KLFNRRDEFF DKALAFAQRV
     NENTDCVVTV TDLADQQAFA EALASDDILT NGTKVGMKPL ENKSLVNDIS LLHPGLLVTE
     CVYNPHMTKL LQQAQQAGCK TIDGYGMLLW QGAEQFTLWT GKDFPLEYVK QVMGFGA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024