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AROQ2_PSEAE
ID   AROQ2_PSEAE             Reviewed;         148 AA.
AC   Q9I6P3;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=3-dehydroquinate dehydratase 2;
DE            Short=3-dehydroquinase 2;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase 2;
GN   Name=aroQ2; OrderedLocusNames=PA0245;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG03634.1; -; Genomic_DNA.
DR   PIR; G83615; G83615.
DR   RefSeq; NP_248936.1; NC_002516.2.
DR   RefSeq; WP_003106162.1; NZ_QZGE01000024.1.
DR   AlphaFoldDB; Q9I6P3; -.
DR   SMR; Q9I6P3; -.
DR   STRING; 287.DR97_3202; -.
DR   PaxDb; Q9I6P3; -.
DR   DNASU; 882159; -.
DR   EnsemblBacteria; AAG03634; AAG03634; PA0245.
DR   GeneID; 882159; -.
DR   KEGG; pae:PA0245; -.
DR   PATRIC; fig|208964.12.peg.255; -.
DR   PseudoCAP; PA0245; -.
DR   HOGENOM; CLU_090968_1_0_6; -.
DR   InParanoid; Q9I6P3; -.
DR   OMA; CAGIVIN; -.
DR   PhylomeDB; Q9I6P3; -.
DR   BioCyc; PAER208964:G1FZ6-247-MON; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
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   GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; -; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   InterPro; IPR036441; DHquinase_II_sf.
DR   PANTHER; PTHR21272; PTHR21272; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   SUPFAM; SSF52304; SSF52304; 1.
DR   TIGRFAMs; TIGR01088; aroQ; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..148
FT                   /note="3-dehydroquinate dehydratase 2"
FT                   /id="PRO_0000159919"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            19
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  16273 MW;  1F343909FD1655E3 CRC64;
     MTRTVLVLNG PNLNLLGTRE PQTYGRRTLG EIADECAAFA ETRGFAVDFR QTNQEGQLLD
     WIHQARGRVA GIVINPAAWT HTSVALRDAL AAVELPVVEV HLSNVHQREA FRHHSYVSPV
     ALGVICGFGS LGYRLALEHF AERFEAAA
 
 
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