(data stored in ACNUC7421 zone)

SWISSPROT: AROB_PSEPF

ID   AROB_PSEPF              Reviewed;         366 AA.
AC   Q3KJA1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110};
DE            Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110};
DE            EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110};
GN   Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110};
GN   OrderedLocusNames=Pfl01_0411;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-
CC       heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
CC       {ECO:0000255|HAMAP-Rule:MF_00110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394;
CC         EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC       Note=Binds 1 divalent metal cation per subunit. Can use either
CC       Co(2+) or Zn(2+). {ECO:0000255|HAMAP-Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC       Dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_00110}.
DR   EMBL; CP000094; ABA72155.1; -; Genomic_DNA.
DR   RefSeq; WP_011332082.1; NC_007492.2.
DR   SMR; Q3KJA1; -.
DR   STRING; 205922.Pfl01_0411; -.
DR   PRIDE; Q3KJA1; -.
DR   EnsemblBacteria; ABA72155; ABA72155; Pfl01_0411.
DR   KEGG; pfo:Pfl01_0411; -.
DR   eggNOG; ENOG4105D49; Bacteria.
DR   eggNOG; COG0337; LUCA.
DR   HOGENOM; HOG000007970; -.
DR   KO; K01735; -.
DR   OMA; CGFIADP; -.
DR   BioCyc; PFLU205922:G1G4S-415-MONOMER; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd08195; DHQS; 1.
DR   HAMAP; MF_00110; DHQ_synthase; 1.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJA1.
DR   SWISS-2DPAGE; Q3KJA1.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW   Complete proteome; Cytoplasm; Lyase; Metal-binding; NAD;
KW   Nucleotide-binding; Zinc.
FT   CHAIN         1    366       3-dehydroquinate synthase.
FT                                /FTId=PRO_0000231115.
FT   NP_BIND      69     74       NAD. {ECO:0000255|HAMAP-Rule:MF_00110}.
FT   NP_BIND     103    107       NAD. {ECO:0000255|HAMAP-Rule:MF_00110}.
FT   NP_BIND     127    128       NAD. {ECO:0000255|HAMAP-Rule:MF_00110}.
FT   METAL       182    182       Cobalt or zinc. {ECO:0000255|HAMAP-
FT                                Rule:MF_00110}.
FT   METAL       245    245       Cobalt or zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00110}.
FT   METAL       262    262       Cobalt or zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00110}.
FT   BINDING     140    140       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00110}.
FT   BINDING     149    149       NAD. {ECO:0000255|HAMAP-Rule:MF_00110}.
SQ   SEQUENCE   366 AA;  39833 MW;  6849C2A1BEB3155B CRC64;
     MQTLKVDLGE RSYPIHIGEG LLDQPELLAP HIHGRQVAII SNETVAPLYL ERLTRSLAQF
     SVVSVVLPDG EAFKNWETLQ LIFDGLLTAR HDRRTTVIAL GGGVIGDMAG FAAACYQRGV
     DFIQIPTTLL SQVDSSVGGK TGINHPLGKN MVGAFYQPNV VLIDTASLKT LPARELSAGL
     AEVIKYGLIC DEPFLTWLED NVDALRALDQ TALTYAIERS CAAKAAVVGA DEKETGVRAT
     LNLGHTFGHA IETHMGYGVW LHGEAVAAGT VMALEMSARL GWISEQERDR GIRLFQRAGL
     PVIPPEEMTE ADFLEHMAID KKVIDGRLRL VLLRRMGEAV VTDDYPKEVL QATLGADYRA
     LAQLKG
//

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