(data stored in SCRATCH zone)

SWISSPROT: AROB_PSEU2

ID   AROB_PSEU2              Reviewed;         367 AA.
AC   Q4ZZE3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 89.
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}; OrderedLocusNames=Psyr_0409;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC       7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-
CC       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, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         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 Co(2+)
CC       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 biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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; CP000075; AAY35479.1; -; Genomic_DNA.
DR   RefSeq; WP_003403032.1; NC_007005.1.
DR   RefSeq; YP_233517.1; NC_007005.1.
DR   SMR; Q4ZZE3; -.
DR   STRING; 205918.Psyr_0409; -.
DR   EnsemblBacteria; AAY35479; AAY35479; Psyr_0409.
DR   GeneID; 3365885; -.
DR   KEGG; psb:Psyr_0409; -.
DR   PATRIC; fig|205918.7.peg.424; -.
DR   eggNOG; ENOG4105D49; Bacteria.
DR   eggNOG; COG0337; LUCA.
DR   HOGENOM; HOG000007970; -.
DR   KO; K01735; -.
DR   OMA; YGVIWDA; -.
DR   BioCyc; PSYR205918:G1G4J-410-MONOMER; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000000426; 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   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; Q4ZZE3.
DR   SWISS-2DPAGE; Q4ZZE3.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW   Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding; Zinc.
FT   CHAIN           1..367
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_0000231117"
FT   NP_BIND         69..74
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   NP_BIND         103..107
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   NP_BIND         127..128
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   METAL           182
FT                   /note="Cobalt or zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   METAL           245
FT                   /note="Cobalt or zinc; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   METAL           262
FT                   /note="Cobalt or zinc; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         140
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT   BINDING         149
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   367 AA;  40024 MW;  3887C5BA5C5EFA1B CRC64;
     MQTLKVELGE RSYPIHIGEG LLDQPELLTP HIVGRQVAIV SNTTVAPLYL ERLTQTLAGY
     NVLPIVLPDG EAFKNWETLQ TIFDGLLTAR HDRRTTVIAL GGGVIGDMAG FAAACYQRGV
     NFIQIPTTLL SQVDSSVGGK TGINHPLGKN MVGAFYQPSV VLIDTASLNT LPERELSAGL
     AEVIKYGLIC DEPFLTWLEE HVDALRGLDQ AALTVAIERS CAAKALVVGA DERESGVRAT
     LNLGHTFGHA IETHMGYGVW LHGEAVAAGT VMALEMSSRL GWISTQERDR GIRLFQRAGL
     PVVPPQDMTQ DNFLEHMAID KKVIDGRLRL VLLRRMGEAV ITDEYPKEVL QATLVADYRA
     LVDQLRG
//

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