AROB_PSEAE
ID AROB_PSEAE Reviewed; 368 AA.
AC P34002;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=PA5038;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-221.
RC STRAIN=ATCC 25102 / PAK;
RX PubMed=7901733; DOI=10.1111/j.1365-2958.1993.tb01744.x;
RA Martin P.R., Hobbs M., Free P.D., Jeske Y., Mattick J.S.;
RT "Characterization of pilQ, a new gene required for the biogenesis of type 4
RT fimbriae in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 9:857-868(1993).
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=NAD(+); Xref=ChEBI:CHEBI:57540;
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 -!- 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,
CC ECO:0000305}.
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DR EMBL; AE004091; AAG08423.1; -; Genomic_DNA.
DR EMBL; L13866; AAC36825.1; -; Unassigned_DNA.
DR PIR; G83015; G83015.
DR RefSeq; NP_253725.1; NC_002516.2.
DR RefSeq; WP_003114574.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; P34002; -.
DR SMR; P34002; -.
DR STRING; 287.DR97_2393; -.
DR PaxDb; P34002; -.
DR PRIDE; P34002; -.
DR EnsemblBacteria; AAG08423; AAG08423; PA5038.
DR GeneID; 881253; -.
DR KEGG; pae:PA5038; -.
DR PATRIC; fig|208964.12.peg.5282; -.
DR PseudoCAP; PA5038; -.
DR HOGENOM; CLU_001201_0_2_6; -.
DR InParanoid; P34002; -.
DR OMA; YGVIWDA; -.
DR PhylomeDB; P34002; -.
DR BioCyc; PAER208964:G1FZ6-5154-MON; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
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_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;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..368
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140768"
FT BINDING 69..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 103..107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 127..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ SEQUENCE 368 AA; 40109 MW; 04D3C425DF75A6FA CRC64;
MRTLHVDLGE RSYPIYIGEN LLGDARWFAP HIVGRRVAVI SNETVAPLYL ETLLKALQGH
EVTPVVLPDG EAYKQWETLQ LIFDVLLKER HDRKTTLIAL GGGVIGDMAG FAAACYQRGV
NFIQVPTTLL SQVDSSVGGK TGINHPLGKN MIGAFYQPQA VVIDTASLKT LPSRELSAGL
AEVIKYGFIC DEPFITWLEA HMDALLALEP TVVTEAIERS CAAKARVVGA DERESGVRAT
LNLGHTFGHA IETQQGYGVW LHGEAVGAGT VMALEMSHRL GWLSAAERDR GIRLLRRAGL
PVVPPAEMTA EDFMEHMAVD KKVLDGRLRL VLLQGLGNAV VTGDFPREIL DATLRTDYRA
LADQLGDE
