AROB_RHOPA
ID AROB_RHOPA Reviewed; 381 AA.
AC Q6NCG9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RPA0503;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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}.
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DR EMBL; BX572594; CAE25947.1; -; Genomic_DNA.
DR RefSeq; WP_011156071.1; NC_005296.1.
DR AlphaFoldDB; Q6NCG9; -.
DR SMR; Q6NCG9; -.
DR STRING; 258594.RPA0503; -.
DR PRIDE; Q6NCG9; -.
DR EnsemblBacteria; CAE25947; CAE25947; RPA0503.
DR GeneID; 66891521; -.
DR KEGG; rpa:RPA0503; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_2_5; -.
DR OMA; YGVIWDA; -.
DR PhylomeDB; Q6NCG9; -.
DR BioCyc; RPAL258594:TX73_RS02610-MON; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000001426; 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: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..381
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000231121"
FT BINDING 81..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 115..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ SEQUENCE 381 AA; 40366 MW; C5C20E55E401E8D2 CRC64;
MNAPQKHSAP ITVEVALGDR AYEIVIGRDV IASLGERIAK LRPGARTAIV TDRTVAKTWL
KRTEEVLDQA GIAHASVIVG EGESSKSYAG LEQVCEALIA AKIERNDLVI ALGGGVIGDL
AGFSASLLRR GVDFVQVPTS LLAQVDSSVG GKTGINSPQG KNLIGTFHQP VLVLADTAIL
DTLSPRQFRA GYAEVAKYGA LGDEAFFAWL EANHAELFSG GAAREHAVAT SCRAKAAIVA
RDERETGDRA LLNLGHTFGH ALEAATGFSD RLFHGEGVAI GMVLAAEFSA ERGMMPATDA
ERLAKHLAEV GLPTRLQDIA GFTQEGLADA DRLMALMAQD KKVKRGELTF ILMEGIGRAV
IASKVEPAPV RDFLQRKLAQ A
