AROB_VIBCH
ID AROB_VIBCH Reviewed; 361 AA.
AC Q9KNV2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=VC_2628;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2] {ECO:0007744|PDB:3OKF}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NAD.
RA Minasov G., Light S.H., Shuvalova L., Papazisi L., Anderson W.F.;
RT "2.5 angstrom resolution crystal structure of 3-dehydroquinate synthase
RT (aroB) from Vibrio cholerae.";
RL Submitted (AUG-2010) to the PDB data bank.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF95769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF95769.1; ALT_INIT; Genomic_DNA.
DR PIR; B82053; B82053.
DR RefSeq; NP_232256.1; NC_002505.1.
DR RefSeq; WP_000439805.1; NZ_LT906614.1.
DR PDB; 3OKF; X-ray; 2.50 A; A/B=1-361.
DR PDBsum; 3OKF; -.
DR AlphaFoldDB; Q9KNV2; -.
DR SMR; Q9KNV2; -.
DR STRING; 243277.VC_2628; -.
DR DNASU; 2615645; -.
DR EnsemblBacteria; AAF95769; AAF95769; VC_2628.
DR GeneID; 57741229; -.
DR KEGG; vch:VC_2628; -.
DR PATRIC; fig|243277.26.peg.2506; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_2_6; -.
DR OMA; YGVIWDA; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000000584; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cobalt; Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..361
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140804"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 70..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 104..108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 128..129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 150..151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 168..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3OKF"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3OKF"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 174..190
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 211..233
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:3OKF"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 263..280
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:3OKF"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:3OKF"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:3OKF"
SQ SEQUENCE 361 AA; 39049 MW; D0388B733EFD3F2A CRC64;
MERITVNLGE RSYPISIGAG LFANPALLSL SAKQKVVIVT NHTVAPLYAP AIISLLDHIG
CQHALLELPD GEQYKTLETF NTVMSFLLEH NYSRDVVVIA LGGGVIGDLV GFAAACYQRG
VDFIQIPTTL LSQVDSSVGG KTAVNHPLGK NMIGAFYQPK AVVIDTDCLT TLPAREFAAG
MAEVIKYGII YDSAFFDWLE AQMEALYALD EQALTYAIAR CCQIKAEVVA QDEKESGIRA
LLNLGHTFGH AIEAHMGYGN WLHGEAVSAG TVMAAKTAQL QGLIDASQFE RILAILKKAH
LPVRTPENMT FADFMQHMMR DKKVLAGELR LVLPTSIGTS AVVKGVPEAV IAQAIEYCRT
V
