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Database: UniProt
Entry: E6KVL7_9PAST
LinkDB: E6KVL7_9PAST
Original site: E6KVL7_9PAST 
ID   E6KVL7_9PAST            Unreviewed;       362 AA.
AC   E6KVL7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684, ECO:0000256|HAMAP-Rule:MF_00110};
DE            Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE            EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031, ECO:0000256|HAMAP-Rule:MF_00110};
GN   Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110,
GN   ECO:0000313|EMBL:EFU68326.1};
GN   ORFNames=HMPREF9064_0199 {ECO:0000313|EMBL:EFU68326.1};
OS   Aggregatibacter segnis ATCC 33393.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU68326.1, ECO:0000313|Proteomes:UP000032871};
RN   [1] {ECO:0000313|EMBL:EFU68326.1, ECO:0000313|Proteomes:UP000032871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU68326.1,
RC   ECO:0000313|Proteomes:UP000032871};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC       7-phosphate (DAHP) to dehydroquinate (DHQ).
CC       {ECO:0000256|ARBA:ARBA00003485, ECO:0000256|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, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001393, ECO:0000256|HAMAP-
CC         Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC       Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC       or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911,
CC         ECO:0000256|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:0000256|ARBA:ARBA00004661, ECO:0000256|HAMAP-Rule:MF_00110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00110}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC       Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412,
CC       ECO:0000256|HAMAP-Rule:MF_00110}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFU68326.1}.
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DR   EMBL; AEPS01000002; EFU68326.1; -; Genomic_DNA.
DR   RefSeq; WP_005715889.1; NZ_LS483443.1.
DR   AlphaFoldDB; E6KVL7; -.
DR   STRING; 739.GCA_001059425_00226; -.
DR   GeneID; 60799606; -.
DR   HOGENOM; CLU_001201_0_2_6; -.
DR   OrthoDB; 9806583at2; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000032871; Unassembled WGS sequence.
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:0008652; P:amino acid biosynthetic process; 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   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 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   NCBIfam; TIGR01357; aroB; 1.
DR   PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR43622:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00110};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00110};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00110};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00110};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00110}; Reference proteome {ECO:0000313|Proteomes:UP000032871};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT   DOMAIN          66..324
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   BINDING         70..75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         104..108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         128..129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         150
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         168..171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   362 AA;  39414 MW;  4C53F75526661B6A CRC64;
     MLCVNVELKE RSYPIHIGAG LLTNTDCYPL KSGNKVMIVT NPTVAQHYLS TVTDTLEKIG
     CLVEHVLLPD GEQYKTLDSL NLIFTALLKA NHGRDTTIVA LGGGVIGDVT GYAAASYQRG
     VRFIQIPTTL LAQVDSSVGG KTAVNHELGK NMIGAFYQPT AVIIDTLTLN TLPKREVNAG
     LAEVIKYGAI LDFPFFQWLE QHIDNLVALD QNALQQCIAR CCQLKADIVA RDETEKGDRA
     LLNLGHTFGH AIETHLGYGN WLHGEAVSAG CMMAAVLSEK LGDLTPHDVA RLEKLLARAN
     LPTVSPDGMT AQDYLQLMMR DKKVLNGKLR LVLLKALGQA YVATDVPQEQ VIEAINRCTQ
     VD
//
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