ID A0A2R8AB75_9RHOB Unreviewed; 379 AA.
AC A0A2R8AB75;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:SPF29335.1};
GN ORFNames=POI8812_01643 {ECO:0000313|EMBL:SPF29335.1};
OS Pontivivens insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pontivivens.
OX NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF29335.1, ECO:0000313|Proteomes:UP000244932};
RN [1] {ECO:0000313|EMBL:SPF29335.1, ECO:0000313|Proteomes:UP000244932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF29335.1,
RC ECO:0000313|Proteomes:UP000244932};
RA Keele B.F.;
RL Submitted (MAR-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}.
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DR EMBL; OMKW01000002; SPF29335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AB75; -.
DR OrthoDB; 9806583at2; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000244932; 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:UP000244932};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT DOMAIN 79..341
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT BINDING 116..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 140..141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ SEQUENCE 379 AA; 40270 MW; D4C8624C6ABC51BC CRC64;
MTLSQAFDTQ CETVRVELGD RSYDIVIGAD VLTEAGARIA PLLKRPKVAI LTESRVAGLH
LNALQVSLKA AGIESTALEL APGEATKGWA GLQQAVEWLL EQKVERDDIV VAFGGGVIGD
LAGFAAAILR RGVRFVQIPT SLLAQVDSSV GGKTGINSPQ GKNLIGAFHQ PHLVLADTAL
LGTLTERDFL AGYGEVVKYG LLGDAAFFDW MEREGPRLAA GDMAARARAV RRSCEMKAEI
VARDEQERGD RALLNLGHTF GHALEAATGY SDRLLHGEGV AVGCVLAFEL SSRLGLCPQE
APGRVAAHLT MMGMKVRLGD IDGALPDADG LIALMGQDKK VQDGQITFIL ARAIGEAFVA
RDVDLSVVRD LLTEELAAR
//
