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Database: UniProt
Entry: A0A2V5K6K8_9BACL
LinkDB: A0A2V5K6K8_9BACL
Original site: A0A2V5K6K8_9BACL 
ID   A0A2V5K6K8_9BACL        Unreviewed;       364 AA.
AC   A0A2V5K6K8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-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:PYI54918.1};
GN   ORFNames=DLM86_10230 {ECO:0000313|EMBL:PYI54918.1};
OS   Paenibacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI54918.1, ECO:0000313|Proteomes:UP000247476};
RN   [1] {ECO:0000313|EMBL:PYI54918.1, ECO:0000313|Proteomes:UP000247476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DXL2 {ECO:0000313|EMBL:PYI54918.1,
RC   ECO:0000313|Proteomes:UP000247476};
RA   Dai X.;
RT   "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL   Submitted (MAY-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}.
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:PYI54918.1}.
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DR   EMBL; QJVJ01000004; PYI54918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5K6K8; -.
DR   OrthoDB; 9806583at2; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000247476; 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:UP000247476};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT   DOMAIN          71..326
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   BINDING         108..112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         132..133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         144
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         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   364 AA;  38996 MW;  6CB4D7D0E0CB8556 CRC64;
     MRELKVDLGE RSYPIYIGEG ILDGLAATLA KHGIGVKSPL LVVTDENVAK HYLTKVTELL
     EADGYRVANA VVAPGEKSKS LSVMEEIITV ALEAGLDRNS AVIALGGGVV GDLAGFVAAS
     YMRGVRFVQI PTTILAHDSS VGGKVAVNHR LAKNVIGAFH QPEFVLYDIA TLKSLPDRVV
     REGLSELVKE GFIMDREFVE WCDANASRLL ALDSAALEHA LYIGCGVKAK VVSADEKEGG
     LRAVLNLGHT IGHALEAVAG YDELHHGEAI AIGMVGAALL SAKLGNPPSI AEETERILRQ
     FGLPVRIPAH FDTDAIMSAM MHDKKFKEGK MVFIVPTAIG QVEINPNVPS EWVREIVDRL
     KGEA
//
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