ID A0A099W6L9_9LIST Unreviewed; 363 AA.
AC A0A099W6L9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ORFNames=EP57_08735 {ECO:0000313|EMBL:KGL40632.1}, HB810_03580
GN {ECO:0000313|EMBL:MBC1245665.1}, HB811_02780
GN {ECO:0000313|EMBL:MBC1315689.1}, HCA46_03125
GN {ECO:0000313|EMBL:MBC1777817.1}, HCB83_02615
GN {ECO:0000313|EMBL:MBC2303745.1}, HCJ43_11630
GN {ECO:0000313|EMBL:MBC1975920.1}, HCJ81_02875
GN {ECO:0000313|EMBL:MBC2309811.1};
OS Listeria booriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL40632.1, ECO:0000313|Proteomes:UP000029844};
RN [1] {ECO:0000313|EMBL:KGL40632.1, ECO:0000313|Proteomes:UP000029844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL40632.1,
RC ECO:0000313|Proteomes:UP000029844};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing environments.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000526161, ECO:0000313|Proteomes:UP000543379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL L7-0035 {ECO:0000313|EMBL:MBC2303745.1,
RC ECO:0000313|Proteomes:UP000526161}, FSL L7-0039
RC {ECO:0000313|EMBL:MBC2309811.1, ECO:0000313|Proteomes:UP000565628},
RC FSL L7-0520 {ECO:0000313|EMBL:MBC1975920.1,
RC ECO:0000313|Proteomes:UP000587214}, FSL L7-1017
RC {ECO:0000313|EMBL:MBC1777817.1, ECO:0000313|Proteomes:UP000547643},
RC FSL L7-1816 {ECO:0000313|EMBL:MBC1315689.1,
RC ECO:0000313|Proteomes:UP000543379}, and FSL L7-1827
RC {ECO:0000313|EMBL:MBC1245665.1, ECO:0000313|Proteomes:UP000574869};
RA Liao J., Wiedmann M.;
RT "Soil Listeria distribution.";
RL Submitted (MAR-2020) 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:KGL40632.1}.
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DR EMBL; JNFA01000023; KGL40632.1; -; Genomic_DNA.
DR EMBL; JAAROQ010000001; MBC1245665.1; -; Genomic_DNA.
DR EMBL; JAAROV010000001; MBC1315689.1; -; Genomic_DNA.
DR EMBL; JAARUV010000001; MBC1777817.1; -; Genomic_DNA.
DR EMBL; JAASWF010000007; MBC1975920.1; -; Genomic_DNA.
DR EMBL; JAARZW010000002; MBC2303745.1; -; Genomic_DNA.
DR EMBL; JAASWV010000003; MBC2309811.1; -; Genomic_DNA.
DR RefSeq; WP_036085840.1; NZ_UGPF01000002.1.
DR AlphaFoldDB; A0A099W6L9; -.
DR STRING; 1552123.EP57_08735; -.
DR GeneID; 58717458; -.
DR eggNOG; COG0337; Bacteria.
DR OrthoDB; 9806583at2; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000029844; Unassembled WGS sequence.
DR Proteomes; UP000526161; Unassembled WGS sequence.
DR Proteomes; UP000543379; Unassembled WGS sequence.
DR Proteomes; UP000547643; Unassembled WGS sequence.
DR Proteomes; UP000565628; Unassembled WGS sequence.
DR Proteomes; UP000574869; Unassembled WGS sequence.
DR Proteomes; UP000587214; 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:UP000029844};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT DOMAIN 69..324
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT BINDING 106..110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 130..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ SEQUENCE 363 AA; 40237 MW; A7BF498950BF1A07 CRC64;
MAEITVTTKD KVYPVYISKN ALHEQADNLV AELGRFSQVF VMTDVNVAKA HLNKLDELLA
PLEKVSYYVT PAGEEAKTFA VYEDAMTKAI EAGLDRKSVL VAFGGGVIGD LGGFVAATYM
RGIAFYQIPT TVLAHDSAVG GKVAINHPLG KNMVGNFYQP EAVIYDTSLF GTLSEREMRS
GFAELVKHAL IRDPAMLVEL METYKTPRDL YEVDLTPYLA RGIAIKAEIV SQDETEQGIR
AFLNFGHTFG HAMEAYGAFG KWLHGESITF GMIYALDMSE QLLGLHFDKE ALLKWLAALG
YEVHLPNNLD FDVLLEHMKH DKKTTFNEIT MVLLEEIGKP TIQKVTDDVI EATFKRVSQE
GQG
//
