ID A0A0P0GFU7_9BACT Unreviewed; 422 AA.
AC A0A0P0GFU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00013031, 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:ALJ56861.1};
GN ORFNames=AMD24_00696 {ECO:0000313|EMBL:ALJ56861.1};
OS Candidatus Xiphinematobacter sp. Idaho Grape.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Xiphinematobacter.
OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56861.1, ECO:0000313|Proteomes:UP000062177};
RN [1] {ECO:0000313|EMBL:ALJ56861.1, ECO:0000313|Proteomes:UP000062177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56861.1,
RC ECO:0000313|Proteomes:UP000062177};
RX PubMed=26362082; DOI=10.1093/gbe/evv176;
RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT Role in Nutritional Symbiosis.";
RL Genome Biol. Evol. 7:2727-2746(2015).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|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: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|HAMAP-Rule:MF_00110}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110}.
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DR EMBL; CP012665; ALJ56861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0GFU7; -.
DR STRING; 1704307.AMD24_00696; -.
DR KEGG; xii:AMD24_00696; -.
DR PATRIC; fig|1704307.3.peg.777; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000062177; Chromosome.
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; 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 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}; Cobalt {ECO:0000256|HAMAP-Rule:MF_00110};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00110};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000062177};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00110}.
FT DOMAIN 130..382
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT BINDING 134..139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 168..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 192..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 232..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ SEQUENCE 422 AA; 45770 MW; 6F574304307980F7 CRC64;
MTCLAIFLFF TRVKETLVSI AVAFIKDSFY LAASFPWSPN LPLSTADRTR PRVYTGKDNF
SSMLKIPISC SHASYDVLVG GGLLTHSGDL VAKILAPSRC AVVTDSNVAR HYLQPVLASL
KNVGFKPITL VVPSGERSKS FRQVYNLCHS MVVAGLDRKS VLFSLGGGVI GDLSGFAAAI
FQRGIPLVQL PTTVTAQVDS SVGGKTGVNV AAGKNLIGAF HQPQLVIADP LTLNTLPNRE
YWEGFAEIVK HAIIQDMAML KTLSPERPKD LSALIARNIT VKSALIASDE GDKSGLRALL
NFGHTIGHGI ETAAGYGSLF HGEAISLGII AALWLSKRFS GLLQSDLEYI ARILQRLSLP
IVLPDRILTD SVLTTMRKDK KFEQGKPRFV LTHRLGSAYL SDEVDLQDAR SAIEFLRKLQ
PN
//
