3DHQ_ACIAD
ID 3DHQ_ACIAD Reviewed; 272 AA.
AC Q59087; Q6FBK7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Catabolic 3-dehydroquinate dehydratase {ECO:0000303|PubMed:7592351};
DE Short=3-dehydroquinase {ECO:0000303|PubMed:7592351};
DE EC=4.2.1.10 {ECO:0000250|UniProtKB:P58687};
GN Name=quiB {ECO:0000303|PubMed:7592351}; OrderedLocusNames=ACIAD1713;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=7592351; DOI=10.1128/jb.177.20.5971-5978.1995;
RA Elsemore D.A., Ornston L.N.;
RT "Unusual ancestry of dehydratases associated with quinate catabolism in
RT Acinetobacter calcoaceticus.";
RL J. Bacteriol. 177:5971-5978(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Involved in the biosynthesis of protocatechuate. Catalyzes
CC the catabolic dehydration of 3-dehydroquinate (DHQ) to yield 3-
CC dehydroshikimate. {ECO:0000269|PubMed:7592351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10;
CC Evidence={ECO:0000250|UniProtKB:P58687};
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2.
CC {ECO:0000305|PubMed:7592351}.
CC -!- INDUCTION: By protocatechuate. {ECO:0000269|PubMed:7592351}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000250|UniProtKB:P58687}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37158.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG68555.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L05770; AAC37158.1; ALT_INIT; Genomic_DNA.
DR EMBL; CR543861; CAG68555.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004926647.1; NC_005966.1.
DR AlphaFoldDB; Q59087; -.
DR SMR; Q59087; -.
DR STRING; 62977.ACIAD1713; -.
DR EnsemblBacteria; CAG68555; CAG68555; ACIAD1713.
DR GeneID; 45234100; -.
DR KEGG; aci:ACIAD1713; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_6; -.
DR BioCyc; MetaCyc:MON-33; -.
DR UniPathway; UPA00088; UER00178.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PE 2: Evidence at transcript level;
KW Lyase; Quinate metabolism; Reference proteome; Schiff base.
FT CHAIN 1..272
FT /note="Catabolic 3-dehydroquinate dehydratase"
FT /id="PRO_0000138842"
FT ACT_SITE 163
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT ACT_SITE 190
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 66..68
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 102
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 232
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 251
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 255
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
SQ SEQUENCE 272 AA; 29899 MW; 98646DC5E88BF6D3 CRC64;
MSLPILSTTY AAENTVPASK STYVVKNLNI GDLPVKTLVP ITAKTREQAL AQAKVIAENK
DADIAEFRID LLEFASDTKK VIALGQELNQ ILKDKPLLAT IRTSNEGGKL KVTDQEYEKI
YSEYLKKPFM QLLDIEMFRD QAAVAKLTKL AHQKKVLVVM SNHDFDKTPS EQEIVSRLLK
QDQMGADILK IAVMPKSKQD VFTLMNATLK VSEQSTKPLL TMSMGRLGTI SRIATANMGG
SLSFGMIGEA SAPGQIDVTA LKQFLKTVQP TP
