QUIC_ACIAD
ID QUIC_ACIAD Reviewed; 486 AA.
AC Q43922;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3-dehydroshikimate dehydratase;
DE Short=3-DHS dehydratase;
DE Short=DHSase;
DE EC=4.2.1.118;
GN Name=quiC; OrderedLocusNames=ACIAD1714;
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], AND CHARACTERIZATION.
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: Converts dehydroshikimate to protocatechuate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O;
CC Xref=Rhea:RHEA:24848, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36241; EC=4.2.1.118;
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 2/2.
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DR EMBL; L05770; AAC37159.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68556.1; -; Genomic_DNA.
DR PIR; I39523; I39523.
DR RefSeq; WP_004926650.1; NC_005966.1.
DR AlphaFoldDB; Q43922; -.
DR SMR; Q43922; -.
DR STRING; 62977.ACIAD1714; -.
DR EnsemblBacteria; CAG68556; CAG68556; ACIAD1714.
DR GeneID; 45234101; -.
DR KEGG; aci:ACIAD1714; -.
DR eggNOG; COG3420; Bacteria.
DR HOGENOM; CLU_044040_0_0_6; -.
DR OMA; SKQQKTC; -.
DR OrthoDB; 190791at2; -.
DR BioCyc; ASP62977:ACIAD_RS07900-MON; -.
DR BioCyc; MetaCyc:MON-37; -.
DR UniPathway; UPA00088; UER00179.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0046565; F:3-dehydroshikimate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR007742; NosD_dom.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF05048; NosD; 2.
DR SMART; SM00710; PbH1; 7.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Lyase; Quinate metabolism; Reference proteome.
FT CHAIN 1..486
FT /note="3-dehydroshikimate dehydratase"
FT /id="PRO_0000097137"
SQ SEQUENCE 486 AA; 52221 MW; 36D2E9073166C4C0 CRC64;
MKLTSLRVSL LALGLVTSGF AAAETYTVDR YQDDSEKGSL RWAIEQSNAN SAQENQILIQ
AVGKAPYVIK VDKPLPPIKS SVKIIGTEWD KTGEFIAIDG SNYIKGEGEK ACPGANPGQY
GTNVRTMTLP GLVLQDVNGV TLKGLDVHRF CIGVLVNRSS NNLIQHNRIS NNYGGAGVMI
TGDDGKGNPT STTTNNNKVL DNVFIDNGDG LELTRGAAFN LIANNLFTST KANPEPSQGI
EILWGNDNAV VGNKFENYSD GLQINWGKRN YIAYNELTNN SLGFNLTGDG NIFDSNKVHG
NRIGIAIRSE KDANARITLT KNQIWDNGKD IKRCEAGGSC VPNQRLGAIV FGVPALEHEG
FVGSRGGGVV IEPAKLQKTC TQPNQQNCNA IPNQGIQAPK LTVSKKQLTV EVKGTPNQRY
NVEFFGNRNA SSSEAEQYLG SIVVVTDHQG LAKANWAPKV SMPSVTANVT DHLGATSELS
SAVKMR
