QUIA_ACIAD
ID QUIA_ACIAD Reviewed; 809 AA.
AC Q59086; Q6FBK4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Quinate/shikimate dehydrogenase (quinone);
DE EC=1.1.5.8;
DE AltName: Full=NAD(P)-independent quinate dehydrogenase;
GN Name=quiA; OrderedLocusNames=ACIAD1716;
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=8002591; DOI=10.1128/jb.176.24.7659-7666.1994;
RA Elsemore D.A., Ornston L.N.;
RT "The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains
RT quiA, the structural gene for quinate-shikimate dehydrogenase.";
RL J. Bacteriol. 176:7659-7666(1994).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
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).
CC -!- FUNCTION: Can act either on quinate or on shikimate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-quinate = 3-dehydroquinate + a quinol;
CC Xref=Rhea:RHEA:23672, ChEBI:CHEBI:24646, ChEBI:CHEBI:29751,
CC ChEBI:CHEBI:32364, ChEBI:CHEBI:132124; EC=1.1.5.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + shikimate = 3-dehydroshikimate + a quinol;
CC Xref=Rhea:RHEA:47048, ChEBI:CHEBI:16630, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:132124;
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3-dehydroquinate from D-quinate (PQQ route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By protocatechuate.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG68558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L05770; AAC37161.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68558.1; ALT_INIT; Genomic_DNA.
DR PIR; A55547; A55547.
DR RefSeq; WP_004926659.1; NC_005966.1.
DR AlphaFoldDB; Q59086; -.
DR SMR; Q59086; -.
DR STRING; 62977.ACIAD1716; -.
DR EnsemblBacteria; CAG68558; CAG68558; ACIAD1716.
DR GeneID; 45234103; -.
DR KEGG; aci:ACIAD1716; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_1_0_6; -.
DR OrthoDB; 1377603at2; -.
DR BioCyc; ASP62977:ACIAD_RS07910-MON; -.
DR BioCyc; MetaCyc:MON-28; -.
DR UniPathway; UPA00088; UER00177.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047519; F:quinate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
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 CDD; cd10280; PQQ_mGDH; 1.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017511; PQQ_mDH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR PANTHER; PTHR32303:SF4; PTHR32303:SF4; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03074; PQQ_membr_DH; 1.
DR PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Oxidoreductase; PQQ; Quinate metabolism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..809
FT /note="Quinate/shikimate dehydrogenase (quinone)"
FT /id="PRO_0000205340"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 809 AA; 88196 MW; 71F67CEBEA62BFCB CRC64;
MSDPQEKSHI ILKVWCFILG LALLITGAFY VIGGGKLISL GGSWYFLIAG LMITTSAFFM
FKKKATGVWL YALAFIGTVI WALIDAGFEF WPLHSRLMFP AGLFAAVMLT LPSIRKYQYQ
TPMSAPAYVI GGLTVLGMLG GLYGMFIPHE TVKASGEELP LVPVDPAKKQ VNWDHYGNDA
GGSRFVALDQ INRNNVSKLK EAWRFRTGDF TTGTGNGAED QMTPLQVGNK VFLCTPHNNI
FAIDADSGKQ LWKAEVNSTA DAWERCRGVA YFDSTQPLVQ PTLAGATPVA ALAANTECPR
RVYTNTVDGR LIAVNADTGA RCKDFGVNGT VNLHEGLGEN TKAPRFEVTS APTIAGTTIV
VGSRIADNVA ADMPGGVIRA YDVITGKLRW AFDPRNPDPN YVLKPGEIYK RSSTNSWAAM
SYDPQMNTVF LPMGSSSVDV WGGNRTAADH KYNTSVLALD ATTGKEKWVY NTVHNDLWDF
DLPMQPSLVD FPMKDGTTKP AVVIGTKSGQ FYVLDRVTGK PLTKVIEQPI KVADIPGEQY
SKTQPRSVEM PQIGNQTLKE SDMWGATPFD QLMCRINFKS MRYDGLYTAP GTDVSLSFPG
SLGGMNWGSI AFDPTHRYMF VNDMRLGLWI QLIKQTPEDI KIQANGGEKV NTGMGAVPMK
GTPYKVNKNR FMSALGIPCQ KPPFGTMTAI DMKTRQVAWQ VPLGTIQDTG PMGIKMGLKA
PIGMPTIGGP MATQGGLVFF AATQDYYLRA FNSSNGKELW KARLPVGSQG TPMSYMSPKT
GKQYVVVSAG GARQSPDHGD YVIAYALEK
