ID   QUIA_XANCJ              Reviewed;         790 AA.
AC   Q9XD78;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Probable quinate dehydrogenase (quinone);
DE            EC=1.1.5.8;
GN   Name=qumA;
OS   Xanthomonas campestris pv. juglandis (Xanthomonas arboricola pv.
OS   juglandis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=195709;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C5;
RX   PubMed=10594704; DOI=10.1046/j.1365-2672.1999.00864.x;
RA   Lee Y.-A., Lo Y.-C., Yu P.-P.;
RT   "A gene involved in quinate metabolism is specific to one DNA homology
RT   group of Xanthomonas campestris.";
RL   J. Appl. Microbiol. 87:649-658(1999).
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   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000250};
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   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF109471; AAD38453.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XD78; -.
DR   SMR; Q9XD78; -.
DR   UniPathway; UPA00088; UER00177.
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; 4.
DR   SMART; SM00564; PQQ; 5.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   TIGRFAMs; TIGR03074; PQQ_membr_DH; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Oxidoreductase; PQQ; Quinate metabolism;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..790
FT                   /note="Probable quinate dehydrogenase (quinone)"
FT                   /id="PRO_0000205341"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          171..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  82897 MW;  B75F29B52A49FE6F CRC64;
     MLIALVGLIF LLGGARLASL GGSWYFLLMG LATALAGVLI VLRRPAGALV YGVAFALTLV
     WALWDAGLEF WPLVSRLMLP AAFAVLVALA WPALRRSRAL PTGRTAYGVA TVLALAVVAG
     IGGMFVPHPP VAGNAGPGMT AVPPGSVQQN WSAYGNTDGG SRFAALDQIN RSNGRPAAGS
     PGPTTPGEIA NSDGNGAEDQ LTPLQVGEKV FLCTPHNNLI ALDASTGKQL WRREINATSS
     VWQRCRGLGY FDADAALPAP SVANPSPIAA VTVAQGANCR RRLFTNTIDG RLIAVDADTG
     AFCQGFGSNG QVDLKAGLGA APDPFYQLTS PPLVAGTTVV GGRTRADDNV QTDMPGGVVR
     GSMWSPVRSA GLDPGNPHDR QAPAAGSSYV RSTPNVWAPM SYDAAMNTVF LPLGGPSTDL
     YGAERTALDH RYGASVLALD ATTGAEKWVY QTVHNDLWDF DLPMQPSLID FPNQDGSHTP
     AVVIGTKAGQ IYVLDRATGK PLTEVREVPV KGSDIAHEQY APTQPLSVGM PQIGTKHLTE
     SDMWGATAMD QMLCRIAFKQ MRYEGLYTAP GTDVSLSFPG SLGGMNWGGL STDPVHDVVF
     ANDMRLGLWV QMIPADTRKA EAAGGGEAVN TGMGAVPLKG TPYAVNKNRF LSALGIPCQA
     PPYGTLSAID LKTRSIAWQV PVGTVQDTGP FGIKMHLPIP IGMPTLGGTL STQGGLVFIA
     GTQDYYLRAF DSATGKELWK GRLPVGSQGG PITYVSHKTG KQYVVISAGG ARQSPDRGDY
     VIAYSLPDAH