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 16-JUN-2009, entry version 57. DE RecName: Full=Probable quinate dehydrogenase [Pyrroloquinoline-quinone]; DE EC=1.1.99.25; 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 MEDLINE=20063481; PubMed=10594704; RX 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: Quinate + pyrroloquinoline-quinone = 3- CC dehydroquinate + reduced pyrroloquinoline-quinone. CC -!- COFACTOR: PQQ (By similarity). CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3-dehydroquinate from quinate (PQQ route): step 1/1. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF109471; AAD38453.1; -; Genomic_DNA. DR BRENDA; 1.1.99.25; 295646. DR GO; GO:0016021; C:integral to 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:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0047519; F:quinate dehydrogenase (pyrroloquinoline-qui...; IEA:EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR017511; PQQ-dep_membr-bd_DH. DR InterPro; IPR019556; PQQ-dependent_C. DR InterPro; IPR019551; PQQ-dependent_N. DR InterPro; IPR018391; PQQ_beta_propeller_repeat. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR011047; Quino_AlcDH-like. DR InterPro; IPR001479; Quinoprotein_DH_CS. DR Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1. DR Pfam; PF01011; PQQ; 4. DR Pfam; PF10535; PQQ_C; 1. DR Pfam; PF10527; PQQ_N; 1. DR SMART; SM00564; PQQ; 5. DR TIGRFAMs; TIGR03074; PQQ_membr_DH; 1. DR PROSITE; PS00363; BACTERIAL_PQQ_1; FALSE_NEG. DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1. PE 3: Inferred from homology; KW Cell membrane; Membrane; Oxidoreductase; PQQ; Quinate metabolism; KW Transmembrane. FT CHAIN 1 790 Probable quinate dehydrogenase FT [Pyrroloquinoline-quinone]. FT /FTId=PRO_0000205341. FT TRANSMEM 22 42 Potential. FT TRANSMEM 48 68 Potential. FT TRANSMEM 77 94 Potential. FT TRANSMEM 106 126 Potential. 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 //