ID BETA_XANC5 Reviewed; 556 AA. AC Q3BXK8; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 04-NOV-2008, entry version 25. DE RecName: Full=Choline dehydrogenase; DE Short=CHD; DE Short=CDH; DE EC=1.1.99.1; GN Name=betA; OrderedLocusNames=XCV0774; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., RA Bonas U., Bartels D., Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed RT by the complete genome sequence."; RL J. Bacteriol. 187:7254-7266(2005). CC -!- FUNCTION: Can catalyze the oxidation of choline to betaine CC aldehyde and betaine aldehyde to glycine betaine (By similarity). CC -!- CATALYTIC ACTIVITY: Choline + acceptor = betaine aldehyde + CC reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis CC via choline pathway; betaine aldehyde from choline (cytochrome c CC reductase route): step 1/1. CC -!- SIMILARITY: Belongs to the GMC oxidoreductase 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; AM039952; CAJ22405.1; -; Genomic_DNA. DR RefSeq; YP_362505.1; -. DR GeneID; 3729799; -. DR GenomeReviews; AM039952_GR; XCV0774. DR KEGG; xcv:XCV0774; -. DR NMPDR; fig|316273.3.peg.1262; -. DR HOGENOM; Q3BXK8; -. DR BioCyc; XCAM316273:XCV0774-MON; -. DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:HAMAP. DR GO; GO:0019285; P:glycine betaine biosynthetic process from c...; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00750; -; 1. DR InterPro; IPR011533; Choline_dehydrogenase. DR InterPro; IPR012132; GMC_OxRdtase. DR InterPro; IPR000172; GMC_OxRdtase_N. DR InterPro; IPR007867; GMC_OxRtase_C. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR PIRSF; PIRSF000137; Alcohol_oxidase; 1. DR TIGRFAMs; TIGR01810; betA; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase. FT CHAIN 1 556 Choline dehydrogenase. FT /FTId=PRO_0000258938. FT NP_BIND 6 35 FAD (Probable). FT ACT_SITE 475 475 By similarity. SQ SEQUENCE 556 AA; 61437 MW; 0950ACBCC7F4392A CRC64; MQREYDYIII GAGSAGNVLA ARLTEDPGVT VLLLEAGGPD YRLDFRTQMP AALAFPLQGR RYNWAYETEP EPYMDNRRME CGRGKGLGGS SLINGMCYIR GNALDFDHWA KRPGLEDWSY RDVLPYFRKA ETRDIGANDY HGGDGPVSVA TPKNDNNVLF HAMVEAGVQA GYPRTDDLNG YQQEGFGPMD RTVTPRGRRA STARGYLDMA KPRDGLHIVT HATTDRILFA GKRAIGVHYL VGNSSEGIDA HARREVLVCA GAIASPQLLQ RSGVGAPDLL RALDVQLVHD LPGVGQNLQD HLEVYIQYAC TKPVSLYPAL QWWNQPAIGA EWLFAGTGTG ASNQFEAGGF IRTREEFDWP NIQYHFLPVA INYNGSNAVK EHGFQAHVGS MRTPSRGRVH AKSRDPRQHP SILFNYQSTD QDWQEFRDAI RITREIIAQP ALDPYRGREI SPSADCKTDA ELDAFVRSRA ETAYHPSCSC AMGTDDMAVV DGQGRVHGME GLRVIDASIM PRIITGNLNA TTIMIAEKIA DRMRGRPPLP RSTADYYIAG DAPVRG //