ID BETA_BURPS Reviewed; 565 AA. AC Q63KK7; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 25-NOV-2008, entry version 35. DE RecName: Full=Choline dehydrogenase; DE Short=CHD; DE Short=CDH; DE EC=1.1.99.1; GN Name=betA; OrderedLocusNames=BPSS1355; OS Burkholderia pseudomallei (Pseudomonas pseudomallei). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). 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; BX571966; CAH38826.1; -; Genomic_DNA. DR RefSeq; YP_111365.1; -. DR GeneID; 3096018; -. DR GenomeReviews; BX571966_GR; BPSS1355. DR KEGG; bps:BPSS1355; -. DR NMPDR; fig|272560.3.peg.1381; -. DR HOGENOM; Q63KK7; -. DR BioCyc; BPSE272560:BPSS1355-MON; -. DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:HAMAP. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0006066; P:cellular alcohol metabolic process; IEA:InterPro. 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 1 565 Choline dehydrogenase. FT /FTId=PRO_0000258919. FT NP_BIND 7 36 FAD (Probable). FT ACT_SITE 474 474 By similarity. SQ SEQUENCE 565 AA; 62703 MW; 6990A10A40FD48C0 CRC64; MTTREFDYII CGAGSAGNVL ATRLTEDPGV TVLLLEAGGP DYRFDFRTQM PAALAYPLQG RRYNWAYETD PEPHMNHRRM ECGRGKGLGG SSLINGMCYI RGNALDYDNW ATHKALEDWA YLDCLPYFRK AETRDVGPND YHGGDGPVSV TTSKPGVNPL FEAMVEAGVQ AGYPRTDDLN GYQQEGFGPM DRTVTPRGRR ASTARGYLDQ ARARPNLEIV THALADRILF SGKRATGVTF LHGSARVTAH ARREVLVCSG AIASPQLLQR SGVGPGEWLR ELDIPVVLDL PGVGRNLQDH LEMYIQFECK EPVSLYPALK WWNQPKIGLE WMLNGTGLGA SNHFEAGGFI RTRDDDPWPN IQYHFLPVAI NYNGSNAIEM HGFQAHVGSM RSPSRGRVKL KSRDPHAHPS ILFNYMAEAL DWREFRDAIR ATREIMRQPA LDRFRGRELN PGADLKSDNE LDTFVRARAE TAFHPSCSCK MGYDDMAVVD NEGRVHGIDG LRVVDASIMP IITTGNLNAP TIMIAEKIAD RIRQHKPLER SNAQYYVANG APARGGKPAR APAVV //