ID BETA_ECOL6 Reviewed; 556 AA. AC Q8FKI9; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 16-JUN-2009, entry version 47. DE RecName: Full=Choline dehydrogenase; DE Short=CHD; DE Short=CDH; DE EC=1.1.99.1; GN Name=betA; OrderedLocusNames=c0431; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). 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 -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein CC (By similarity). 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; AE014075; AAN78912.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_752368.2; -. DR GeneID; 1036260; -. DR GenomeReviews; AE014075_GR; c0431. DR KEGG; ecc:c0431; -. DR NMPDR; fig|199310.1.peg.412; -. DR HOGENOM; Q8FKI9; -. DR OMA; Q8FKI9; PNLQYHF. DR BRENDA; 1.1.99.1; 292881. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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 Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane; KW Oxidoreductase. FT CHAIN 1 556 Choline dehydrogenase. FT /FTId=PRO_0000205588. FT NP_BIND 4 33 FAD (Probable). FT ACT_SITE 473 473 By similarity. SQ SEQUENCE 556 AA; 61899 MW; 7958C0BD6D20BFC1 CRC64; MQFDYIIIGA GSAGNVLATR LTEDPNTTVL LLEAGGPDYR FDFRTQMPAA LAFPLQGKRY NWAYETEPEP FMNNRRMECG RGKGLGGSSL INGMCYIRGN ALDLDNWAQE PSLENWSYLD CLPYYRKAET RDVGENDYHG GDGPVSVTTS KPGVNPLFEA MIEAGMQAGY PRTDDLNGYQ QEGFGPMDRT VTPHGRRAST ARGYLDQAKS RPNLTIRTHA MTDHIIFDGK RAVGVEWLEG DSTIPTRAAA NKEVLLCAGA IASPQILQRS GVGNAELLAE FDIPLVHELP GVGENLQDHL EMYLQYECKE PVSLYPALQW WNQPRIGAEW LFGGTGVGAS NHFEAGGFIR SREEFAWPNI QYHFLPVAIN YNGSNAVKEH GFQCHVGSMR SPSRGHVRIK SRDPHQHPGI LFNYMSHEQD WQEFRDAIRI TREIMHQPAL DQYRGREISP GVECQTDEQL DEFVRNHAET AFHPCGTCKM GYDEMAVVDG EGRVHGLEGL RVVDASIMPQ IITGNLNATT IMIGEKIADM IRGKEALPRS TAGYFVANGM PVRAKK //