ID BETA1_CHRSD Reviewed; 560 AA. AC Q1QXE1; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Choline dehydrogenase; DE Short=CHD; DE Short=CDH; DE EC=1.1.99.1; GN Name=betA; OrderedLocusNames=Csal_1514; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000285; ABE58867.1; -; Genomic_DNA. DR RefSeq; YP_573566.1; -. DR GeneID; 4029210; -. DR GenomeReviews; CP000285_GR; Csal_1514. DR KEGG; csa:Csal_1514; -. DR NMPDR; fig|290398.4.peg.2343; -. DR HOGENOM; Q1QXE1; -. DR OMA; Q1QXE1; PNLQYHF. DR BioCyc; CSAL290398:CSAL_1514-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 1 560 Choline dehydrogenase. FT /FTId=PRO_0000245316. FT NP_BIND 8 37 FAD (Probable). FT ACT_SITE 475 475 By similarity. SQ SEQUENCE 560 AA; 62246 MW; 8C6D127276CBC454 CRC64; MTQAREYDYI IIGAGSAGNV LATRLTEDPD VQVLLLEAGG PDYRFDFRTQ MPAALAYPLQ GKRYNWAFET DPEPYMNNRR MECGRGKGLG GSSLINGMCY LRGNALDYDN WAKIPGLEDW NYLQCLPYFK RAETRDIGPN DYHGGDGPVS VATPKEGNNE LYGAFIRAGI EAGYPATEDV NGYQQEGFGP MDRTTTPNGR RASTARGYLD IAKQRPNLTI ETHATTDVIE FEGKRAVGVS YERKGQAQRV RARREVLLCA GAIASPQILQ RSGVGNPEHL EEFDIPVVHE LPGVGENLQD HLEMYIQYEC KKPISLYPAL KWYNQPKIGA EWLFFGKGIG ASNQFEAAGF IRTNDQEEWP NLQYHFLPIA ISYNGKSAVQ AHGFQAHVGS MRSMSRGRIR LTSRDPKAAP SILFNYMSHD KDWQEFRDAI RITREIIEQP TMDEYRGREI SPGPNVQSDA ELDEFVRQHA ETAYHPAGSC KMGSADDAMA VVDGAGRVHG LEGLRVIDAS IMPVIATGNL NAPTIMIAEK MADKVRGRDP LPPAKVDYYV ANGAPARRRA //