ID   BETA_XANCP              Reviewed;         556 AA.
AC   Q8P5D7;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Choline dehydrogenase;
DE            Short=CHD;
DE            Short=CDH;
DE            EC=1.1.99.1;
GN   Name=betA; OrderedLocusNames=XCC3404;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(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   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
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DR   EMBL; AE012459; AAM42674.1; -; Genomic_DNA.
DR   RefSeq; NP_638750.1; -.
DR   GeneID; 999936; -.
DR   GenomeReviews; AE008922_GR; XCC3404.
DR   KEGG; xcc:XCC3404; -.
DR   HOGENOM; Q8P5D7; -.
DR   OMA; Q8P5D7; GRRMECG.
DR   BioCyc; XCAM190485:XCC3404-MON; -.
DR   BRENDA; 1.1.99.1; 281360.
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    556       Choline dehydrogenase.
FT                                /FTId=PRO_0000205609.
FT   NP_BIND       6     35       FAD (Probable).
FT   ACT_SITE    475    475       By similarity.
SQ   SEQUENCE   556 AA;  61445 MW;  12409448073F6478 CRC64;
     MQREYDYIII GAGSAGNVLA ARLTEDPGVS VLLLEAGGPD YRLDFRTQMP AALAFPLQGR
     RYNWAYETEP EPHMDNRRME CGRGKGLGGS SLINGMCYIR GNALDFDHWA KRPGLEDWGY
     RDVLPYFRKA ETRDIGANDY HGGEGPVSVA TPKNDNNVLF QAMVDAGVQA GYPRTDDLNG
     YQQEGFGPMD RTVTPQGRRA STARGYLDMA KPRDSLHIVT HATTDRILFA GKRAVGVHYL
     VGNSSEGIDA HARREVLVCA GAIASPQLLQ RSGVGAPDLL RALDVQLVHD LPGVGQNLQD
     HLEVYMQYAC TKPVSLYPAL QWWNQPAIGA EWLFAGTGTG ASNQFEAGGF IRTREEFDWP
     NIQYHFLPVA INYNGSNAVK EHGFQAHVGS MRTPSRGRVH ARSRDPRQHP SILFNYQSTD
     QDWQEFRDAI RITREIIAQP ALDPYRGREI SPSADCKTDA ELDAFVRARA ETAYHPSCSC
     AMGTDDMAVV DGQGRVHGME GLRVIDASIM PRIITGNLNA TTIMIAEKIV DRIRGRAPLP
     RSTADYYVAG DAPVRR
//