ID   BETA_XANAC              Reviewed;         556 AA.
AC   Q8PPG8;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Choline dehydrogenase;
DE            Short=CHD;
DE            Short=CDH;
DE            EC=1.1.99.1;
GN   Name=betA; OrderedLocusNames=XAC0718;
OS   Xanthomonas axonopodis pv. citri (Citrus canker).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=92829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
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; AE011702; AAM35607.1; -; Genomic_DNA.
DR   RefSeq; NP_641071.1; -.
DR   GeneID; 1154789; -.
DR   GenomeReviews; AE008923_GR; XAC0718.
DR   KEGG; xac:XAC0718; -.
DR   NMPDR; fig|190486.1.peg.715; -.
DR   HOGENOM; Q8PPG8; -.
DR   OMA; Q8PPG8; GRRMECG.
DR   BioCyc; XAXO190486:XAC0718-MON; -.
DR   BRENDA; 1.1.99.1; 289771.
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_0000205608.
FT   NP_BIND       6     35       FAD (Probable).
FT   ACT_SITE    475    475       By similarity.
SQ   SEQUENCE   556 AA;  61266 MW;  026BB7F3EEE9B8DA CRC64;
     MQREYDYIII GAGSAGNVLA ARLTEDPGVT VLLLEAGGPD YRVDFRTQMP AALAFPLQGR
     RYNWAYETEP EPYMDNRRME CGRGKGLGGS SLINGMCYIR GNALDFDHWA KRPGLEDWSY
     RDVLPYFRKA ETRDIGANDY HGGDGPVSVA TPKNDNNVLF HAMVEAGVQA GYPRTGDLNG
     YQQEGFGPMD RTVTPRGRRA STARGYLDMA KPRDGLHIVT HATTDRILFA GKRAIGVHYL
     VGNSSEGIDA HARREVLVCA GAIASPQLLQ RSGVGAPDLL RALDVQLVHD LPGVGQNLQD
     HLEVYIQYAC TKPVSLYPAL QWWNQPAIGA QWLFAGTGTG ASNQFEAGGF IRTREEFDWP
     NIQYHFLPVA INYNGSNAVK EHGFQAHVGS MRTPSRGRVH AKSRDPRQHP SILFNYQSTD
     QDWQEFRDAI RITREIIAQP ALDAYRGREI SPSADCKTDA ELDAFVRSRA ETAYHPSCSC
     AMGTDAMAVV DGQGRVHGME GLRVIDASIM PRIITGNLNA TTIMIAEKIA DRVRGRTPLP
     RSTADYYIAG DAPVRG
//