ID   BETA_PSE14              Reviewed;         568 AA.
AC   Q48CM7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Choline dehydrogenase;
DE            Short=CHD;
DE            Short=CDH;
DE            EC=1.1.99.1;
GN   Name=betA; OrderedLocusNames=PSPPH_4766;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ35413.1; -; Genomic_DNA.
DR   RefSeq; YP_276866.1; -.
DR   GeneID; 3557996; -.
DR   GenomeReviews; CP000058_GR; PSPPH_4766.
DR   KEGG; psp:PSPPH_4766; -.
DR   NMPDR; fig|264730.3.peg.4707; -.
DR   HOGENOM; Q48CM7; -.
DR   OMA; Q48CM7; PNLQYHF.
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    568       Choline dehydrogenase.
FT                                /FTId=PRO_0000258930.
FT   NP_BIND       8     37       FAD (Probable).
FT   ACT_SITE    477    477       By similarity.
SQ   SEQUENCE   568 AA;  62732 MW;  EDA8D9020368A32B CRC64;
     MTTQSEYDYI IIGAGSAGNT LAARLTEDAG VTVLLLEAGG PDYRLDFRTQ MPAALAFPLQ
     GRRYNWAYET EPEPHMNNRR MECGRGKGLG GSSLINGMCY IRGNAMDYDG WAKEPGLEDW
     SYLDCLPYFR KAETRDIGPN DYHGGEGPVS VTKPKAGNNP LFHAMVEAGV QAGFPRTDDL
     NGYQQEGFGP MDRTVTPNGR RASTARGYLD EAKKRSTLTI VTHALTDRIL FEGKRAVGVA
     YLVGDSDTRI QARARKEVLL CGGAIASPQI LQRSGVGPAE VLNKLDIPVV HDLPGVGQNL
     QDHLEMYLQY ACTQPVSLYP SLKWWNQPAI GAKWMFLGTG IGASNQFEAG GFIRSSEAFE
     WPNIQYHFLP VAINYNGTKG VQEHGFQAHV GSMRSPSRGR VQVKSKDPRE YPSILFNYMS
     SEQDWQEFRD GIRLTREIMQ QPALDPYRGR EISPGIDVQS DEALDQFVRE HAETAYHPSC
     SCKMGTDEMA VVDGQGRVHG LQSLRVVDAS IMPIITTGNL NAPTIMIAEK IADKIRGRQP
     LPRSTADYFV AGDKPARGKP LREISHQA
//