BETA_BURPS
ID BETA_BURPS Reviewed; 565 AA.
AC Q63KK7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750};
DE Short=CDH {ECO:0000255|HAMAP-Rule:MF_00750};
DE Short=CHD {ECO:0000255|HAMAP-Rule:MF_00750};
DE EC=1.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750};
DE Short=BADH {ECO:0000255|HAMAP-Rule:MF_00750};
DE EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00750};
GN Name=betA {ECO:0000255|HAMAP-Rule:MF_00750}; OrderedLocusNames=BPSS1355;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine. Catalyzes the oxidation of choline to betaine aldehyde and
CC betaine aldehyde to glycine betaine at the same rate.
CC {ECO:0000255|HAMAP-Rule:MF_00750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC ChEBI:CHEBI:17499; EC=1.1.99.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00750};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00750};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00750};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00750}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00750}.
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DR EMBL; BX571966; CAH38826.1; -; Genomic_DNA.
DR RefSeq; WP_009940671.1; NZ_CP009537.1.
DR RefSeq; YP_111365.1; NC_006351.1.
DR AlphaFoldDB; Q63KK7; -.
DR SMR; Q63KK7; -.
DR STRING; 272560.BPSS1355; -.
DR EnsemblBacteria; CAH38826; CAH38826; BPSS1355.
DR KEGG; bps:BPSS1355; -.
DR PATRIC; fig|272560.51.peg.4659; -.
DR eggNOG; COG2303; Bacteria.
DR OMA; NHFESCA; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00750; Choline_dehydrogen; 1.
DR InterPro; IPR011533; BetA.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 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 FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..565
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_0000258919"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT BINDING 7..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ SEQUENCE 565 AA; 62703 MW; 6990A10A40FD48C0 CRC64;
MTTREFDYII CGAGSAGNVL ATRLTEDPGV TVLLLEAGGP DYRFDFRTQM PAALAYPLQG
RRYNWAYETD PEPHMNHRRM ECGRGKGLGG SSLINGMCYI RGNALDYDNW ATHKALEDWA
YLDCLPYFRK AETRDVGPND YHGGDGPVSV TTSKPGVNPL FEAMVEAGVQ AGYPRTDDLN
GYQQEGFGPM DRTVTPRGRR ASTARGYLDQ ARARPNLEIV THALADRILF SGKRATGVTF
LHGSARVTAH ARREVLVCSG AIASPQLLQR SGVGPGEWLR ELDIPVVLDL PGVGRNLQDH
LEMYIQFECK EPVSLYPALK WWNQPKIGLE WMLNGTGLGA SNHFEAGGFI RTRDDDPWPN
IQYHFLPVAI NYNGSNAIEM HGFQAHVGSM RSPSRGRVKL KSRDPHAHPS ILFNYMAEAL
DWREFRDAIR ATREIMRQPA LDRFRGRELN PGADLKSDNE LDTFVRARAE TAFHPSCSCK
MGYDDMAVVD NEGRVHGIDG LRVVDASIMP IITTGNLNAP TIMIAEKIAD RIRQHKPLER
SNAQYYVANG APARGGKPAR APAVV
