BETA_SINMW
ID BETA_SINMW Reviewed; 549 AA.
AC A6U6Y8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Smed_0562;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000738; ABR59418.1; -; Genomic_DNA.
DR RefSeq; WP_011974764.1; NC_009636.1.
DR RefSeq; YP_001326253.1; NC_009636.1.
DR AlphaFoldDB; A6U6Y8; -.
DR SMR; A6U6Y8; -.
DR STRING; 366394.Smed_0562; -.
DR PRIDE; A6U6Y8; -.
DR EnsemblBacteria; ABR59418; ABR59418; Smed_0562.
DR GeneID; 61609838; -.
DR KEGG; smd:Smed_0562; -.
DR PATRIC; fig|366394.8.peg.3654; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 543793at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000001108; Chromosome.
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.
FT CHAIN 1..549
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_1000046572"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT BINDING 4..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ SEQUENCE 549 AA; 61179 MW; 97AF35082E32BEB7 CRC64;
MQADFVIIGS GSAGSALAYR LSEDGANSVV VLEFGGSDVG PFIQMPAALA WPMSMNRYNW
GYLSEPEPNL NNRRITAPRG KVIGGSSSIN GMVYVRGHSE DFDRWEELGA KGWAYADVLP
YYKRMEHSHG GEEGWRGTDG PLHVQRGPVK NPLFHAFIEA GKQAGFEVTE DYNGSKQEGF
GLMEQTTWRG RRWSAASAYL RPALKRPNVE LVRCFARKIV IENGRATGVE IERGGRTEVV
RANREVIVSA SSFNSPKLLM LSGIGPAAHL QEMGIDVKAD RPGVGQNLQD HMEFYFQQVS
TKPVSLYSWL PWFWQGVAGA QWLFFKRGLG ISNQFESCAF LRSAPGVKQP DIQYHFLPVA
ISYDGKAAAK SHGFQVHVGY NLSKSRGDVT LRSSDPKADP VIRFNYMSHP EDWEKFRHCV
RLTREIFGQK AFDLYRGPEI QPGEKVRTDE EIDAFLREHL ESAYHPCGTC KMGAKDDPMA
VVDPETRVIG VDGLRVADSS IFPHITYGNL NAPSIMTGEK AADHILGKQP LARSNQEPWI
NPRWAVSDR