BETA_RHIME
ID BETA_RHIME Reviewed; 549 AA.
AC P54223;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=R00947;
GN ORFNames=SMc00093;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=102F34;
RX PubMed=9141699; DOI=10.1099/00221287-143-4-1369;
RA Pocard J.A., Vincent N., Boncompagni E., Tombras Smith L., Poggi M.-C.,
RA Le Rudulier D.;
RT "Molecular characterization of the bet genes encoding glycine betaine
RT synthesis in Sinorhizobium meliloti 102F34.";
RL Microbiology 143:1369-1379(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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, ECO:0000269|PubMed:9141699}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9141699};
CC Peripheral membrane protein {ECO:0000269|PubMed:9141699}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00750}.
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DR EMBL; U39940; AAC13369.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45519.1; -; Genomic_DNA.
DR RefSeq; NP_385053.1; NC_003047.1.
DR RefSeq; WP_010968940.1; NC_003047.1.
DR AlphaFoldDB; P54223; -.
DR SMR; P54223; -.
DR STRING; 266834.SMc00093; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblBacteria; CAC45519; CAC45519; SMc00093.
DR GeneID; 61602413; -.
DR KEGG; sme:SMc00093; -.
DR PATRIC; fig|266834.11.peg.2346; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR OMA; NHFESCA; -.
DR BioCyc; MetaCyc:MON-244; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_0000205594"
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"
FT CONFLICT 267
FT /note="A -> R (in Ref. 1; AAC13369)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..424
FT /note="RHCVRLTR -> DLRAVTG (in Ref. 1; AAC13369)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="Q -> E (in Ref. 1; AAC13369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 61291 MW; 29BE064F40CB88F4 CRC64;
MQADFVIIGS GSAGSALAYR LSEDGRNSVI VLEFGGSDVG PFIQMPAALA WPMSMNRYNW
GYLSEPEPNL NNRRITAPRG KVIGGSSSIN GMVYVRGHSE DFNRWEELGA QGWAYADVLP
YYKRMEHSHG GEEGWRGTDG PLHVQRGPVK NPLFHAFIEA GKEAGFEVTE DYNGSKQEGF
GLMEQTTWRG RRWSAASAYL RPALKRPNVE LIRCFARKIV IENGRATGVE IERGGRIEVV
KANREVIVSA SSFNSPKLLM LSGIGPAAHL KEMGIDVKVD RPGVGQNLQD HMEFYFQQVS
TKPVSLYSWL PWFWQGVAGA QWLFFKRGLG ISNQFESCAF LRSAPGVKQP DIQYHFLPVA
ISYDGKAAAK SHGFQVHVGY NLSKSRGNVS LRSSDPKADP VIRFNYMSHP EDWEKFRHCV
RLTREIFGQK AFDLYRGPEI QPGEKVQTDE EIDGFLREHL ESAYHPCGTC KMGAKDDPMA
VVDPETRVIG VDGLRVADSS IFPHITYGNL NAPSIMTGEK SADHILGRQP LARSNQEPWI
NPRWAVSDR
