BETA_RHILW
ID BETA_RHILW Reviewed; 549 AA.
AC B5ZUG2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Rleg2_0776;
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304;
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI54071.1; -; Genomic_DNA.
DR RefSeq; WP_012556953.1; NC_011369.1.
DR AlphaFoldDB; B5ZUG2; -.
DR SMR; B5ZUG2; -.
DR STRING; 395492.Rleg2_0776; -.
DR EnsemblBacteria; ACI54071; ACI54071; Rleg2_0776.
DR KEGG; rlt:Rleg2_0776; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 543793at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000008330; 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_1000133337"
FT REGION 529..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 60411 MW; E3D1869F1DE37DBB CRC64;
MQADFVIIGS GSAGSALAYR LSEDGKNSVL VIEAGGSDFG PFIQMPAALA WPMSMKRYNW
GYLSEPEPNL NNRRITAPRG KVIGGSSSIN GMVYVRGHAE DFNRWEELGA GGWAYADVLP
YFKRMEHSHG GEEGWRGTDG PLHVQRGGFT NPLFRAFVEA GKQAGFETTE DYNGSKQEGF
GLMEQTIFSG RRWSAANAYL KPALKRKNVE IIYGFAQRIV IEDGRATGVE IERGGKIEVV
KANREVIVSA SSFNSPKLLM LSGIGPGEHL KEMGIEVKAD RPGVGANLQD HMEFYFQQVS
TKPVSLYSWL PWFWQGVAGA QWLLSKGGLG ASNQFEACAF LRSAPGLKQP DIQYHFLPVA
ISYDGKAAAK SHGFQVHVGY NLSKSRGSVT LRSPDPKADP VLRFNYMSHA EDWEKFRHCV
RLTRELFGQA AFDDYRGAEI QPGESVQSDE EIDAFLREHL ESAYHPCGTC KMGAKDDPMA
VVDPQTRVIG VEALRVADSS IFPHVTYGNL NGPSIMTGEK AADHILGKQP LARSNQEPWV
NPRAAVSDR