BETA_RHILO
ID BETA_RHILO Reviewed; 550 AA.
AC Q985M5;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=mll7609;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB54037.1; -; Genomic_DNA.
DR RefSeq; WP_010914985.1; NC_002678.2.
DR AlphaFoldDB; Q985M5; -.
DR SMR; Q985M5; -.
DR STRING; 266835.14027083; -.
DR EnsemblBacteria; BAB54037; BAB54037; BAB54037.
DR GeneID; 66685136; -.
DR KEGG; mlo:mll7609; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 543793at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000000552; 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..550
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_0000205593"
FT REGION 529..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT BINDING 5..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ SEQUENCE 550 AA; 60125 MW; B3FC4F94EA6B5E21 CRC64;
MLEADFVIIG SGSAGSAMAY RLSEDGKHSV IVIEFGGSDI GPLIQMPSAL SIPLNMSLYD
WGFASEPEPH LGGRVLATPR GKVIGGSSSI NGMVYVRGHA RDFDHWAEEG ATGWGFADVL
PYFKRMEDND GGEDGWRGHG GPLHVQRGSR KNPLYGAFVE AGRQAGFELT DDYNGSKQEG
FGPMEQTISG GRRWSAASAY LKPALKRKNV SLVKGFARRV IIENQRAIGV EIEAHKQIQV
VKARREVIVA ASSINSPKIL MLSGIGPAEH LRENGIAVVA DRPGVGRNLQ DHMELYIQQE
STKPITLNSV LNPFSKALIG AQWLFFKSGL GATNHFEAAA FVRSRAGVDY PDIQYHFIPA
AVRYDGKAAA KSHGFQAHVG PMRSKSRGSV TLRSPDPKAK PVIRFNYMSH PDDWTEFRHC
IRLTREIFGQ SAFDAFRGQE ISPGSHVQSD DDLDVFIRDH AESAYHPCGT CKMGRADDVT
SVVDPECRVI GVDGLRVADS SIFPRVTNGN LNAPSIMTGE KASDHILGRT PLAPSNQEPW
INPRWQVSDR