ID A0A291P5A9_9GAMM Unreviewed; 563 AA.
AC A0A291P5A9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE Short=CDH {ECO:0000256|HAMAP-Rule:MF_00750};
DE Short=CHD {ECO:0000256|HAMAP-Rule:MF_00750};
DE EC=1.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00750};
DE AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE Short=BADH {ECO:0000256|HAMAP-Rule:MF_00750};
DE EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00750};
GN Name=betA1 {ECO:0000313|EMBL:ATJ82070.1};
GN Synonyms=betA {ECO:0000256|HAMAP-Rule:MF_00750};
GN ORFNames=BEI_1083 {ECO:0000313|EMBL:ATJ82070.1};
OS Halomonas beimenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ82070.1, ECO:0000313|Proteomes:UP000219993};
RN [1] {ECO:0000313|EMBL:ATJ82070.1, ECO:0000313|Proteomes:UP000219993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ82070.1,
RC ECO:0000313|Proteomes:UP000219993};
RX PubMed=29026163;
RA Chen Y.H., Lin S.S., Shyu Y.T.;
RT "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT Halomonas beimenensis through High-throughput Omics and Transposon
RT Mutagenesis Approaches.";
RL Sci. Rep. 7:13037-13037(2017).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00750, ECO:0000256|RuleBase:RU003969};
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:0000256|HAMAP-
CC Rule:MF_00750};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00750,
CC ECO:0000256|RuleBase:RU003969}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|HAMAP-Rule:MF_00750,
CC ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CP021435; ATJ82070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291P5A9; -.
DR KEGG; hbe:BEI_1083; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000219993; 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; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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 NCBIfam; TIGR01810; betA; 1.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00750};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00750}; NAD {ECO:0000256|HAMAP-Rule:MF_00750};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00750}; Reference proteome {ECO:0000313|Proteomes:UP000219993}.
FT DOMAIN 86..109
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 261..275
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 536..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
FT BINDING 8..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
SQ SEQUENCE 563 AA; 62533 MW; 350C4C8D67C50EFA CRC64;
MSQSREFDYV IIGAGSAGNV LATRLTEDPD VSVLLLEAGG PDHRFDFRTQ MPAALAYPLQ
GKRYNWAFET DPEPHMDGRR MECGRGKGLG GSSLINGMCY IRGNALDYDN WAKRDGLEDW
TYADCLPYFR KAETRDIGPD DYHGGDGPVS VTTPKEGNNP LYHAFIEAGQ QAGYPATEDV
NGYQQEGFGP MDRFVTPSGR RASTARGYLD QAKGRPNLTI ETRATTDVIT FEGRRATGVR
YERRGQQQEV RARREVLLCA GAIASPQILQ RSGVGPKDVL DELGITPVQV NENVGQHLQD
HLEMYIQYEC KKPISLYPAL KWWNQPKIGA EWLLFGKGVG ASNQFEAAGF IRSRDEEEWP
NLQYHFLPIA ISYNGKSAVQ AHGFQAHVGS MRSESEGRVR LTSRDPKAAP SILFNYMSTE
KDWQEFRDAI RLTREIIAQP AMDEYRGREI SPGPDVRSDA ELDAFVRQHA ETAYHPCGSC
RMGEGDDAVV DGAGRVHGVE ALRVVDASLF PVIPTGNLNA PTIMLAEKMA DKIRGRDPLP
RSDAPYYVAD GAPAQREPMR RLA
//
