ID A0A285NUQ9_9PSED Unreviewed; 579 AA.
AC A0A285NUQ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=betA {ECO:0000256|HAMAP-Rule:MF_00750};
GN ORFNames=SAMN05660463_02180 {ECO:0000313|EMBL:SNZ12747.1};
OS Pseudomonas sp. URIL14HWK12:I9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ12747.1, ECO:0000313|Proteomes:UP000232228};
RN [1] {ECO:0000313|EMBL:SNZ12747.1, ECO:0000313|Proteomes:UP000232228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ12747.1,
RC ECO:0000313|Proteomes:UP000232228};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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: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; OBEM01000004; SNZ12747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285NUQ9; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000232228; Unassembled WGS sequence.
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:UP000232228}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
FT BINDING 5..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
SQ SEQUENCE 579 AA; 63342 MW; B1EDD940E998C2F9 CRC64;
MKDYDYIIIG AGSAGNVLAA RLTEDAGVSV LLLEAGGPDH RLDFRTQMPA ALAFPLQGRR
YNWAYETDPE PHMNNRRMEC GRGKGLGGSS LINGMCYIRG NAMDLDNWAA QPGLEDWTYL
DCLPYYRKAE TRDAGPNDWH GGDGPVSVTT AKPGVNPLFE AMVEAGVQAG YPRTEDLNGY
QQEGFGPMDR TVTPNGRRAS TARGYLDVAK QRDTLTIVTH AMTDRILFEG KRASGVRYLV
GGQAHEARAR KEVLLCGGAI ASPQILQRSG VGPADLLQQH GVPVVHDLPG VGENLQDHLE
MYIQYACTQP VSLYPSLLLH NQPAIGAQWL FNGTGIGASN QFEAGGFIRS RPEFEWPNIQ
YHFLPVAINY NGSNGVREHG FQAHVGSMRS PSRGRVQIKS TDPHEHPSIL FNYMSSEQDW
QEFRDAIRIT REIIAQPALD AFRGREISPG PEVSTDEQLD AFVREHAETA FHPSCSCKMG
TDPMAVVDGQ GRVHGLQGLR VVDASIMPEI ITGNLNATTI MLAEKIADRI RGRQPLPRST
AKYYKANGAP VRGTPMRKTE HTAGMDALAT PAMAEPALS
//
