ID A0A0P9Z8L6_PSESX Unreviewed; 568 AA.
AC A0A0P9Z8L6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=ALO94_201070 {ECO:0000313|EMBL:KPY56923.1};
OS Pseudomonas syringae pv. spinaceae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY56923.1, ECO:0000313|Proteomes:UP000050384};
RN [1] {ECO:0000313|EMBL:KPY56923.1, ECO:0000313|Proteomes:UP000050384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY56923.1,
RC ECO:0000313|Proteomes:UP000050384};
RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT "Genome announcement of multiple Pseudomonas syringae strains.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPY56923.1}.
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DR EMBL; LJRI01001588; KPY56923.1; -; Genomic_DNA.
DR RefSeq; WP_057428767.1; NZ_LJRI01001588.1.
DR AlphaFoldDB; A0A0P9Z8L6; -.
DR PATRIC; fig|264459.3.peg.3346; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000050384; 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}.
FT DOMAIN 86..109
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 263..277
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 477
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 568 AA; 62778 MW; A680FBAC0CF07006 CRC64;
MTTQSEYDYI IIGAGSAGNT LAARLTEDAG VTVLLLEAGG PDYRLDFRTQ MPAALAFPLQ
GRRYNWAYET EPEPHMDNRR MECGRGKGLG GSSLINGMCY IRGNAMDYDG WAKEPGLEDW
SYLDCLPYFR KAETRDIGPN DYHGGEGPVS VTTPKAGNNP LFHAMVEAGV QAGFPRTDDL
NGYQQEGFGP MDRTVTPKGR RASTARGYLD EAKKRDTLSI VTHALTDRIL FEGKRAVGVA
YLVGDSDTRI EVRARKEVLL CGGAIASPQI LQRSGVGPAE VLNKLDIPVV HDLPGVGQNL
QDHLEMYLQY ACTQPVSLYP SLKWWNQPAI GAEWMFLGTG IGASNQFEAG GFIRSSEAFE
WPNIQYHFLP VAINYNGTKG VQEHGFQAHV GSMRSPSRGR VNVKSKDPRE YPSILFNYMA
SDQDWQEFRD GIRLTREIMQ QPALDPYRGR EISPGIDVQS DEALDQFVRE HAETAYHPSC
SCKMGTDEMA VVDGQGRVHG MQNLRVVDAS IMPIITNGNL NAPTIMIAEK IADKIRGRQP
LPRSTADYFV AGDKPARGKP LREISHQA
//
