ID D4E8Y0_SEROD Unreviewed; 554 AA.
AC D4E8Y0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 76.
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 ECO:0000313|EMBL:EFE93746.1};
GN ORFNames=HMPREF0758_4630 {ECO:0000313|EMBL:EFE93746.1};
OS Serratia odorifera DSM 4582.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE93746.1, ECO:0000313|Proteomes:UP000005723};
RN [1] {ECO:0000313|EMBL:EFE93746.1, ECO:0000313|Proteomes:UP000005723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE93746.1,
RC ECO:0000313|Proteomes:UP000005723};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2010) 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:EFE93746.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADBY01000058; EFE93746.1; -; Genomic_DNA.
DR RefSeq; WP_004965386.1; NZ_GG753567.1.
DR AlphaFoldDB; D4E8Y0; -.
DR STRING; 667129.HMPREF0758_4630; -.
DR HOGENOM; CLU_002865_7_1_6; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000005723; 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:UP000005723}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 259..273
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
FT BINDING 4..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
SQ SEQUENCE 554 AA; 61200 MW; EF99C7BF117B50E2 CRC64;
MEFDYIIIGA GSAGNVLATR LTEDADVSVL LLEAGGPDYR MDFRTQMPAA LAFPLQGRRY
NWAYETDPEP HMNNRRMECG RGKGLGGSSL INGMCYIRGN AMDFDNWATA PGLEDWSYLD
CLPYFRKAET RDIGPNDYHG GDGPVSVTTP KTGNNELFHA MIEAGVQAGY PRTDDLNGYQ
QEGFGPMDRT VTPKGRRAST ARGYLDQARS RPNLTIVTHA LTDHIDFAGK RAVGVSYLKG
EGNRIHSARA RREVLLCAGA IASPQILQRS GVGPAPLLNS LDIPLVHDLP GVGENLQDHL
EMYLQYACKK PVSLYPALQW FNQPKIGAEW LFNGSGVGAS NQFEAGGFIR SREEFAWPNI
QYHFLPVAIN YNGSNAVKEH GFQAHVGSMR SPSRGRVQVK SKDPRQHPSI LFNYMSSEQD
WQEFRDAIRI TREIMAQPAL DPYRGREISP GADVTSDEQL DAFIREHAET AFHPSCSCKM
GEDDMAVVDG QGRVHGMEGL RVVDASIMPQ IITGNLNATT IMIAEKIADR IRNRAALQRS
SADYYVAGDA PVRK
//
