ID C4IUR4_BRUAO Unreviewed; 532 AA.
AC C4IUR4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EEP61807.1};
GN ORFNames=BAAA_7000282 {ECO:0000313|EMBL:EEP61807.1};
OS Brucella abortus str. 2308 A.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=641140 {ECO:0000313|EMBL:EEP61807.1, ECO:0000313|Proteomes:UP000003313};
RN [1] {ECO:0000313|EMBL:EEP61807.1, ECO:0000313|Proteomes:UP000003313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 A {ECO:0000313|EMBL:EEP61807.1,
RC ECO:0000313|Proteomes:UP000003313};
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:EEP61807.1}.
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DR EMBL; ACOR01000007; EEP61807.1; -; Genomic_DNA.
DR RefSeq; WP_002965689.1; NZ_ACOR01000007.1.
DR AlphaFoldDB; C4IUR4; -.
DR GeneID; 3827764; -.
DR Proteomes; UP000003313; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
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: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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 532 AA; 58227 MW; F1580158DA9EBB98 CRC64;
MTDTYDYIVV GAGTAGCALA NRLSADQNRS VLLLEAGGKD NYAWIHIPVG YLYCIGNPRT
DWCFTTEAEP GLNGRSLNYP RGKVLGGCSS INGMIYMRGQ ACDYDLWRQA GCDGWGWDDV
LPLFKKSEDY FAGASALHGM GGEWRVENAR LHWDILDAFR DAALAAGIPA TDDFNRGDNE
GVSYFKVNQK HGIRWNTAKA FLRPALDRKN LTVETGAHVR CIEIEGLRAT GVTFDQDGNI
RTVKARREVI LAAGAVGSPQ ILELSGIGRG DVLQQAGIPL KLERRQLGEN LQDHLQLRCA
YKVTGIATLN EKASTLVGKA MIGLEYLLRR SGPMAMAPSQ LGVFTRSDPS YETANLQYHV
QPLSLEKFGD AVHPFPTFTA SVCNLRPESR GSIHIKSPDH RAQPAIRPNY LATETDRRIA
ADAIRLTRHI VSQAPLQKYR PEEFKPGPNY ATQEDLEKAA GDIGTTIFHP VGTCRMGQDA
EAIVDPRLRF NGIAGLRVAD ASIMPAITSG NTNSPTLMIA EKAAQMIIAD NR
//
