ID A0A0N8KC97_9RHOB Unreviewed; 547 AA.
AC A0A0N8KC97;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KPQ05130.1};
DE EC=1.1.99.1 {ECO:0000313|EMBL:KPQ05130.1};
GN Name=betA-2 {ECO:0000313|EMBL:KPQ05130.1};
GN ORFNames=HLUCCA12_15935 {ECO:0000313|EMBL:KPQ05130.1};
OS Rhodobacteraceae bacterium HLUCCA12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ05130.1, ECO:0000313|Proteomes:UP000050476};
RN [1] {ECO:0000313|EMBL:KPQ05130.1, ECO:0000313|Proteomes:UP000050476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ05130.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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, 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:KPQ05130.1}.
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DR EMBL; LJSV01000023; KPQ05130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8KC97; -.
DR STRING; 1666916.HLUCCA12_15935; -.
DR PATRIC; fig|1666916.3.peg.1551; -.
DR Proteomes; UP000050476; Unassembled WGS sequence.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000313|EMBL:KPQ05130.1}.
FT DOMAIN 90..113
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 262..276
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 547 AA; 59097 MW; 2F296956D2EA0710 CRC64;
MSHEISGSRS SVYDFVIVGA GSAGCVLANR LSADPACRVL LIEAGGWDRD PFIKIPIGWG
RIMQKRLHDW GYETEPDPML GIPAMECMRG RVIGGSSSIN AMAYVRGHAH DFDRWASYGL
PSLGYENALR YFRRQETWED GASEFRGGAG PLSTIRATYA DPLAEAFLEA ADATGMPWTD
DYNGAQQEGF SVLQSTIRNG WRCSAADAYL RPALGRPNLT VTTNSVVTSV EFSGDRAVSV
AWQRSGRRHR AHAENRIILC AGAINTPQIL MLSGIGDSEV LSHHGIETRV HLPGVGRNLQ
DHASVAVEFA RKGRGPFVEN MRMDRLVAGL TTAYMAGRGF GTDLPSGWTA FLRTPLAGSM
PDIQLIFRAV PLSANPWFPG VRKPFLDGFA IRAVLLRPKS RGHVALRSAD PFDKVRIVQN
LLHAPGDRAV LREGLRMIPQ FAGHKVLEGF IDRQLAPGPG QWSDQGLDAH ILGTVSTAHH
PAGTCRMGLG GDGCDVSAPD FSVYGTQRLS VVDASVFPDL VGGNINAAVI MLAEMASDFL
SGKHTSA
//
