ID A0A0Q6VFN8_9ACTN Unreviewed; 527 AA.
AC A0A0Q6VFN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KQV74279.1};
GN ORFNames=ASC61_04265 {ECO:0000313|EMBL:KQV74279.1};
OS Aeromicrobium sp. Root344.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV74279.1, ECO:0000313|Proteomes:UP000051702};
RN [1] {ECO:0000313|EMBL:KQV74279.1, ECO:0000313|Proteomes:UP000051702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root344 {ECO:0000313|EMBL:KQV74279.1,
RC ECO:0000313|Proteomes:UP000051702};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV74279.1, ECO:0000313|Proteomes:UP000051702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root344 {ECO:0000313|EMBL:KQV74279.1,
RC ECO:0000313|Proteomes:UP000051702};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQV74279.1}.
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DR EMBL; LMDH01000001; KQV74279.1; -; Genomic_DNA.
DR RefSeq; WP_056209805.1; NZ_LMDH01000001.1.
DR AlphaFoldDB; A0A0Q6VFN8; -.
DR STRING; 1736521.ASC61_04265; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000051702; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051702}.
FT DOMAIN 255..269
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 527 AA; 57156 MW; 367C9F5CF49704E1 CRC64;
MGDDSYDYIV IGSGSAGGVV AARLTEDPSV SVLLLEAGPE DDDDMIHLPA AFPSLFKTKW
DWGYQTTPQK QLDGRRADWP RMKALGGCSS MNAMIYIRGN RADYDEWRDS YGATGWGYDD
VLPYFKKAEG NTRLHDEFHG TSGPLHVEDR RYSHELSHAF VESAVTAGFK RNDDFNGAEQ
EGAGLYQVTC KKGRRWSVAD AYIHPARKRP NLTVLTEAFV TRIELEGTRA TGVTYRRAGA
THTARAKAEI VLSAGAIASP QMLMLSGIGP GAHLREHGID VRVDLPGVGQ NLQDHPVSGA
LFYTKDTTDL AEFLSLGNVL KAQKAGRGPL TSNVGEAGGF FRTRDDMAAP DMQFHVAPSG
FYDNGLHEPV RRGLTIASTL VRVESKGHIR LRSADPTWHP EIEAGYFADG ADLDAMIAGY
RTVQQIVSQG PLAKLIDEPW IPASAEPTTD EIVAAIGRLC QTLYHPVATC AMGTIEGSVV
DPDLKVHGVE GLRVADASVM PRVPRGNTNA PAIMVGEKAA DLIKESR
//
