ID A0A221VYQ5_9PSEU Unreviewed; 525 AA.
AC A0A221VYQ5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000313|EMBL:ASO18660.1};
DE EC=1.1.99.1 {ECO:0000313|EMBL:ASO18660.1};
GN Name=betA {ECO:0000313|EMBL:ASO18660.1};
GN ORFNames=AHOG_05035 {ECO:0000313|EMBL:ASO18660.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO18660.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO18660.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO18660.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) 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}.
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DR EMBL; CP022521; ASO18660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221VYQ5; -.
DR KEGG; ahg:AHOG_05035; -.
DR OrthoDB; 3659813at2; -.
DR Proteomes; UP000204221; Chromosome.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 2.
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:ASO18660.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000204221}.
FT DOMAIN 96..119
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 270..284
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 525 AA; 55508 MW; AD2A3DBCAF820646 CRC64;
MPQTDDRKRD LVYDTIIVGA GSAGAAVASR LTEDEQRRVL VLEAGPDYRS AETAADLQSI
EPGKIKLALH RAQTHTFPNL VATRSSAQPP LPYIRGRGVG GSSAINGLFA IRADVADLDG
WAAAGCTGWG YDDVLPLLTG MENDLDFPDE PYHGSTGPTP VRRPRREDFA TVEAAVDTAA
ERLGHPWAPD HNAPGSTGVS PYAFTSLGER RVSTNDAYLE PARSRPGLHV IGGAVVDRVL
LENGRAVGVR AIVDGEVAEF RAAEVVVSAG AVHSPAILQR SGIGPAADLR RLGIDPVVDL
PVGHGLQDHP GLVLLIALHG PPDYRGQPER GQLCLRFTTG VGDEVNDAMI ALPGAMGIGV
PVSGLIGWGN RVTSTGAVRL ASTDPTVDPT VDFDMLSTQD DLRRFRAVFD EMRAVARQPE
LQRIAVAMGF GPEMTLPETE MSDREFAEFA LTHVTDTVHA SGSCRMGDPN DPEVVVDPAG
RVLGVEGLRV ADASVFPWAT RANTNLTAIL VGEKIAASMH VGAAA
//
