ID A0A138A867_9ACTN Unreviewed; 536 AA.
AC A0A138A867;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Choline oxidase {ECO:0000313|EMBL:KXP06645.1};
GN ORFNames=AXK60_11275 {ECO:0000313|EMBL:KXP06645.1};
OS Tsukamurella pseudospumae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=239498 {ECO:0000313|EMBL:KXP06645.1, ECO:0000313|Proteomes:UP000070258};
RN [1] {ECO:0000313|Proteomes:UP000070258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15929 {ECO:0000313|Proteomes:UP000070258};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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:KXP06645.1}.
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DR EMBL; LSRF01000056; KXP06645.1; -; Genomic_DNA.
DR RefSeq; WP_068572431.1; NZ_LSRF01000056.1.
DR AlphaFoldDB; A0A138A867; -.
DR STRING; 239498.AXK60_11275; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000070258; 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; 3.30.410.40; -; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT DOMAIN 276..290
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 536 AA; 58540 MW; 8B647E1E4D97E720 CRC64;
MVRRAEGRSV TAPESGQEAF DYVVVGAGSA GAAVAARLSE DPTVTVCLLE AGPSDVGDEA
ILRLDRWMEL LESGYDWDYP IEPQENGNSF MRHARAKVLG GCSSHNSCIA FWAPREDLDS
WERDHGAAGW GADSVYRLYP RIETNDAPGE HHGRSGPVHI MTVPPNDPCG VALLDACEEV
GIPRAEFNSG TTVTNGANFF QINRRADGTR SSSSVSYLHP VLDRENLTIR TGAWAKRVVF
DTSGDQPRAT GVDITDNAFG RTTAVEARRE VIVSAGAIDS PKLLMLSGIG PADHLRETGV
DVLVDSPGVG AHLQDHPEGV IGFETSRPMV RESTQWWEIG IFTPTEYGLD RPDLMMHYGS
VPFDMHTLRQ GYPTAENTFC LTPNVTHARS RGTVRLRTRD FRDKPRVDPR YFTDAEGHDL
KVMIAGIRKA REIAEAGPLK DWVERELYPG PGAQTDAELA DYIRRTHNTV YHPAGTVRMG
AVDDPMSPLD PELRVKGVAG LRVADASVFP EHTTVNPNIT VMLVGERCAE LVAAGH
//
