ID A0A1E3SJL9_9MYCO Unreviewed; 517 AA.
AC A0A1E3SJL9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ODR02309.1};
GN ORFNames=BHQ21_22680 {ECO:0000313|EMBL:ODR02309.1};
OS Mycobacterium sherrisii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=243061 {ECO:0000313|EMBL:ODR02309.1, ECO:0000313|Proteomes:UP000094224};
RN [1] {ECO:0000313|Proteomes:UP000094224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1_M4 {ECO:0000313|Proteomes:UP000094224};
RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL Submitted (SEP-2016) 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:ODR02309.1}.
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DR EMBL; MIHC01000051; ODR02309.1; -; Genomic_DNA.
DR RefSeq; WP_069402546.1; NZ_MIHC01000051.1.
DR AlphaFoldDB; A0A1E3SJL9; -.
DR STRING; 243061.AWC25_00645; -.
DR Proteomes; UP000094224; 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: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.
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 Reference proteome {ECO:0000313|Proteomes:UP000094224}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 95..98
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"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 452..453
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 517 AA; 55979 MW; 90628AC1EEFA8A8C CRC64;
MDAKLRERYD VIVCGSGSSG SVIARRLAEK PDVTVLLLEA GGSDDVAAVT DRSQWPLNLG
SDRDWGFVAE PDPKLHGRSI AVSMGKVLGG GSGINAMVWA RGHRSDWDLF AAESGEPAWS
YESVAGLYRR LEDWGGVGEH DYRGRGGPVF MQPAPDPHPL TAATVNVARK QGIPTYQSPS
GRLMENLRGA AMTDLRARHG QRLSVFRTYT APYLGRPNLT VVPHALVTRL TFEGNRVTGV
DFVVDGAVVH AAASVEVVLS LGAIHTPKML MQSGFGDSDD LRQHGIAVRE HLPGVGRNLQ
DHHGFDCVWE FPEDLRTTGQ VEATLFWDSG LSDADGPDLF ACLGVFTKST PENVAKYGLP
QNGWILFGAP THPRSRGQLR LTGPNPADPI QIEANALSDP HDVKTGIACI ETLRQIGNAP
ELRPFVTREV MPGDLTGDEL ETYLRDAVTT YWHPSGTAKM GRDAMSVVDG QLKVYGVENL
RVADASIMPR ITSANTMAPC VVIGERAAQF IIAEHRL
//
