ID A0A3S0TKD6_9SPHN Unreviewed; 531 AA.
AC A0A3S0TKD6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=FAD-binding protein {ECO:0000313|EMBL:RUN78406.1};
GN ORFNames=EJC47_00570 {ECO:0000313|EMBL:RUN78406.1};
OS Sphingomonas sp. TF3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2495580 {ECO:0000313|EMBL:RUN78406.1, ECO:0000313|Proteomes:UP000275325};
RN [1] {ECO:0000313|EMBL:RUN78406.1, ECO:0000313|Proteomes:UP000275325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF3 {ECO:0000313|EMBL:RUN78406.1,
RC ECO:0000313|Proteomes:UP000275325};
RA Afonin A., Vasilieva E., Akhtemova G., Zhukov V.;
RT "The Draft Genome Sequence of a Sphingomonas sp strain TF3.";
RL Submitted (DEC-2018) 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:RUN78406.1}.
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DR EMBL; RWKS01000001; RUN78406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0TKD6; -.
DR Proteomes; UP000275325; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000275325}.
FT DOMAIN 78..101
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 251..265
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 88..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 531 AA; 56136 MW; 24B48BBD466E0ACB CRC64;
MSSYDYVVIG AGSAGCVLAT RLVEAGKSVL LLESGPRDRD FFISMPGGIQ KIAKKLAWHL
WTEPEAAAGG RRVYMKQGRL LGGGSSINGM VYIRGQAEDY DQWQASGCEG WGWDDVLPVF
KRGEANQKYS EPFHGANGPL KVSDAGYHHP LSYAFVRAGQ EAGLPYNDDF NGASQEGVGF
YQTTSAAGRR QSAAVAFLSR VRDNPLLTLR CETHVEAVTM ENGAATGVRY RGSDGAVQQA
AAREEVIVAA GAFGSPKVLQ LSGIGPEPLL AEHGIPVVRA LAGVGENFQD HYQAGVYGQT
RHPISLLGAD KGLTAVRHGL QWLMFKSGLL TSNIVESGGF VSTDGSGRPD IQFTVVAALT
GDADRPPLPG HGISISPCVL RPQARGSVRI SGRDAAAPVR INGNVLGHAD DMATLVRGVR
LARRILHSPS LAQLLDCELA PGHGPDDELS DAAIETHIAS VVKTVYHPCG TCKMGPASDP
AAVVDAKLRV HGVPRLRVAD ASIMPNLVSG NTNAPAIMIG ERCADFVLQR A
//
