ID F5YX15_MYCSD Unreviewed; 450 AA.
AC F5YX15;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AEF34102.1};
GN OrderedLocusNames=JDM601_0102 {ECO:0000313|EMBL:AEF34102.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF34102.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF34102.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF34102.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CP002329; AEF34102.1; -; Genomic_DNA.
DR AlphaFoldDB; F5YX15; -.
DR STRING; 875328.JDM601_0102; -.
DR KEGG; mjd:JDM601_0102; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_11; -.
DR OMA; WAIRECT; -.
DR Proteomes; UP000009224; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009224}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 450 AA; 46403 MW; 75FCCBBFCD8C8483 CRC64;
MSASLLRSLA DVVGSAHVTD DPDVLAGHSV DYTGRYRGRA GALVRPGSAK EVAAVLRACR
DGGAYVTVQG GRTSLVAGTV PEHDDVLLST ERLNTVGEID TVERRIRVGA GVTLAAVQRA
AATAGLVFGV DLTARDTATV GGMASTNAGG LCTVHYGNMG EQVLGMAVAL PDGSLLSRHS
AVRADNTGYN LPALFVGAEG TLGVITGLEL RLRPAPAHRV TAICGFADLD ALIGAARVFR
DLDGIATLEL IDARVAALTG ERLGVAAPVR GDWLLLVELA GDTDQTDRLF GLLQQVSCSD
EPAVGVDTAT RQRLWRVREA VADVLGVFGP PLKFDVSLPL AAVAGFAAAA GAAIRTQAPD
ALPVLFGHIG EGNLHLNVLR CSAAAEPGLY AAMMALIADC GGNVSSEHGV GSRKRAYLPM
SRGPDDIAAM RTVKAAFDPT GYLNAAVLFD
//