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Database: UniProt
Entry: F5YX15_MYCSD
LinkDB: F5YX15_MYCSD
Original site: F5YX15_MYCSD 
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
//
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