ID D9WKH9_9ACTN Unreviewed; 455 AA.
AC D9WKH9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Oxidoreductase, FAD-binding {ECO:0000313|EMBL:EFL25713.1};
GN ORFNames=SSOG_05427 {ECO:0000313|EMBL:EFL25713.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL25713.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL25713.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL25713.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; GG657754; EFL25713.1; -; Genomic_DNA.
DR RefSeq; WP_009717516.1; NZ_GG657754.1.
DR AlphaFoldDB; D9WKH9; -.
DR STRING; 457427.SSOG_05427; -.
DR HOGENOM; CLU_017779_9_2_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000003963; Unassembled WGS sequence.
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; 3.30.70.2740; -; 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; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 4: Predicted;
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 47575 MW; 754496FDD5C3B6AB CRC64;
MTDLIESLRE GLPEEAVLTD PDVTAAYAND MASFCDAGAP AAVVLPRTVE QVQHVCRTAT
ALRVPIVPQG ARTGLSGAAN ASDGCIVLSL IKMDRILEIN PVDRIAVVEP GVVNAALSRA
VLEKGLYYPP DPSSWEQCTI GGNIGTASGG LCCVKYGVTA EYVLGLDIVL ADGRLLSTGR
RTAKGVAGYD LTRLFVGSEG SLGIVVRAVL ALKPAPPEQL VLAAEFPSTA AACDAICRIM
ERGHVPSLLE LMDRTSVRAV NALGDMGLPE STEALLMAAF DTPDPASDLA AVGELCTAAG
ATEVVPADDA AESDLLLQAR RMTLTALEAV KGVTMIDDVC VPRSRLAEMI DGTAAIAEKY
DLTIGVVAHA GDGNTHPTVC FDPADPDESR RARESFDEIM ALGLELGGTI TGEHGVGVLK
REWLARELGP VGVELQQGIK QVFDPLGLLN PGKLF
//