ID D9X5J7_STRVT Unreviewed; 462 AA.
AC D9X5J7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=FAD-dependent oxygenase {ECO:0000313|EMBL:EFL33960.1};
GN ORFNames=SSQG_04478 {ECO:0000313|EMBL:EFL33960.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL33960.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
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 viridochromogenes strain DSM 40736.";
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};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; GG657757; EFL33960.1; -; Genomic_DNA.
DR RefSeq; WP_003992067.1; NZ_GG657757.1.
DR AlphaFoldDB; D9X5J7; -.
DR STRING; 591159.SSQG_04478; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_018354_10_0_11; -.
DR OrthoDB; 9775082at2; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004184}.
FT DOMAIN 39..207
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 462 AA; 49106 MW; BF984C91BE5469C4 CRC64;
MTTTHGTPDL FALSDINGPV LRPGDPAYAD EVTGFNLAAL HTPDIVIGAT GPDDIVTAMR
WAKATGTPVA VQATGHGANF PIEHGLLINT SRMTDVQTDP TTRTATVAAG AKWSDVISAA
APHGLAGLCG TSTDAGVVGY VLGGGLPVLG RAYGYAADLV RSMQVVTPDG HLRETDPQHE
PELFWALRGG KGNVGIVTSL VTDLLPLSRL YGGGLHTPGE HAADLLRAWS DWTRTVPDEM
CSMFSVLRLP PIPQIPEPLR GGFWGRVAIT WPGDPAEGEA LIAPLRRAAP VAVDTVEDME
FAALDRIHME PQDPLPAREC CLLLRDLSPD ALSTFLEQVG PAAGPDYPLL VASLRHMGGA
LARPSAVEDA VCARDARYFM ESVGLMPAPP VAEAVEQATR RLYTAMAPYG TGHTMVNIHG
TPGDEQDRAR AWTPEVYARL RHDKATYDPS NLLRYGHAVT PA
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