ID D9XKE4_9ACTN Unreviewed; 415 AA.
AC D9XKE4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aromatic-ring hydroxylase {ECO:0000313|EMBL:EFL43170.1};
GN ORFNames=SSRG_05974 {ECO:0000313|EMBL:EFL43170.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL43170.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL43170.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL43170.1};
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 griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG657758; EFL43170.1; -; Genomic_DNA.
DR AlphaFoldDB; D9XKE4; -.
DR STRING; 467200.SSRG_05974; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_19_3_11; -.
DR Proteomes; UP000002968; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 2..342
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 415 AA; 45280 MW; BBA75EDB9DACE3D7 CRC64;
MVGGGIGGLG VACSLTRQGQ SVRLLESAPA FGEVGAGIQL APNCTRILDD YGLLDEAKSL
GVVPDAMVMR DAVDGEELTR LDLRDLERRY GYPYLVIHRS DLHGLLLRAC ERAGVELVND
ARVTSYENTD GGARVTLASG ETHEAGMVIA ADGLHSPARK LFVDDRPVSS AYVAYRGTVP
AAQPRVKSVD LSEVVVYIGP RCHFVHYGLR GGEMLNQVAV FESPKALAGH DDWGTPDELD
AAFAGTCGFV QDGLPFMWRD KWWRMFDRDP IMTWVHGRIA LLGDSAHPPL QYIAQGAIMA
VEDGWVLGEH VARNRAEDGT VDWTAALAAY EAVRPEHCRR VLTTSRKWGE LWHLDGLARE
QRNVLLRARD TYDYAFTDWL YGPTALTPDE EPPMFTAIPL DSAVTGEPVP AGGAA
//