ID D6ANF7_STRFL Unreviewed; 286 AA.
AC D6ANF7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Dioxygenase {ECO:0000313|EMBL:EFE75564.2};
GN ORFNames=SSGG_02931 {ECO:0000313|EMBL:EFE75564.2};
OS Streptomyces filamentosus NRRL 15998.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE75564.2, ECO:0000313|Proteomes:UP000003986};
RN [1] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA Molnar K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00007825}.
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DR EMBL; DS999644; EFE75564.2; -; Genomic_DNA.
DR RefSeq; WP_006125564.1; NZ_DS999644.1.
DR AlphaFoldDB; D6ANF7; -.
DR Proteomes; UP000003986; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR CDD; cd12214; ChiA1_BD; 1.
DR CDD; cd00421; intradiol_dioxygenase; 1.
DR Gene3D; 2.60.130.10; Aromatic compound dioxygenase; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR33711:SF7; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14270)-RELATED; 1.
DR PANTHER; PTHR33711; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF49482; Aromatic compound dioxygenase; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:EFE75564.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 240..286
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 30418 MW; B5980A0A28FBB551 CRC64;
MDNATPHEPN ASDEASGDRR RISRKGLLKA ALVASAAPLL AGGGVALARD AAATGDGPLA
LTPECDDGDD TTPPQMEGPY FKPNSPRRTS LVTTGTPGVP LTVSGYVFGR ACRPISGALL
DFWQADTNGA YDMVRFDFRG HQFTGADGSF SLTTIVPGLY PGRTRHIHVK AQAPGGRILT
TQLYFPNEPR NNTDALFDPR LLMNVRNVGN GRQGTFDFVL DVAQTPGPTD PPTDPPTEPG
TSWAAGTSYR AGDRVTYGGV AYRCLQAHQA VSGWEPPNVP ALWERG
//
