ID D9WHA5_9ACTN Unreviewed; 450 AA.
AC D9WHA5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Benzoate 1,2-dioxygenase, large subunit {ECO:0000313|EMBL:EFL29031.1};
GN ORFNames=SSOG_08745 {ECO:0000313|EMBL:EFL29031.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL29031.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL29031.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL29031.1,
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 -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; GG657754; EFL29031.1; -; Genomic_DNA.
DR AlphaFoldDB; D9WHA5; -.
DR STRING; 457427.SSOG_08745; -.
DR HOGENOM; CLU_026244_4_1_11; -.
DR Proteomes; UP000003963; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd08879; RHO_alpha_C_AntDO-like; 1.
DR CDD; cd03542; Rieske_RO_Alpha_HBDO; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017639; Benzo_1-2-diOase_lsu.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR NCBIfam; TIGR03229; benzo_1_2_benA; 1.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:EFL29031.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 53..134
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 450 AA; 51372 MW; BC5B69A521BBB909 CRC64;
MIMADDFSRA RAIVEDALVE DPDSGVYRVR RGVFTDEELF ELEMKHIFEG NWVYLAHESQ
IPEVGDYFTT YIGRHPVVIS RDKQGELHCL INACSHRGAM LCRRKTDNRT TFTCPFHGWT
FSNSGRLLKV KDPREAGYPE QFNTDGSHDL KKVARFENYR GFLFGSLNPD VKPLTEHLGD
AAVVIDMIVD QSPEGLEVLR GSSTYHYDGN WKLQAENGAD GYHVSATHWN YAATQARRTS
GESRNDTKTM DSGGWSKQQG GFYSFDHGHL LLWTRWLDPT NRPLHDKREE LAAEFGEEKA
DWMIGVSRNL CLYPNVYLMD QFSSQIRHFR PISVDKTEVT IYCIAPKGEP AEARAQRIRQ
YEDFFNATGM ATPDDLEEFR SCQKTYLAES MPWNDLSRGA VHRIDGPDED AKKIGIHPIA
SGVRTEDEGL YPIQHGYWLD TLRKALEAAK
//
