ID A6WBD6_KINRD Unreviewed; 255 AA.
AC A6WBD6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Extradiol ring-cleavage dioxygenase class III protein subunit B {ECO:0000313|EMBL:ABS04125.1};
GN OrderedLocusNames=Krad_2653 {ECO:0000313|EMBL:ABS04125.1};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS04125.1, ECO:0000313|Proteomes:UP000001116};
RN [1] {ECO:0000313|Proteomes:UP000001116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC {ECO:0000313|Proteomes:UP000001116};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA Fliermans C., Richardson P.;
RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
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DR EMBL; CP000750; ABS04125.1; -; Genomic_DNA.
DR AlphaFoldDB; A6WBD6; -.
DR STRING; 266940.Krad_2653; -.
DR KEGG; kra:Krad_2653; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_046582_2_1_11; -.
DR OrthoDB; 9790889at2; -.
DR Proteomes; UP000001116; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR Gene3D; 3.40.830.10; LigB-like; 1.
DR InterPro; IPR014436; Extradiol_dOase_DODA.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1.
DR PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR Pfam; PF02900; LigB; 1.
DR PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:ABS04125.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..247
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
SQ SEQUENCE 255 AA; 28100 MW; ED74D9770A481981 CRC64;
MPALYLSHGA PPLFDDPHWI NQLFGWAQNL PTPRAVLIVS AHWESQSAML SSPVAATPLV
YDFGGFAQRY FEMTYATPDA TTLAAQVAAL MPDTESLHTS ATRGLDHGAW VPLKVMYPYA
DVPVLQLSMP THDPQKLLDL GRRLRPLREQ GVLVIGSGYM THGLPYITRD MIMYGTIPGW
SSEFDAWSTE ALLRGDIDTL ADYRRAPGMP YAHPTVEHFT PLFITMGAAT DATAAPKMII
SDYAMGMAKR SFQVA
//
