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Database: UniProt
Entry: M1NM68_9CORY
LinkDB: M1NM68_9CORY
Original site: M1NM68_9CORY 
ID   M1NM68_9CORY            Unreviewed;       260 AA.
AC   M1NM68;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Extradiol ring-cleavage dioxygenase class III protein subunit B {ECO:0000313|EMBL:AGF72458.1};
GN   ORFNames=A605_07280 {ECO:0000313|EMBL:AGF72458.1};
OS   Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF72458.1, ECO:0000313|Proteomes:UP000011723};
RN   [1] {ECO:0000313|EMBL:AGF72458.1, ECO:0000313|Proteomes:UP000011723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF72458.1};
RX   PubMed=23408721;
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA   Kalinowski J.;
RT   "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT   type strain YIM 70093(T) (= DSM 44683(T)).";
RL   Stand. Genomic Sci. 7:284-293(2012).
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; CP003697; AGF72458.1; -; Genomic_DNA.
DR   RefSeq; WP_015400877.1; NZ_JIAJ01000001.1.
DR   AlphaFoldDB; M1NM68; -.
DR   STRING; 1121362.A605_07280; -.
DR   KEGG; chn:A605_07280; -.
DR   PATRIC; fig|1121362.3.peg.1469; -.
DR   eggNOG; COG3384; Bacteria.
DR   HOGENOM; CLU_046582_2_0_11; -.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000011723; 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:AGF72458.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          5..238
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   260 AA;  28398 MW;  61004FDAEFD8F970 CRC64;
     MTTNALFVGH GTPMNAIEDN EFTHTWKNLG ASISESAPRA ILSVSAHWYT RGTGVTAMTN
     PKTIHDFWGF PPELNAVQYD APGDPEVAEL VRDLAKPTLV QEDYNWGLDH GTWSVLKHMF
     PEAKIPVVQL SIDGTKPFSE HVALGTRLAR LAQEHNVLIV GSGNVVHNLS MVQWHKGNSG
     FDWADSFDDA AKAIMLDDPD RVETLAEHDG FTRAVPTPDH FLPLAYIAGV TAGLGETDVS
     TFNEQRTMGS LSMTGYQVAS
//
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