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Database: UniProt
Entry: A0A0T6UI81_9PSED
LinkDB: A0A0T6UI81_9PSED
Original site: A0A0T6UI81_9PSED 
ID   A0A0T6UI81_9PSED        Unreviewed;       265 AA.
AC   A0A0T6UI81;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Aromatic ring-opening dioxygenase LigA {ECO:0000313|EMBL:KRW57594.1};
GN   ORFNames=AO726_20435 {ECO:0000313|EMBL:KRW57594.1};
OS   Pseudomonas sp. TTU2014-080ASC.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW57594.1, ECO:0000313|Proteomes:UP000051864};
RN   [1] {ECO:0000313|EMBL:KRW57594.1, ECO:0000313|Proteomes:UP000051864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW57594.1,
RC   ECO:0000313|Proteomes:UP000051864};
RA   Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA   Loneragan G.H.;
RT   "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT   Cattle.";
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRW57594.1}.
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DR   EMBL; LKKK01000016; KRW57594.1; -; Genomic_DNA.
DR   RefSeq; WP_058069983.1; NZ_LKKK01000016.1.
DR   AlphaFoldDB; A0A0T6UI81; -.
DR   STRING; 1729724.AO726_20435; -.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000051864; Unassembled WGS sequence.
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:KRW57594.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051864};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..245
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   265 AA;  29318 MW;  A24E83EC969FBF5C CRC64;
     MSLPSLFIPH GAGPCFFMQG HPGFPDIWEP LGDWLRGLAT QIGQRPRAIL VVSAHWQSPV
     FSVTASAKPS LLYDYYGFPA HTYLLKYPVS GSPELAGRVC ELLRAGGFEA QQDPQRGLDH
     GAFIPLMLSY PQADIPVLQL SLQRQLDAAQ HLAAGRCLAA LRDEGVLIVA SGMSFHNMRP
     DQNQLAERAR AFDEWLNEAM TAAPTERWER LCNWQQAPYA RFAHPTEEHL VPLMVVCGAA
     SEEPAQRIYS ERLAGLVDVS AFRLG
//
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