ID F2LK28_BURGS Unreviewed; 446 AA.
AC F2LK28;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Protocatechuate 4,5-dioxygenase {ECO:0000313|EMBL:AEA62653.1};
GN OrderedLocusNames=bgla_2g01750 {ECO:0000313|EMBL:AEA62653.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA62653.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA62653.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA62653.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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DR EMBL; CP002600; AEA62653.1; -; Genomic_DNA.
DR RefSeq; WP_013688985.1; NC_015376.1.
DR AlphaFoldDB; F2LK28; -.
DR STRING; 999541.bgla_2g01750; -.
DR KEGG; bgd:bgla_2g01750; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_653589_0_0_4; -.
DR Proteomes; UP000008316; Chromosome 2.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR CDD; cd07923; Gallate_dioxygenase_C; 1.
DR Gene3D; 1.10.700.10; Dioxygenase LigAB, LigA subunit; 1.
DR Gene3D; 3.40.830.10; LigB-like; 1.
DR InterPro; IPR034940; Gallate_dioxygenase_C.
DR InterPro; IPR036622; LigA_sf.
DR InterPro; IPR011986; Xdiol_dOase_LigA.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR Pfam; PF07746; LigA; 1.
DR Pfam; PF02900; LigB; 1.
DR SUPFAM; SSF48076; LigA subunit of an aromatic-ring-opening dioxygenase LigAB; 1.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:AEA62653.1};
KW Oxidoreductase {ECO:0000313|EMBL:AEA62653.1}.
FT DOMAIN 8..271
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
FT DOMAIN 321..407
FT /note="Extradiol ring-cleavage dioxygenase LigAB LigA
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF07746"
FT REGION 426..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 49484 MW; 19FF7790173CD381 CRC64;
MARIIGGIAA SHTPTIGFAF DKNKRDDPVW APIFENFAPL AAWIDAKRPD VLLMIYNDHA
TSFFFDHYSA FALGVGPRWE VADEGGGARA LPPIEGHPAL AAHIGRSLMA DEFDMSFFQN
KPLDHGCFSP LSMLCPNRPS WPVQLVPLQM GVLQLPMPSA RRFYKLGQAL RRAVESYPED
LRVAIVATGG LSHQVHGERA GFNNTAWDQR FLDLFEHDPE QLANMTLADY ARLGGYEGAE
VVMWLTMRGA LPAQVQCRQR GYYLPSMAGI ATAIYEGAED EPDAVQAARH RARMAAELDG
IEQLEGTYPF SVETAVRAWR INDFLHRRIE PAHREAFLAD PERSFEAAGL SEEERDLVRR
RDWRGLLHYG VIFFMLEKLG AVSGISNLHI YAAMRGETLD AFQRTRNAPG ALYSVAGKGA
GALAWDRQAG DAQTDAQQGR TSRGDN
//
