ID A0A0Q6VPT6_9BURK Unreviewed; 268 AA.
AC A0A0Q6VPT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Aromatic ring-opening dioxygenase LigA {ECO:0000313|EMBL:KQV78543.1};
GN ORFNames=ASD15_22320 {ECO:0000313|EMBL:KQV78543.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV78543.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV78543.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV78543.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV78543.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV78543.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQV78543.1}.
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DR EMBL; LMDJ01000036; KQV78543.1; -; Genomic_DNA.
DR RefSeq; WP_057158891.1; NZ_LMDJ01000036.1.
DR AlphaFoldDB; A0A0Q6VPT6; -.
DR OrthoDB; 9790889at2; -.
DR Proteomes; UP000051876; 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:KQV78543.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..254
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
SQ SEQUENCE 268 AA; 28759 MW; B1B5238D57411DE1 CRC64;
MSSTALPTYF LSHGGGPWPW MLDQYGGRYD ALKASLEDIP RQLGGVRPKA VLVVTAHWEA
REPLISASPR PPMIYDYGGF PAYTYEIQYS APGSPEVAAR VQQLLNGAGI AAQLDPQRGF
DHGTFSAMQP IYPAADVPIV QLSLKQGLDP AEHIAIGRAL APLRKESVLI VGSGLSYHNL
RQFGAAGAAA SHQFDAWLRE SMALPPAERE ARLLAWASAP AARAAHPREE HLLPLMVAHG
AAGGEPASNV YHEDAFMGSL AVSSFRFA
//
