ID C1DPE7_AZOVD Unreviewed; 270 AA.
AC C1DPE7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Catalytic LigB subunit of aromatic ring-opening dioxygenase {ECO:0000313|EMBL:ACO77379.1};
GN OrderedLocusNames=Avin_11500 {ECO:0000313|EMBL:ACO77379.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO77379.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO77379.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO77379.1; -; Genomic_DNA.
DR RefSeq; WP_012699800.1; NC_012560.1.
DR AlphaFoldDB; C1DPE7; -.
DR STRING; 322710.Avin_11500; -.
DR EnsemblBacteria; ACO77379; ACO77379; Avin_11500.
DR KEGG; avn:Avin_11500; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_046582_0_0_6; -.
DR OrthoDB; 9790889at2; -.
DR Proteomes; UP000002424; 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:ACO77379.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 11..249
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
SQ SEQUENCE 270 AA; 29452 MW; 0B95A403DD76DD63 CRC64;
MSARETIQPT LFVPHGAGPC FFMDWNPPDA WSAMAAFLRG IAGTLARPPR AILMVSAHWL
EAEFAVGAGR QPELIYDYYG FPPHTYELRY PAPGDPALAA EVARLLGAAG LPCRGDARRG
FDHGMFIPLK LMFPAADIPV VQLSLRQDLD PQAHFDAGCA LAPLREEGVL IVGSGMSFHN
MRGYGDPRFA PVSDEFDQWL TATVEAGPAE RAARLARWEA APAARLCHPP RAEEHLLPLM
TVAGAAAEGR GRRVFSDRVM ETTLSAFRFD
//
