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Database: UniProt
Entry: D3NSJ5_AZOS1
LinkDB: D3NSJ5_AZOS1
Original site: D3NSJ5_AZOS1 
ID   D3NSJ5_AZOS1            Unreviewed;       260 AA.
AC   D3NSJ5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Extradiol aromatic ring-opening dioxygenase {ECO:0000313|EMBL:BAI71374.1};
GN   OrderedLocusNames=AZL_007360 {ECO:0000313|EMBL:BAI71374.1};
OS   Azospirillum sp. (strain B510).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI71374.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI71374.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI71374.1,
RC   ECO:0000313|Proteomes:UP000002040};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
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; AP010946; BAI71374.1; -; Genomic_DNA.
DR   RefSeq; WP_012973360.1; NC_013854.1.
DR   AlphaFoldDB; D3NSJ5; -.
DR   STRING; 137722.AZL_007360; -.
DR   KEGG; azl:AZL_007360; -.
DR   HOGENOM; CLU_046582_2_1_5; -.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000002040; 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:BAI71374.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040};
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   260 AA;  27658 MW;  982A4203CF57A095 CRC64;
     MSETFPSVFV SHGSPTLILE EDSAGRDFLS KLGQRLGRPS AILAVSAHWT TRVPAVSTAA
     APETIHDFYG FPDALYRMRY AAPGAPALAE RVMALTGAVT DPSQGLDHGA WVPLTLMYPQ
     ADIPVAQFSV MPYRSAADHI ALGRLLEPLR REGVLILASG GAVHNLREFR FGGTSAAPWA
     TGFADWLDRT LEAGDAEAVG NWLAACPDAR RAHPTDEHFL PLPVALGAAG PRPKTERLHA
     GFEHGSLGMH AYAFSAGDAA
//
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