ID   NAAB_BRASZ              Reviewed;         207 AA.
AC   D3WZ86;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=5-nitrosalicylic acid 1,2-dioxygenase;
DE            Short=5NSA 1,2-dioxygenase;
DE            EC=1.13.11.64;
DE   AltName: Full=5-nitroanthranilic acid degradation protein B;
GN   Name=naaB;
OS   Bradyrhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=JS329;
RX   PubMed=20081004; DOI=10.1128/aem.02816-09;
RA   Qu Y., Spain J.C.;
RT   "Biodegradation of 5-Nitroanthranilic Acid by Bradyrhizobium sp. Strain
RT   JS329.";
RL   Appl. Environ. Microbiol. 76:1417-1422(2010).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=JS329;
RX   PubMed=21498645; DOI=10.1128/jb.01188-10;
RA   Qu Y., Spain J.C.;
RT   "Molecular and biochemical characterization of the 5-nitroanthranilic acid
RT   degradation pathway in Bradyrhizobium sp. strain JS329.";
RL   J. Bacteriol. 193:3057-3063(2011).
CC   -!- FUNCTION: Dioxygenase that catalyzes the cleavage of the aromatic ring
CC       of 5-nitrosalicylate (5NSA) without prior removal of the nitro group in
CC       biodegradation of 5-nitroanthranilate. {ECO:0000269|PubMed:20081004,
CC       ECO:0000269|PubMed:21498645}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-nitrosalicylate + O2 = 2-oxo-3-(5-oxofuran-2-
CC         ylidene)propanoate + H(+) + nitrite; Xref=Rhea:RHEA:34227,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16301,
CC         ChEBI:CHEBI:61268, ChEBI:CHEBI:65081; EC=1.13.11.64;
CC         Evidence={ECO:0000269|PubMed:20081004, ECO:0000269|PubMed:21498645};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GU188569; ADC93717.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3WZ86; -.
DR   SMR; D3WZ86; -.
DR   KEGG; ag:ADC93717; -.
DR   BioCyc; MetaCyc:MON-17373; -.
DR   BRENDA; 1.13.11.64; 930.
DR   GO; GO:0051213; F:dioxygenase activity; IDA:CACAO.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF07883; Cupin_2; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Oxidoreductase.
FT   CHAIN           1..207
FT                   /note="5-nitrosalicylic acid 1,2-dioxygenase"
FT                   /id="PRO_0000418740"
SQ   SEQUENCE   207 AA;  23624 MW;  198FE54CE6DD357C CRC64;
     MKWSNKDGYP WSKIIHAEKF FDKVIQNDTR PGKWEWADVV SGLRDLDKDP RMNSERRYVA
     IVNEDVGLGE TKGIGITPGL FCGCQLIHPG EEVTSHRHNS VALYFIVEGT GELEVEGEVY
     SYKPFDIMTC PAWSYHAWRA TGDKDTLMYV IHDMALLAYM RALFWEEPKG SENIRHMVKG
     STHTWSNTKA PEVSKTQAAK ELLKQGE