NAAC_BRASZ
ID NAAC_BRASZ Reviewed; 248 AA.
AC F8QQ74;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Probable 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase;
DE EC=3.1.1.91;
DE AltName: Full=5-nitroanthranilic acid degradation protein C;
DE AltName: Full=Lactone hydrolase NaaC;
GN Name=naaC;
OS Bradyrhizobium sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=376;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
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: Involved in the 5-nitroanthranilic acid (5NAA) degradation.
CC Catalyzes the hydrolysis of the lactone to produce maleylpyruvate
CC biodegradation of 5-nitroanthranilate (Probable).
CC {ECO:0000305|PubMed:21498645}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-3-(5-oxofuran-2-ylidene)propanoate + H2O = 3-
CC maleylpyruvate + H(+); Xref=Rhea:RHEA:33967, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16727, ChEBI:CHEBI:65081; EC=3.1.1.91;
CC -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC {ECO:0000305}.
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DR EMBL; GU188569; AEH76925.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QQ74; -.
DR SMR; F8QQ74; -.
DR KEGG; ag:AEH76925; -.
DR BioCyc; MetaCyc:MON-17374; -.
DR GO; GO:0102355; F:2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046573; F:lactonohydrolase activity; IDA:CACAO.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002925; Dienelactn_hydro.
DR Pfam; PF01738; DLH; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..248
FT /note="Probable 2-oxo-3-(5-oxofuran-2-ylidene)propanoate
FT lactonase"
FT /id="PRO_0000418747"
FT ACT_SITE 123
FT /evidence="ECO:0000250"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 27660 MW; FBE1325E4A0F7012 CRC64;
MATETIAMDW VDIGTNGESR LAYLARPVVT GRLPAVIVMP AIHGINTYIK DVAIDLAKAG
FVALLIDIHS PEQEPDLSNA EKIQIAVETL DDRKVLKDVD AAVRYLEQHA AVRADRLGIL
GFCVGGTYAL LAARTPAIRV SVGFYGLLEY QSRTDNKPVS PLDSVAQFTA PILFHVGDKD
PWIDSKMLAE FTKRMQQHQK SYELCIYRGA GHAFHEHFRD AYRPIAAQSA WNNTLIYLRW
HLCGKRTV