ID NAAA_BRASZ Reviewed; 425 AA.
AC D3WZ85;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 13-SEP-2023, entry version 40.
DE RecName: Full=5-nitroanthranilic acid aminohydrolase;
DE EC=3.5.99.8;
DE AltName: Full=5-nitroanthranilic acid degradation protein A;
DE AltName: Full=5NAA deaminase;
GN Name=naaA;
OS Bradyrhizobium sp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=376;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: Catalyzes the deamination of 5-nitroanthranilate (5NAA) to 5-
CC nitrosalicylate (5NSA), the first step in biodegradation of 5-
CC nitroanthranilate. {ECO:0000269|PubMed:20081004,
CC ECO:0000269|PubMed:21498645}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-nitroanthranilate + H(+) + H2O = 5-nitrosalicylate + NH4(+);
CC Xref=Rhea:RHEA:28166, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:61267, ChEBI:CHEBI:61268; EC=3.5.99.8;
CC Evidence={ECO:0000269|PubMed:21498645};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21498645};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21498645};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21498645};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:21498645};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:21498645};
CC Note=Divalent metal cations. Co(2+), Mn(2+), Zn(2+), Fe(2+) or Ni(2+).
CC {ECO:0000269|PubMed:21498645};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=335.1 uM for 5-nitroanthranilate {ECO:0000269|PubMed:21498645};
CC Vmax=181.5 nmol/min/mg enzyme {ECO:0000269|PubMed:21498645};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:21498645};
CC Temperature dependence:
CC Optimum temperature is degrees Celsius.
CC {ECO:0000269|PubMed:21498645};
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; GU188569; ADC93716.1; -; Genomic_DNA.
DR PDB; 5K8M; X-ray; 2.75 A; A/B/C/D=1-425.
DR PDB; 5K8N; X-ray; 3.23 A; A/B/C/D/E/F/G/H=1-425.
DR PDB; 5K8O; X-ray; 2.89 A; A/B/C/D/E/F/G/H=1-425.
DR PDB; 5K8P; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-425.
DR PDBsum; 5K8M; -.
DR PDBsum; 5K8N; -.
DR PDBsum; 5K8O; -.
DR PDBsum; 5K8P; -.
DR AlphaFoldDB; D3WZ85; -.
DR SMR; D3WZ85; -.
DR KEGG; ag:ADC93716; -.
DR BioCyc; MetaCyc:MONOMER-15902; -.
DR BRENDA; 3.5.99.8; 930.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03896; M20_PAAh_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding.
FT CHAIN 1..425
FT /note="5-nitroanthranilic acid aminohydrolase"
FT /id="PRO_0000418738"
FT ACT_SITE 88
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5K8P"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5K8M"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5K8P"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5K8N"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 239..260
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 375..380
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:5K8P"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:5K8P"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5K8P"
FT HELIX 403..420
FT /evidence="ECO:0007829|PDB:5K8P"
SQ SEQUENCE 425 AA; 46349 MW; 026B430C5B3C9276 CRC64;
MAGSNDVAKV MKTLDGMREG LIQTAVELGS IEAPTGREGA AGDYVYEWMA RNGFGPERVG
VFDDRFNVVG RLRGTGGGAS LSFNSHLDTI MAREDTARFA DANDRIYHEA WHEEGRIYGY
SVVNCKGPMA CWLIAAKALK EAGAALKGDV VLTAVCGEID CEPVDEFQGH DYLAEDIGAR
YAISHGAISD YALVAEATNF KPAWVEAGKV FLKVTVFAGP SRYTPYVPRP VAALDSPNAI
VRMAKLVEAL EEWADNYEKR YTREYGGGTV VPKVAIGAIR GGVPYKIYRF PELCSIYMDI
RLNPDTNPLV VQREVEAVVS KLGLKAEVKP FLFRRGYEAQ GIEPLQNALE VAHREVVGRP
TERPGSPECS MWRDTNPYNE LGIPSLTYGC GGGAGGGNTY FLVDDMLKAA KVYAMTAMDL
CNRTP
//
