ID   NNHA_MYCS0              Reviewed;         379 AA.
AC   F4ZCI3;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=2-nitroimidazole nitrohydrolase;
DE            Short=2NI nitrohydrolase;
DE            EC=3.5.99.9;
GN   Name=nnhA;
OS   Mycobacterium sp. (strain JS330).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=1004011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=21244596; DOI=10.1111/j.1462-2920.2010.02406.x;
RA   Qu Y., Spain J.C.;
RT   "Catabolic pathway for 2-nitroimidazole involves a novel nitrohydrolase
RT   that also confers drug resistance.";
RL   Environ. Microbiol. 13:1010-1017(2011).
CC   -!- FUNCTION: Involved in the biodegradation of 2-Nitroimidazole (2NI)
CC       which is a natural antibiotic and an analog of the synthetic
CC       nitroimidazoles used for treatment of tuberculosis, Chagas disease
CC       (also called American Trypanosomiasis) and cancer. Catalyzes the
CC       hydrolytic denitration of 2NI to produce imidazol-2-one and nitrite. It
CC       is also active against the 2NI synthetic derivative benznidazole. NnhA
CC       confers drug resistance to 2NI. {ECO:0000269|PubMed:21244596}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-nitroimidazole + H2O = 1,3-dihydro-2H-imidazol-2-one + H(+)
CC         + nitrite; Xref=Rhea:RHEA:34271, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:51022,
CC         ChEBI:CHEBI:67135; EC=3.5.99.9;
CC         Evidence={ECO:0000269|PubMed:21244596};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:21244596};
CC       Temperature dependence:
CC         Optimum temperature is 24 degrees Celsius.
CC         {ECO:0000269|PubMed:21244596};
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR   EMBL; HM538831; AEB33883.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4ZCI3; -.
DR   SMR; F4ZCI3; -.
DR   KEGG; ag:AEB33883; -.
DR   BioCyc; MetaCyc:MON-17531; -.
DR   BRENDA; 3.5.99.9; 3490.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IDA:UniProtKB.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:UniProtKB.
DR   GO; GO:0052804; P:nitroimidazole catabolic process; IDA:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Hydrolase.
FT   CHAIN           1..379
FT                   /note="2-nitroimidazole nitrohydrolase"
FT                   /id="PRO_0000422782"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  42028 MW;  0ED8643846D08A26 CRC64;
     MTTVDKRPSS RGYGDWRLSD IPQYKDGIST YEFVRATHEA DYRTHQAEPV AGRTFGFNGI
     GRLTEVALHM PTKYTLHDQS SQYKESPSFF QGLMGVPDRG PVDLAAFQRE TEELATAFEN
     NGIKVHWVDY PEEPANPYGP LMGHVFLSWG SIWRGGSVIS RFGFLPGMVG VSEYLAKWAW
     NTLNIPPLVA ITEGAMEPGA CNMIADEVLV TCLSASYDQR GTDQLVAAIS KTSGTEEFHN
     LQLRPAVEGF FNKATGACAH PDININAIDV GKLVVSPAAL DWDARTWLYD NNFELIEADP
     DEQREFLAPC NVLLLEPGKV IAHADCHKTN QKIRDAGVEV IEVTGTEIRK ACGGIKCRVM
     QINREPGPTL ADVRNRVWR