ID   NB2_MYCTO               Reviewed;         164 AA.
AC   P9WFG6; L0TAF4; O07216; Q7D6Q1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Peroxynitrite isomerase 2;
DE            EC=5.99.-.- {ECO:0000255|HAMAP-Rule:MF_01297};
DE   AltName: Full=Ferric nitrobindin;
DE            Short=Nb(III);
GN   OrderedLocusNames=MT2790;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Heme-binding protein able to scavenge peroxynitrite and to
CC       protect free L-tyrosine against peroxynitrite-mediated nitration, by
CC       acting as a peroxynitrite isomerase that converts peroxynitrite to
CC       nitrate. Therefore, this protein likely plays a role in peroxynitrite
CC       sensing and in the detoxification of reactive nitrogen and oxygen
CC       species (RNS and ROS, respectively). Is able to bind nitric oxide (NO)
CC       in vitro, but may act as a sensor of peroxynitrite levels in vivo.
CC       {ECO:0000255|HAMAP-Rule:MF_01297}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=peroxynitrite = nitrate; Xref=Rhea:RHEA:63116,
CC         ChEBI:CHEBI:17632, ChEBI:CHEBI:25941; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01297};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63117;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01297};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01297};
CC       Note=Binds 1 heme b group per subunit, that coordinates a highly
CC       solvent-exposed Fe(III) atom. {ECO:0000255|HAMAP-Rule:MF_01297};
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000255|HAMAP-Rule:MF_01297}.
CC   -!- DOMAIN: Forms a 10-stranded antiparallel beta-barrel structure able to
CC       accommodate a hydrophobic ligand in its interior. In fact, this fold
CC       hosts the heme group, which is located in a wide surface cleft.
CC       {ECO:0000255|HAMAP-Rule:MF_01297}.
CC   -!- SIMILARITY: Belongs to the nitrobindin family. {ECO:0000255|HAMAP-
CC       Rule:MF_01297}.
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DR   EMBL; AE000516; AAK47106.1; -; Genomic_DNA.
DR   PIR; H70532; H70532.
DR   RefSeq; WP_003900559.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFG6; -.
DR   SMR; P9WFG6; -.
DR   EnsemblBacteria; AAK47106; AAK47106; MT2790.
DR   GeneID; 45426704; -.
DR   KEGG; mtc:MT2790; -.
DR   PATRIC; fig|83331.31.peg.3004; -.
DR   HOGENOM; CLU_085483_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0062213; F:peroxynitrite isomerase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd07828; lipocalin_heme-bd-THAP4-like; 1.
DR   Gene3D; 2.40.128.20; -; 1.
DR   HAMAP; MF_01297; nitrobindin; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR022939; Nb(III)_bact/plant.
DR   InterPro; IPR045165; Nitrobindin.
DR   InterPro; IPR014878; THAP4-like_heme-bd.
DR   PANTHER; PTHR15854; PTHR15854; 1.
DR   Pfam; PF08768; THAP4_heme-bd; 1.
DR   SUPFAM; SSF50814; SSF50814; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Isomerase; Metal-binding.
FT   CHAIN           1..164
FT                   /note="Peroxynitrite isomerase 2"
FT                   /id="PRO_0000428542"
FT   MOTIF           17..23
FT                   /note="GXWXGXG"
FT   BINDING         155
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
SQ   SEQUENCE   164 AA;  17846 MW;  F3194F002502BB28 CRC64;
     MTRDLAPALQ ALSPLLGSWA GRGAGKYPTI RPFEYLEEVV FAHVGKPFLT YTQQTRAVAD
     GKPLHSETGY LRVCRPGCVE LVLAHPSGIT EIEVGTYSVT GDVIELELST RADGSIGLAP
     TAKEVTALDR SYRIDGDELS YSLQMRAVGQ PLQDHLAAVL HRQR