ID   NB2_MYCUA               Reviewed;         161 AA.
AC   A0PT73;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=MUL_3360;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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   -!- SUBUNIT: Homodimer. {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; CP000325; ABL05542.1; -; Genomic_DNA.
DR   RefSeq; WP_011741150.1; NC_008611.1.
DR   AlphaFoldDB; A0PT73; -.
DR   SMR; A0PT73; -.
DR   STRING; 362242.MUL_3360; -.
DR   EnsemblBacteria; ABL05542; ABL05542; MUL_3360.
DR   GeneID; 64260681; -.
DR   KEGG; mul:MUL_3360; -.
DR   eggNOG; COG4044; Bacteria.
DR   HOGENOM; CLU_085483_1_0_11; -.
DR   OMA; YSQKTWK; -.
DR   Proteomes; UP000000765; 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..161
FT                   /note="Peroxynitrite isomerase 2"
FT                   /id="PRO_0000356938"
FT   MOTIF           17..23
FT                   /note="GXWXGXG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT   BINDING         152
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   161 AA;  17368 MW;  1A6052CF5F6AAD59 CRC64;
     MPADLHPDLD ALAPLLGTWA GQGAGEYPTI EPFEYLEEVV FSHVGKPFLV YAQKTRAVAD
     GTPLHAETGY LRVPKPGQVE LVLAHPSGIT EIEVGTYSAS GGVIEMEMVT TAIGMTPTAK
     EVTALSRSFR MVGDELSYRL RMGAVGLPLQ HHLGARLRRK S