ID   NB2_MYCPA               Reviewed;         235 AA.
AC   Q743E2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=MAP_0643c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS02960.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q743E2; -.
DR   SMR; Q743E2; -.
DR   STRING; 262316.MAP_0643c; -.
DR   EnsemblBacteria; AAS02960; AAS02960; MAP_0643c.
DR   KEGG; mpa:MAP_0643c; -.
DR   eggNOG; COG4044; Bacteria.
DR   HOGENOM; CLU_085483_0_0_11; -.
DR   OMA; EKCNFGQ; -.
DR   Proteomes; UP000000580; 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; Reference proteome.
FT   CHAIN           1..235
FT                   /note="Peroxynitrite isomerase 2"
FT                   /id="PRO_0000356925"
FT   MOTIF           82..88
FT                   /note="GXWXGXG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT   BINDING         198
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT   BINDING         225
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   235 AA;  25341 MW;  4E60F857D84F2DD9 CRC64;
     MVCALHAVPA HHRRVVTPAG DDPSGPAGSG DRAVAAAAER AKLTAGRNIP SFDDLPLPAD
     TANLREGANL SDALLALLPL VGVWRGEGEG RGHDGDYRFG QQIVVSHDGG DYLNWEARSW
     RLNDTGDYQE RGLRETGFWR FVRDPDDPSE SQAIELLLAH SAGYVELFYG RPRTQSSWEL
     VTDALARSRS GVLVGGAKRL YGIVEGGDLA YVEERVDADG GLVPHLSARL SRFAG