ID   NB1_RHOJR               Reviewed;         176 AA.
AC   Q0S4V4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Peroxynitrite isomerase 1;
DE            EC=5.99.-.- {ECO:0000255|HAMAP-Rule:MF_01297};
DE   AltName: Full=Ferric nitrobindin;
DE            Short=Nb(III);
GN   OrderedLocusNames=RHA1_ro05653;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG97432.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0S4V4; -.
DR   SMR; Q0S4V4; -.
DR   STRING; 101510.RHA1_ro05653; -.
DR   EnsemblBacteria; ABG97432; ABG97432; RHA1_ro05653.
DR   KEGG; rha:RHA1_ro05653; -.
DR   eggNOG; COG4044; Bacteria.
DR   HOGENOM; CLU_085483_1_1_11; -.
DR   OMA; YSQKTWK; -.
DR   Proteomes; UP000008710; 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..176
FT                   /note="Peroxynitrite isomerase 1"
FT                   /id="PRO_0000356946"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           37..43
FT                   /note="GXWXGXG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT   BINDING         168
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   176 AA;  19185 MW;  121204EB24B58F46 CRC64;
     MDENSTLSPA HSDAAASSSA NTPPLPYVPS ALAPFAGLWR GEGEGAYPTI DDFAYTEEIE
     FAPTGKPFLA YRSRTREAGS GRPLHSESGF LRLVGEDEAE LLVAQPTGFT EIHRGQVREG
     TIELSMVVLS ASPDAKPVHS IRRQLSVRGG DLTYDLWMAH DLTPLTHHLH GHLRRD