ID   NB_MYCSK                Reviewed;         224 AA.
AC   A1ULV3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Peroxynitrite isomerase;
DE            EC=5.99.-.- {ECO:0000255|HAMAP-Rule:MF_01297};
DE   AltName: Full=Ferric nitrobindin;
DE            Short=Nb(III);
GN   OrderedLocusNames=Mkms_4620;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL93811.1; -; Genomic_DNA.
DR   RefSeq; WP_011561910.1; NC_008705.1.
DR   AlphaFoldDB; A1ULV3; -.
DR   SMR; A1ULV3; -.
DR   STRING; 189918.Mkms_4620; -.
DR   PRIDE; A1ULV3; -.
DR   EnsemblBacteria; ABL93811; ABL93811; Mkms_4620.
DR   KEGG; mkm:Mkms_4620; -.
DR   HOGENOM; CLU_085483_0_0_11; -.
DR   OMA; EKCNFGQ; -.
DR   OrthoDB; 1524197at2; -.
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..224
FT                   /note="Peroxynitrite isomerase"
FT                   /id="PRO_0000356930"
FT   MOTIF           71..77
FT                   /note="GXWXGXG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT   BINDING         187
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT   BINDING         214
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   224 AA;  24302 MW;  67ED70D89B57F553 CRC64;
     MTAPQEPEDA AGSIFSTSGD RAVADAAERA KVTASRNIPV FDDLPLPADT ANLRKGVDFN
     DALLALLPLV GVWRGEGEGR GPHGDYRFGQ QIVVSHDGGD YLNWEARSWR LTESGEYDRV
     GLRETGFWRF VSDPADPSES QAIELLLAHS AGYIELFYGH PRNQSSWELV TDALARSKSG
     MLVGGAKRLY GIVEGGDLAY VEERVDADGG LVPHLSARLA RYVG