NB1_MYCPA
ID NB1_MYCPA Reviewed; 161 AA.
AC Q73W27;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=MAP_2833c;
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; AAS05150.1; -; Genomic_DNA.
DR RefSeq; WP_003875226.1; NC_002944.2.
DR AlphaFoldDB; Q73W27; -.
DR SMR; Q73W27; -.
DR STRING; 262316.MAP_2833c; -.
DR EnsemblBacteria; AAS05150; AAS05150; MAP_2833c.
DR KEGG; mpa:MAP_2833c; -.
DR PATRIC; fig|262316.17.peg.3000; -.
DR eggNOG; COG4044; Bacteria.
DR HOGENOM; CLU_085483_1_0_11; -.
DR OMA; YSQKTWK; -.
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..161
FT /note="Peroxynitrite isomerase 1"
FT /id="PRO_0000356924"
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; 17422 MW; F24C4ED21FEFB401 CRC64;
MPTDLHPDLA ALAPLLGTWT GRGSGKYPTI QPFDYLEEVT FSHVGKPFLA YAQKTRAAAD
GKPLHAETGY LRVPQPGRLE LVLAHPSGIT EIEVGSYAVT GGLIEMRMST TSIGLTPSAK
EVTALARWFR IDGDELSYSV QMGAVGQPLQ DHLAAVLHRQ R