NB1_MYCMM
ID NB1_MYCMM Reviewed; 223 AA.
AC B2HH20;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=MMAR_4871;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000854; ACC43275.1; -; Genomic_DNA.
DR RefSeq; WP_012396402.1; NC_010612.1.
DR AlphaFoldDB; B2HH20; -.
DR SMR; B2HH20; -.
DR STRING; 216594.MMAR_4871; -.
DR EnsemblBacteria; ACC43275; ACC43275; MMAR_4871.
DR GeneID; 64258132; -.
DR KEGG; mmi:MMAR_4871; -.
DR eggNOG; COG4044; Bacteria.
DR HOGENOM; CLU_085483_0_0_11; -.
DR OMA; EKCNFGQ; -.
DR OrthoDB; 1524197at2; -.
DR Proteomes; UP000001190; 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..223
FT /note="Peroxynitrite isomerase 1"
FT /id="PRO_0000356922"
FT MOTIF 69..75
FT /note="GXWXGXG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT BINDING 186
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT BINDING 213
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 223 AA; 24042 MW; 614171FBED310C2B CRC64;
MTSDASQDGP DAVAGSGDRA VAAAAERAKL TAARNIPTFD DLPLPADTAN LRHGANLHDA
LLALLPLVGV WRGEGEGRGP HGDYRFGQQI VVSHDGGDYL NWEARSWRLD EDGQYEEPGL
RETGFWRFVS DPEDDPSESQ AIELLLAHSA GYVELFYGRP LTQSSWELVT DALARSRSGV
LVGGAKRLYG IIEGGDLAYV EERVDADGGL VPHLSARLSR YAG