NB_STRAW
ID NB_STRAW Reviewed; 180 AA.
AC Q82ND8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=SAV_1365;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
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; BA000030; BAC69075.1; -; Genomic_DNA.
DR RefSeq; WP_010982803.1; NZ_JZJK01000078.1.
DR AlphaFoldDB; Q82ND8; -.
DR SMR; Q82ND8; -.
DR STRING; 227882.SAV_1365; -.
DR EnsemblBacteria; BAC69075; BAC69075; SAVERM_1365.
DR KEGG; sma:SAVERM_1365; -.
DR eggNOG; COG4044; Bacteria.
DR HOGENOM; CLU_085483_0_0_11; -.
DR OMA; YSQKTWK; -.
DR OrthoDB; 1524197at2; -.
DR Proteomes; UP000000428; 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..180
FT /note="Peroxynitrite isomerase"
FT /id="PRO_0000356952"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..40
FT /note="GXWXGXG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01297"
FT BINDING 171
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 180 AA; 20008 MW; 9A91277CB5512310 CRC64;
MVDPAPEHPY PDGHRPDEAP APHALLEPVL GLLGSWYGRG EGGYPTLTGD FGYAQELTFS
HDGRPFLRYE ARAWLLDADD APLRPSAREC GWWRLQPDGR VEALITQPTG IAEIMVGRAT
GNTIDLSTHE VALAPTAKKV NATRRRYTLT DDDTLTFHHD LEAVGQPMQH HLSARLRRRG
