NB1_MYCSS
ID NB1_MYCSS Reviewed; 224 AA.
AC Q1B397;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Mmcs_4533;
OS Mycobacterium sp. (strain MCS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=164756;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS;
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 Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL Submitted (JUN-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; CP000384; ABG10637.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1B397; -.
DR SMR; Q1B397; -.
DR KEGG; mmc:Mmcs_4533; -.
DR HOGENOM; CLU_085483_0_0_11; -.
DR OMA; EKCNFGQ; -.
DR BioCyc; MSP164756:G1G6O-4634-MON; -.
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 1"
FT /id="PRO_0000356931"
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