ID Q4DCQ3_TRYCC Unreviewed; 233 AA. AC Q4DCQ3; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414}; GN ORFNames=Tc00.1047053509775.40 {ECO:0000313|EMBL:EAN90306.1}; OS Trypanosoma cruzi (strain CL Brener). OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum. OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN90306.1, ECO:0000313|Proteomes:UP000002296}; RN [1] {ECO:0000313|EMBL:EAN90306.1, ECO:0000313|Proteomes:UP000002296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN90306.1, RC ECO:0000313|Proteomes:UP000002296}; RX PubMed=16020725; DOI=10.1126/science.1112631; RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F., RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., RA Andersson B.; RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas RT disease."; RL Science 309:409-415(2005). RN [2] {ECO:0007829|PDB:4DVH} RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 32-233 IN COMPLEX WITH IRON. RX PubMed=24616096; DOI=10.1074/jbc.M113.545590; RA Martinez A., Peluffo G., Petruk A.A., Hugo M., Pineyro D., Demicheli V., RA Moreno D.M., Lima A., Batthyany C., Duran R., Robello C., Marti M.A., RA Larrieux N., Buschiazzo A., Trujillo M., Radi R., Piacenza L.; RT "Structural and molecular basis of the peroxynitrite-mediated nitration and RT inactivation of Trypanosoma cruzi iron-superoxide dismutases (Fe-SODs) A RT and B: disparate susceptibilities due to the repair of Tyr35 radical by RT Cys83 in Fe-SODB through intramolecular electron transfer."; RL J. Biol. Chem. 289:12760-12778(2014). RN [3] {ECO:0007829|PDB:4H3E} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH IRON. RX PubMed=25961325; DOI=10.1107/S2053230X15004185; RA Phan I.Q., Davies D.R., Moretti N.S., Shanmugam D., Cestari I., Anupama A., RA Fairman J.W., Edwards T.E., Stuart K., Schenkman S., Myler P.J.; RT "Iron superoxide dismutases in eukaryotic pathogens: new insights from RT Apicomplexa and Trypanosoma structures."; RL Acta Crystallogr. F Struct. Biol. Commun. 71:615-621(2015). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000256|RuleBase:RU000414}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:18421; EC=1.15.1.1; CC Evidence={ECO:0000256|RuleBase:RU000414}; CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAN90306.1}. 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; AAHK01000648; EAN90306.1; -; Genomic_DNA. DR RefSeq; XP_812157.1; XM_807064.1. DR PDB; 4DVH; X-ray; 2.23 A; A/B=32-233. DR PDB; 4H3E; X-ray; 2.25 A; A/B=1-233. DR PDBsum; 4DVH; -. DR PDBsum; 4H3E; -. DR AlphaFoldDB; Q4DCQ3; -. DR SMR; Q4DCQ3; -. DR STRING; 353153.Q4DCQ3; -. DR BindingDB; Q4DCQ3; -. DR ChEMBL; CHEMBL4295602; -. DR PaxDb; 353153-Q4DCQ3; -. DR EnsemblProtists; EAN90306; EAN90306; Tc00.1047053509775.40. DR GeneID; 3543251; -. DR KEGG; tcr:509775.40; -. DR eggNOG; KOG0876; Eukaryota. DR InParanoid; Q4DCQ3; -. DR OMA; DHHGNVG; -. DR OrthoDB; 4839at2759; -. DR Proteomes; UP000002296; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1. DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR InterPro; IPR036324; Mn/Fe_SOD_N_sf. DR InterPro; IPR036314; SOD_C_sf. DR PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1. DR PANTHER; PTHR42769:SF12; SUPEROXIDE DISMUTASE; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1. DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4DVH, ECO:0007829|PDB:4H3E}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000349-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}; KW Reference proteome {ECO:0000313|Proteomes:UP000002296}. FT DOMAIN 35..117 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 126..226 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 59 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0007829|PDB:4H3E" FT BINDING 59 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0007829|PDB:4DVH" FT BINDING 59 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 110 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0007829|PDB:4H3E" FT BINDING 110 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0007829|PDB:4DVH" FT BINDING 110 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 194 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0007829|PDB:4H3E" FT BINDING 194 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0007829|PDB:4DVH" FT BINDING 194 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 198 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0007829|PDB:4H3E" FT BINDING 198 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0007829|PDB:4DVH" FT BINDING 198 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 233 AA; 26140 MW; 96464D3997DF5797 CRC64; MLRRAVNISI ARGRMALMSY ATLPDLLKPS GAPAELPKLG FNWKDGCAPV FSPRQMELHY TKHHKAYVDK LNALAGTTYD GKSIEEIILA VANDAEKKGL FNQAAQHFNH TFYFRCITPN GKAMPKSLES AVTAQFGSVE QFKDAFVQAG VNNFGSGWTW LCVDPSNKNQ LVIDNTSNAG CPLTKGLRPV LAVDVWEHAY YKDFENRRPD YLKEIWSVID WEFVAKMHAQ AIK //