ID Q5IZD9_ACACA Unreviewed; 197 AA.
AC Q5IZD9;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 64.
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};
OS Acanthamoeba castellanii (Amoeba).
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755 {ECO:0000313|EMBL:AAT91955.1};
RN [1] {ECO:0000313|EMBL:AAT91955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ma {ECO:0000313|EMBL:AAT91955.1};
RA Na B.-K., Cho J.-H., Kim T.-S., Kong Y.;
RT "Molecular cloning and characterization of iron-superoxide dismutase of
RT Acanthamoeba castellanii.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAT91955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ma {ECO:0000313|EMBL:AAT91955.1};
RX PubMed=22752747; DOI=10.1007/s00436-012-3006-7;
RA Kim J.Y., Na B.K., Song K.J., Park M.H., Park Y.K., Kim T.S.;
RT "Functional expression and characterization of an iron-containing
RT superoxide dismutase of Acanthamoeba castellanii.";
RL Parasitol. Res. 0:0-0(2012).
RN [3] {ECO:0007829|PDB:6J55}
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH FE(2+).
RX PubMed=31282867; DOI=10.1107/S2053230X19008112;
RA Dao O., Asaithambi K., Na B.K., Lee K.H.;
RT "Crystal structure of an iron superoxide dismutase from the pathogenic
RT amoeba Acanthamoeba castellanii.";
RL Acta Crystallogr. F 75:480-488(2019).
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}.
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DR EMBL; AY584067; AAT91955.1; -; mRNA.
DR PDB; 6J55; X-ray; 2.33 A; A/B/C/D/E/F/G/H/I/J/K/L=1-197.
DR PDBsum; 6J55; -.
DR AlphaFoldDB; Q5IZD9; -.
DR SMR; Q5IZD9; -.
DR VEuPathDB; AmoebaDB:ACA1_265580; -.
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:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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:6J55};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 3..86
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 96..193
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 27
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0007829|PDB:6J55"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 78
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0007829|PDB:6J55"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 161
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0007829|PDB:6J55"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 165
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0007829|PDB:6J55"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 197 AA; 22593 MW; F04C324BCB7AD230 CRC64;
MLFTLNDPAY LKTGLEPAIS AKTLDFHFNG HHKAYLNKTN DLVKGTSLEN KSLEDVILVA
KTTNNAALFN NATQLWNHSF FWDCMAPTNQ TGQISPELEK LIKESFGSVA DFKKKFTDSA
IANFGSGWTW LVNINGKLEI QNTSNAESPV TLRVTPLLTV DVWEHAYYLD HQNRRPEYLN
KWWEVVNWKF VDQQLKQ
//
