SODF_METTM
ID SODF_METTM Reviewed; 202 AA.
AC Q60036; D9PVF8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sod; Synonyms=sodA; OrderedLocusNames=MTBMA_c06110;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=7781971; DOI=10.1111/j.1574-6968.1995.tb07532.x;
RA Meile L., Fischer K., Leisinger T.;
RT "Characterization of the superoxide dismutase gene and its upstream region
RT from Methanobacterium thermoautotrophicum Marburg.";
RL FEMS Microbiol. Lett. 128:247-253(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X74264; CAA52323.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58206.1; -; Genomic_DNA.
DR PIR; S51097; S51097.
DR RefSeq; WP_013295430.1; NC_014408.1.
DR AlphaFoldDB; Q60036; -.
DR SMR; Q60036; -.
DR STRING; 79929.MTBMA_c06110; -.
DR EnsemblBacteria; ADL58206; ADL58206; MTBMA_c06110.
DR GeneID; 9704319; -.
DR KEGG; mmg:MTBMA_c06110; -.
DR PATRIC; fig|79929.8.peg.595; -.
DR HOGENOM; CLU_031625_2_2_2; -.
DR OMA; KWGSFDK; -.
DR OrthoDB; 74803at2157; -.
DR Proteomes; UP000000345; Chromosome.
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; -; 1.
DR Gene3D; 3.55.40.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..202
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000160007"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 23829 MW; 5C4FBE27EEE63223 CRC64;
MEKKFYELPE LPYPYDALEP YISEEQLRIH HEKHHQAYVD GANGVLRKLD DARENGEEVD
IKAALKELSF HVGGYVLHLF FWGNMGPADE CGGEPDGRLA EYIEKDFGSF QRFKKEFSQA
AVSAEGSGWA VLTYCQRTDR LFIMQVEKHN VNVIPHFRIL MVLDVWEHAY YIDYRNVRPD
YVEAFWNIVN WKEVEKRFDD LF