ID Q8TQG9_METAC Unreviewed; 209 AA.
AC Q8TQG9;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 116.
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 Name=sodB {ECO:0000313|EMBL:AAM04987.1};
GN OrderedLocusNames=MA_1574 {ECO:0000313|EMBL:AAM04987.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM04987.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM04987.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM04987.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TQG9; -.
DR SMR; Q8TQG9; -.
DR STRING; 188937.MA_1574; -.
DR EnsemblBacteria; AAM04987; AAM04987; MA_1574.
DR KEGG; mac:MA_1574; -.
DR HOGENOM; CLU_031625_2_2_2; -.
DR InParanoid; Q8TQG9; -.
DR PhylomeDB; Q8TQG9; -.
DR Proteomes; UP000002487; 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; 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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 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 3: Inferred from homology;
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:UP000002487}.
FT DOMAIN 12..91
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 102..201
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 209 AA; 24580 MW; 98BD06FDB262DF13 CRC64;
MKRVYNMAKD LYKLPPLKYG YADLEPYISE EQLRIHHDKH HQGYVNNTNA LLEMMDKARK
EDTDFDYKAT AKALSFNLSG HVLHDFFWWE MTPASNASKE PVGEFAEAIK EDFGSFERFK
KEFSKVASSV EGSGWAALTF CKGTKRLGIV QIEKHNVNLV PDFPIIMDLD VWEHAYYIDY
KNDRGKFIEG FWNIIDWEEL DKYFKKIQK
//
