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Database: UniProt
Entry: Q604S8_METCA
LinkDB: Q604S8_METCA
Original site: Q604S8_METCA 
ID   Q604S8_METCA            Unreviewed;       194 AA.
AC   Q604S8;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   16-JAN-2019, entry version 84.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB-2 {ECO:0000313|EMBL:AAU91441.1};
GN   OrderedLocusNames=MCA2458 {ECO:0000313|EMBL:AAU91441.1};
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU91441.1, ECO:0000313|Proteomes:UP000006821};
RN   [1] {ECO:0000313|EMBL:AAU91441.1, ECO:0000313|Proteomes:UP000006821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC   {ECO:0000313|Proteomes:UP000006821};
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E.,
RA   Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R.,
RA   Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J.,
RA   Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S.,
RA   Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R.,
RA   Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; AE017282; AAU91441.1; -; Genomic_DNA.
DR   RefSeq; WP_010961683.1; NC_002977.6.
DR   ProteinModelPortal; Q604S8; -.
DR   STRING; 243233.MCA2458; -.
DR   EnsemblBacteria; AAU91441; AAU91441; MCA2458.
DR   KEGG; mca:MCA2458; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; MCAP243233:G1G0X-2432-MONOMER; -.
DR   Proteomes; UP000006821; 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; 2.40.500.20; -; 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   Complete proteome {ECO:0000313|Proteomes:UP000006821};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AAU91441.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006821}.
FT   DOMAIN        2     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        75     75       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   194 AA;  21499 MW;  DD63D8B554B9EB55 CRC64;
     MTHELPALPY AKTALEPHIS AETLEYHYGK HHQTYVTNLN NLIPGTEYEN LSLEEIIRKA
     PAGGVFNNAA QVWNHTFYWN SLSPNGGGEP TGALAEAIVK SFGSFEKFKE AFTQCAVTTF
     GSGWAWLVKN ADGSLALVST SNAGCPLTSD QTPLLTCDVW EHAYYIDYRN ARPKYLEAFW
     NLVNWEFAAA NFAG
//
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