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Database: UniProt/TrEMBL
Entry: A4IQZ1_GEOTN
LinkDB: A4IQZ1_GEOTN
Original site: A4IQZ1_GEOTN 
ID   A4IQZ1_GEOTN            Unreviewed;       204 AA.
AC   A4IQZ1;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=GTNG_2400 {ECO:0000313|EMBL:ABO67745.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO67745.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO67745.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO67745.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil
RT   reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP000557; ABO67745.1; -; Genomic_DNA.
DR   RefSeq; WP_008879878.1; NC_009328.1.
DR   ProteinModelPortal; A4IQZ1; -.
DR   STRING; 420246.GTNG_2400; -.
DR   EnsemblBacteria; ABO67745; ABO67745; GTNG_2400.
DR   GeneID; 31761644; -.
DR   KEGG; gtn:GTNG_2400; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; GTHE420246:GIXT-2457-MONOMER; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   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:UP000001578};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22780 MW;  318C07288149C9B2 CRC64;
     MPFELPALPY AYDALEPHID KETMTIHHTK HHNTYVTNLN AALEGHADLQ NKSLEELLSN
     LEALPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPTGE LAEAINKKFG SFAAFKDEFS
     KAAAGRFGSG WAWLVVNNGE LEITSTPNQD SPIMEGKTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFWNVVN WDEVAKRYSE AKAK
//
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