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Database: UniProt
Entry: T0D4I3_ALIAG
LinkDB: T0D4I3_ALIAG
Original site: T0D4I3_ALIAG 
ID   T0D4I3_ALIAG            Unreviewed;       202 AA.
AC   T0D4I3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=N007_10430 {ECO:0000313|EMBL:EPZ44646.1};
OS   Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP
OS   106132 / NCIMB 13137 / GD3B).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1356854 {ECO:0000313|EMBL:EPZ44646.1, ECO:0000313|Proteomes:UP000015607};
RN   [1] {ECO:0000313|EMBL:EPZ44646.1, ECO:0000313|Proteomes:UP000015607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49025 / DSM 3922 / CIP 106132 / NCIMB 13137 / GD3B
RC   {ECO:0000313|Proteomes:UP000015607};
RX   PubMed=24009113; DOI=10.1128/genomeA.00638-13;
RA   Shemesh M., Pasvolsky R., Sela N., Green S.J., Zakin V.;
RT   "Draft genome sequence of Alicyclobacillus acidoterrestris strain ATCC
RT   49025.";
RL   Genome Announc. 5:E00638-E00638(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EPZ44646.1}.
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DR   EMBL; AURB01000145; EPZ44646.1; -; Genomic_DNA.
DR   RefSeq; WP_021297139.1; NZ_AURB01000145.1.
DR   EnsemblBacteria; EPZ44646; EPZ44646; N007_10430.
DR   PATRIC; fig|1356854.4.peg.2526; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000015607; Unassembled WGS sequence.
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:UP000015607};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015607}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       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   202 AA;  22313 MW;  FA631AF678A06DF3 CRC64;
     MAHELPALPY AFDALEPHID ALTMEIHHDR HHGTYVTNLN KALEGQADLA NKSVEDLISD
     LNAVPENIRT AVRNNGGGHA NHSLFWKLLS PNGGGQPTGK LAEAINSTFG SFDKFKEQFN
     AAATGRFGSG WAWLVVDGGK LAIISTANQD NPLMEGKKPV LGLDVWEHAY YLKYQNKRPD
     YIAAFWNVVN WDEANKNYEA AL
//
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