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Database: UniProt
Entry: U1JN76_9GAMM
LinkDB: U1JN76_9GAMM
Original site: U1JN76_9GAMM 
ID   U1JN76_9GAMM            Unreviewed;       204 AA.
AC   U1JN76;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   28-MAR-2018, entry version 18.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PCIT_11234 {ECO:0000313|EMBL:ERG18452.1};
OS   Pseudoalteromonas citrea DSM 8771.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG18452.1, ECO:0000313|Proteomes:UP000016487};
RN   [1] {ECO:0000313|EMBL:ERG18452.1, ECO:0000313|Proteomes:UP000016487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L.,
RA   Shi M., He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine
RT   bacterium Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
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}.
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:ERG18452.1}.
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DR   EMBL; AHBZ02000130; ERG18452.1; -; Genomic_DNA.
DR   RefSeq; WP_010361770.1; NZ_AHBZ02000130.1.
DR   EnsemblBacteria; ERG18452; ERG18452; PCIT_11234.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000016487; 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:UP000016487};
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:UP000016487}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       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;  23111 MW;  E2305E930854893F CRC64;
     MAFTLPALPY AYDALEPHID AKTMEIHHTL HHQTYINKAN AALEGSEFSD KPTQWLLNNI
     KTLPESLQKA VQEHVGGHNN HSLFWQVMSP TGGTLQAGKL ATAIDETFGS FDEFKALFTA
     AAVSRFGSGW AWLVVDENQQ LQVTSSLNQD SPFMDQHTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFYNVIN WQDVERRFLA ALSS
//
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