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Database: UniProt
Entry: P84612
LinkDB: P84612
Original site: P84612 
ID   SODF_PSEHT              Reviewed;         192 AA.
AC   P84612; Q3IKP4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   26-NOV-2014, entry version 65.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB {ECO:0000312|EMBL:CAI86290.1}; OrderedLocusNames=PSHAa1215;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=16713057; DOI=10.1016/j.biochi.2006.04.005;
RA   Castellano I., Di Maro A., Ruocco M.R., Chambery A., Parente A.,
RA   Di Martino M.T., Parlato G., Masullo M., De Vendittis E.;
RT   "Psychrophilic superoxide dismutase from Pseudoalteromonas
RT   haloplanktis: biochemical characterization and identification of a
RT   highly reactive cysteine residue.";
RL   Biochimie 88:1377-1389(2006).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000269|PubMed:16713057}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000269|PubMed:16713057}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:16713057};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:16713057};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P09157}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000255}.
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DR   EMBL; CR954246; CAI86290.1; -; Genomic_DNA.
DR   RefSeq; YP_339733.1; NC_007481.1.
DR   PDB; 3LIO; X-ray; 1.50 A; A/B=1-192.
DR   PDB; 3LJ9; X-ray; 2.10 A; A/B=1-192.
DR   PDB; 3LJF; X-ray; 2.10 A; A/B/C/D=1-192.
DR   PDB; 4L2A; X-ray; 2.06 A; A/B=1-192.
DR   PDB; 4L2B; X-ray; 1.97 A; A/B=1-192.
DR   PDB; 4L2C; X-ray; 1.66 A; A/B/C/D=1-192.
DR   PDB; 4L2D; X-ray; 2.07 A; A/B/C/D=1-192.
DR   PDBsum; 3LIO; -.
DR   PDBsum; 3LJ9; -.
DR   PDBsum; 3LJF; -.
DR   PDBsum; 4L2A; -.
DR   PDBsum; 4L2B; -.
DR   PDBsum; 4L2C; -.
DR   PDBsum; 4L2D; -.
DR   ProteinModelPortal; P84612; -.
DR   SMR; P84612; 1-191.
DR   STRING; 326442.PSHAa1215; -.
DR   EnsemblBacteria; CAI86290; CAI86290; PSHAa1215.
DR   GeneID; 3710743; -.
DR   KEGG; pha:PSHAa1215; -.
DR   PATRIC; 32296007; VBIPseHal105694_1169.
DR   eggNOG; COG0605; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; WTWLVKG; -.
DR   OrthoDB; EOG63NMNT; -.
DR   BioCyc; PHAL326442:GJIU-1249-MONOMER; -.
DR   EvolutionaryTrace; P84612; -.
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   PANTHER; PTHR11404; PTHR11404; 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; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Iron;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN         1    192       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159970.
FT   METAL        26     26       Iron. {ECO:0000250|UniProtKB:P09157}.
FT   METAL        73     73       Iron. {ECO:0000250|UniProtKB:P09157}.
FT   METAL       157    157       Iron. {ECO:0000250|UniProtKB:P09157}.
FT   METAL       161    161       Iron. {ECO:0000250|UniProtKB:P09157}.
FT   TURN         11     17       {ECO:0000244|PDB:3LIO}.
FT   HELIX        20     26       {ECO:0000244|PDB:3LIO}.
FT   TURN         27     29       {ECO:0000244|PDB:3LIO}.
FT   HELIX        30     41       {ECO:0000244|PDB:3LIO}.
FT   TURN         46     49       {ECO:0000244|PDB:3LIO}.
FT   HELIX        52     56       {ECO:0000244|PDB:3LIO}.
FT   HELIX        61     78       {ECO:0000244|PDB:3LIO}.
FT   HELIX        90    100       {ECO:0000244|PDB:3LIO}.
FT   HELIX       103    115       {ECO:0000244|PDB:3LIO}.
FT   STRAND      119    127       {ECO:0000244|PDB:3LIO}.
FT   STRAND      133    139       {ECO:0000244|PDB:3LIO}.
FT   HELIX       144    146       {ECO:0000244|PDB:3LIO}.
FT   STRAND      151    157       {ECO:0000244|PDB:3LIO}.
FT   HELIX       160    162       {ECO:0000244|PDB:3LIO}.
FT   HELIX       164    167       {ECO:0000244|PDB:3LIO}.
FT   HELIX       171    181       {ECO:0000244|PDB:3LIO}.
FT   HELIX       184    191       {ECO:0000244|PDB:3LIO}.
SQ   SEQUENCE   192 AA;  21251 MW;  53500221A8568E27 CRC64;
     AFELPSLPYA IDALEPHISK ETLEFHHGKH HNTYVVKLNG LIPGTKFENK SLEEIVCSSD
     GGVFNNAAQI WNHTFYWNSL SPNGGGAPTG AVADAINAKW GSFDAFKEAL NDKAVNNFGS
     SWTWLVKLAD GSLDIVNTSN AATPLTDDGV TPILTVDLWE HAYYIDYRNV RPDYLKGFWS
     LVNWEFANAN FA
//
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