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 01-MAY-2013, entry version 57.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sodB; 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]
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.
CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC -!- COFACTOR: Binds 1 iron ion per subunit.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC family.
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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 PDBsum; 3LIO; -.
DR PDBsum; 3LJ9; -.
DR PDBsum; 3LJF; -.
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; NCMAPNG; -.
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:EC.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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; SODismutase; 1.
DR SUPFAM; SSF54719; SODismutase; 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.
FT CHAIN 1 192 Superoxide dismutase [Fe].
FT /FTId=PRO_0000159970.
FT METAL 26 26 Iron (By similarity).
FT METAL 73 73 Iron (By similarity).
FT METAL 157 157 Iron (By similarity).
FT METAL 161 161 Iron (By similarity).
FT TURN 11 17
FT HELIX 20 26
FT TURN 27 29
FT HELIX 30 41
FT TURN 46 49
FT HELIX 52 56
FT HELIX 61 78
FT HELIX 90 100
FT HELIX 103 115
FT STRAND 119 127
FT STRAND 133 139
FT HELIX 144 146
FT STRAND 151 157
FT HELIX 160 162
FT HELIX 164 167
FT HELIX 171 181
FT HELIX 184 191
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
//
