SODF_PSET1
ID SODF_PSET1 Reviewed; 192 AA.
AC P84612; Q3IKP4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sodB {ECO:0000312|EMBL:CAI86290.1}; OrderedLocusNames=PSHAa1215;
OS Pseudoalteromonas translucida (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 haloplanktis:
RT biochemical characterization and identification of a highly reactive
RT 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., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT 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 systems.
CC {ECO:0000269|PubMed:16713057}.
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: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 family.
CC {ECO:0000255}.
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DR EMBL; CR954246; CAI86290.1; -; Genomic_DNA.
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 AlphaFoldDB; P84612; -.
DR SMR; P84612; -.
DR STRING; 326442.PSHAa1215; -.
DR EnsemblBacteria; CAI86290; CAI86290; PSHAa1215.
DR KEGG; pha:PSHAa1215; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_0_6; -.
DR OMA; YLHSIFW; -.
DR BRENDA; 1.15.1.1; 5081.
DR EvolutionaryTrace; P84612; -.
DR Proteomes; UP000006843; Chromosome I.
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; 3.55.40.20; -; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..192
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159970"
FT BINDING 26
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09157"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09157"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09157"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09157"
FT TURN 11..17
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:3LIO"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:3LIO"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:3LIO"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:3LIO"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3LIO"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:3LIO"
FT HELIX 184..191
FT /evidence="ECO:0007829|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
