SODF_PSEPU
ID SODF_PSEPU Reviewed; 198 AA.
AC P09223; P77928; Q9AIX5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sodB;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Corvallis;
RX PubMed=10571042; DOI=10.1016/s0378-1119(99)00369-8;
RA Kim Y.C., Miller C.D., Anderson A.J.;
RT "Transcriptional regulation by iron of genes encoding iron- and manganese-
RT superoxide dismutases from Pseudomonas putida.";
RL Gene 239:129-135(1999).
RN [2] {ECO:0007744|PDB:1DT0}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS)
RP OF 2-197 IN COMPLEX WITH IRON, COFACTOR, AND SUBUNIT.
RC STRAIN=Ovalis;
RX PubMed=11053832; DOI=10.1107/s0907444900009537;
RA Bond C.J., Huang J.-Y., Hajduk R., Flick K.E., Heath P.J., Stoddard B.L.;
RT "Cloning, sequence and crystallographic structure of recombinant iron
RT superoxide dismutase from Pseudomonas ovalis.";
RL Acta Crystallogr. D 56:1359-1366(2000).
RN [3]
RP PROTEIN SEQUENCE OF 2-198.
RC STRAIN=Ovalis;
RX PubMed=3666146; DOI=10.1016/0014-5793(87)80516-1;
RA Isobe T., Fang Y.-I., Muno D., Okuyama T., Ohmori D., Yamakura F.;
RT "Amino acid sequence of iron-superoxide dismutase from Pseudomonas
RT ovalis.";
RL FEBS Lett. 223:92-96(1987).
RN [4]
RP PROTEIN SEQUENCE OF 2-36.
RC STRAIN=Ovalis;
RX PubMed=7341230; DOI=10.1111/j.1432-1033.1980.tb06023.x;
RA Harris J.I., Auffret A.D., Northrop F.D., Walker J.E.;
RT "Structural comparisons of superoxide dismutases.";
RL Eur. J. Biochem. 106:297-303(1980).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC STRAIN=Ovalis;
RX PubMed=6575382; DOI=10.1073/pnas.80.13.3879;
RA Ringe D., Petsko G.A., Yamakura F., Suzuki K., Ohmori D.;
RT "Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9-A
RT resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3879-3883(1983).
RN [6] {ECO:0007744|PDB:3SDP}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC STRAIN=Ovalis;
RX PubMed=2271564; DOI=10.1021/bi00490a002;
RA Stoddard B.L., Howell P.L., Ringe D., Petsko G.A.;
RT "The 2.1-A resolution structure of iron superoxide dismutase from
RT Pseudomonas ovalis.";
RL Biochemistry 29:8885-8893(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF COMPLEX WITH AZIDE.
RC STRAIN=Ovalis;
RX PubMed=2075185; DOI=10.1093/protein/4.2.113;
RA Stoddard B.L., Ringe D., Petsko G.A.;
RT "The structure of iron superoxide dismutase from Pseudomonas ovalis
RT complexed with the inhibitor azide.";
RL Protein Eng. 4:113-119(1990).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:11053832};
CC Note=Binds 1 Fe (3+) cation per subunit. {ECO:0000269|PubMed:11053832};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11053832}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; U64798; AAB06332.1; -; Genomic_DNA.
DR EMBL; AF222862; AAK14938.1; -; Genomic_DNA.
DR PIR; S00157; S00157.
DR RefSeq; WP_012274023.1; NZ_RJAH01000002.1.
DR PDB; 1DT0; X-ray; 2.10 A; A/B/C=2-195.
DR PDB; 3SDP; X-ray; 2.10 A; A/B=2-198.
DR PDBsum; 1DT0; -.
DR PDBsum; 3SDP; -.
DR AlphaFoldDB; P09223; -.
DR SMR; P09223; -.
DR STRING; 1240350.AMZE01000055_gene528; -.
DR PRIDE; P09223; -.
DR GeneID; 66680115; -.
DR eggNOG; COG0605; Bacteria.
DR OrthoDB; 1440645at2; -.
DR BRENDA; 1.15.1.1; 5092.
DR EvolutionaryTrace; P09223; -.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3666146,
FT ECO:0000269|PubMed:7341230"
FT CHAIN 2..198
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159995"
FT BINDING 27
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11053832"
FT BINDING 74
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11053832"
FT BINDING 157
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11053832"
FT BINDING 161
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11053832"
FT CONFLICT 26
FT /note="F -> Y (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="T -> TP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..85
FT /note="APNA -> SPDG (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> E (in Ref. 2; AAK14938)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> S (in Ref. 2; AAK14938)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="G -> D (in Ref. 2; AAK14938)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="G -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="W -> C (in Ref. 2; AAK14938)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> C (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="C -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> I (in Ref. 2; AAK14938)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..198
FT /note="FKA -> YKV (in Ref. 2; AAK14938)"
FT /evidence="ECO:0000305"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1DT0"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:1DT0"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3SDP"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1DT0"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:1DT0"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1DT0"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:1DT0"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1DT0"
SQ SEQUENCE 198 AA; 21935 MW; 99AF355F298D779D CRC64;
MAFELPPLPY AHDALQPHIS KETLEFHHDK HHNTYVVNLN NLVPGTEFEG KTLEEIVKTS
SGGIFNNAAQ VWNHTFYWNC LAPNAGGQPT GALADAINAA FGSFDKFKEE FTKTSVGTFG
SGWGWLVKKA DGSLALASTI GAGCPLTSGD TPLLTCDVWE HAYYIDYRNL RPKYVEAFWN
LVNWAFVAEQ FEGKTFKA
