ID C0DWA0_EIKCO Unreviewed; 207 AA.
AC C0DWA0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 16-JAN-2019, entry version 36.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=EIKCOROL_01649 {ECO:0000313|EMBL:EEG23679.1};
OS Eikenella corrodens ATCC 23834.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Eikenella.
OX NCBI_TaxID=546274 {ECO:0000313|EMBL:EEG23679.1, ECO:0000313|Proteomes:UP000005837};
RN [1] {ECO:0000313|EMBL:EEG23679.1, ECO:0000313|Proteomes:UP000005837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23834 {ECO:0000313|EMBL:EEG23679.1,
RC ECO:0000313|Proteomes:UP000005837};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:
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: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:EEG23679.1}.
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DR EMBL; ACEA01000033; EEG23679.1; -; Genomic_DNA.
DR RefSeq; WP_003823764.1; NZ_EQ973320.1.
DR ProteinModelPortal; C0DWA0; -.
DR STRING; 546274.EIKCOROL_01649; -.
DR EnsemblBacteria; EEG23679; EEG23679; EIKCOROL_01649.
DR GeneID; 29691384; -.
DR eggNOG; ENOG4105CK4; Bacteria.
DR eggNOG; COG0605; LUCA.
DR OrthoDB; 1440645at2; -.
DR Proteomes; UP000005837; 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:UP000005837};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW ECO:0000313|EMBL:EEG23679.1}.
FT DOMAIN 2 90 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 96 201 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 82 82 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 168 168 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 172 172 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 207 AA; 23366 MW; 4DCD04BDED3B1739 CRC64;
MAYQLPALLY AYDALEPHFD TQTMEIHHSK HHQAYVNNAN AVLANLSEWE KLSAEELIAR
LAELPENVRI PLRNNAGGHA NHSLFWQILK TGTTLQGKLK AAIERDFGSV EAFQAEFEKA
AATRFGSGWA WLVYEDGKLK VVSTANQDSP LMGQAVSGTS GYPIIGLDVW EHAYYLKFQN
RRPDYIKAFW QVVNWDEAAR RFESVAA
//
