ID F4G514_ALIDK Unreviewed; 193 AA.
AC F4G514;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 16-JAN-2019, entry version 40.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN OrderedLocusNames=Alide2_2940 {ECO:0000313|EMBL:AEB85287.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB85287.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB85287.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A.,
RA Gerritse J., van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A.,
RA Daligault H.E., Bruce D.C., Detter J.C., Tapia R., Han C.S.,
RA Land M.L., Hauser L.J., Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and
RT K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB85287.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
RA Oosterkamp M., Pieper D., van Berkel W., Langenhoff A., Smidt H.,
RA Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans
RT K601.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002657; AEB85287.1; -; Genomic_DNA.
DR RefSeq; WP_013722430.1; NC_015422.1.
DR STRING; 596154.Alide2_2940; -.
DR EnsemblBacteria; AEB85287; AEB85287; Alide2_2940.
DR KEGG; adk:Alide2_2940; -.
DR eggNOG; ENOG4105CK4; Bacteria.
DR eggNOG; COG0605; LUCA.
DR KO; K04564; -.
DR OMA; KWGSFDK; -.
DR BioCyc; ADEN596154:G1GW9-2955-MONOMER; -.
DR Proteomes; UP000007938; Chromosome.
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:UP000007938};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW ECO:0000313|EMBL:AEB85287.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007938}.
FT DOMAIN 2 81 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 89 190 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 74 74 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 157 157 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 161 161 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 193 AA; 21399 MW; DEBFB15C169F530F CRC64;
MEHKLPALPY AIDALAPHYS QETLEYHHGK HHNAYVVNLN NLQKGTEFEN MTLEEIVKKS
SGGIYNNAAQ IWNHTFFWNC MTPNGGGEPG GALAAAINAK WGSYAAFKEA FVKSAVGNFG
SGWTWLVKKA DGSVDIVNTG AAGTPLTTAD KALLTVDVWE HAYYIDYRNL RPKFVETFLD
KLVNWKFAEA NFA
//
