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Database: UniProt
Entry: F4G514_ALIDK
LinkDB: F4G514_ALIDK
Original site: F4G514_ALIDK 
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
//
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