GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0G2RPY4_FRATT Q5NIJ9_FRATT
LinkDB: A0A0G2RPY4_FRATT Q5NIJ9_FRATT
Original site: A0A0G2RPY4_FRATT Q5NIJ9_FRATT 
ID   A0A0G2RPY4_FRATT        Unreviewed;       192 AA.
AC   A0A0G2RPY4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   25-OCT-2017, entry version 4.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:AJI69383.1};
GN   ORFNames=BZ14_823 {ECO:0000313|EMBL:AJI69383.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:AJI69383.1, ECO:0000313|Proteomes:UP000031862};
RN   [1] {ECO:0000313|EMBL:AJI69383.1, ECO:0000313|Proteomes:UP000031862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 {ECO:0000313|Proteomes:UP000031862};
RX   PubMed=25931589;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA   Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C.,
RA   Chertkov O., Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N.,
RA   Gibbons H.S., Palacios G.F., Redden C.L., Xu Y., Minogue T.D.,
RA   Chain P.S.;
RT   "Genome sequencing of 18 francisella strains to aid in assay
RT   development and testing.";
RL   Genome Announc. 3:0-0(2015).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP010290; AJI69383.1; -; Genomic_DNA.
DR   RefSeq; WP_003017326.1; NZ_CP010290.1.
DR   RefSeq; YP_169143.1; NC_006570.2.
DR   SMR; A0A0G2RPY4; -.
DR   GeneID; 3190713; -.
DR   KEGG; ftu:FTT_0068; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   Proteomes; UP000031862; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:UP000031862};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AJI69383.1}.
FT   DOMAIN        2     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    188       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       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21940 MW;  5218CC2D26037774 CRC64;
     MKFELPKLPY AVDALESTIS KETIEYHYGK HHQTYVTNLN NLVEGTEHDG RNLEEIVKTS
     NGGIFNNAAQ VFNHTFYWNC LTPNKTEASS QLKAALIETF GSVENFKEQF SKAAIATFGS
     GWAWLVKNTE GKLEIVTTSN AGCPLTENKK PLLTFDVWEH AYYIDYRNAR PKYVEALWDI
     VNWQFVSEQF AD
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

Download RDF
ID   Q5NIJ9_FRATT            Unreviewed;       192 AA.
AC   Q5NIJ9;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   25-OCT-2017, entry version 95.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:CAG44701.1};
GN   OrderedLocusNames=FTT_0068 {ECO:0000313|EMBL:CAG44701.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG44701.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG44701.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M.,
RA   Fuxelius H.H., Garcia E., Halltorp G., Johansson D., Isherwood K.,
RA   Karp P., Larsson E., Lui Y., Michell S., Prior J., Prior R.,
RA   Sjostedt A., Svensson K., Thompson N., Vergez L., Wagg J., Wren B.,
RA   Lindler L.E., Andersson S.G., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
RN   [2] {ECO:0000213|PDB:3H1S}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON.
RA   Nocek B., Zhou M., Papazisi L., Anderson W.F., Joachimiak A.;
RT   "Crystal structure of superoxide dismutase from Francisella tularensis
RT   subsp. tularensis SCHU S4.";
RL   Submitted (APR-2009) to the PDB data bank.
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ749949; CAG44701.1; -; Genomic_DNA.
DR   RefSeq; WP_003017326.1; NZ_CP010290.1.
DR   RefSeq; YP_169143.1; NC_006570.2.
DR   PDB; 3H1S; X-ray; 1.90 A; A/B=1-192.
DR   PDBsum; 3H1S; -.
DR   SMR; Q5NIJ9; -.
DR   STRING; 177416.FTT_0068; -.
DR   DNASU; 3190713; -.
DR   EnsemblBacteria; AJI69383; AJI69383; BZ14_823.
DR   EnsemblBacteria; CAG44701; CAG44701; FTT_0068.
DR   GeneID; 3190713; -.
DR   KEGG; ftu:FTT_0068; -.
DR   PATRIC; fig|177416.18.peg.74; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; DHHGNVG; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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 {ECO:0000213|PDB:3H1S};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001174};
KW   Iron {ECO:0000213|PDB:3H1S};
KW   Metal-binding {ECO:0000213|PDB:3H1S, ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CAG44701.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        27     27       Iron; via tele nitrogen.
FT                                {ECO:0000213|PDB:3H1S}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Iron; via tele nitrogen.
FT                                {ECO:0000213|PDB:3H1S}.
FT   METAL       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       156    156       Iron. {ECO:0000213|PDB:3H1S}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Iron; via tele nitrogen.
FT                                {ECO:0000213|PDB:3H1S}.
SQ   SEQUENCE   192 AA;  21940 MW;  5218CC2D26037774 CRC64;
     MKFELPKLPY AVDALESTIS KETIEYHYGK HHQTYVTNLN NLVEGTEHDG RNLEEIVKTS
     NGGIFNNAAQ VFNHTFYWNC LTPNKTEASS QLKAALIETF GSVENFKEQF SKAAIATFGS
     GWAWLVKNTE GKLEIVTTSN AGCPLTENKK PLLTFDVWEH AYYIDYRNAR PKYVEALWDI
     VNWQFVSEQF AD
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
3D Structure (1)   
   PDB (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

Download RDF
DBGET integrated database retrieval system