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Database: UniProt/TrEMBL
Entry: A0A0B6CRX6_9GAMM
LinkDB: A0A0B6CRX6_9GAMM
Original site: A0A0B6CRX6_9GAMM 
ID   A0A0B6CRX6_9GAMM        Unreviewed;       192 AA.
AC   A0A0B6CRX6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 14.
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:AJI53234.1};
GN   ORFNames=LA55_1916 {ECO:0000313|EMBL:AJI53234.1};
OS   Francisella philomiragia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=28110 {ECO:0000313|EMBL:AJI53234.1, ECO:0000313|Proteomes:UP000031830};
RN   [1] {ECO:0000313|EMBL:AJI53234.1, ECO:0000313|Proteomes:UP000031830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA01-2794 {ECO:0000313|EMBL:AJI53234.1,
RC   ECO:0000313|Proteomes:UP000031830};
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}.
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DR   EMBL; CP009440; AJI53234.1; -; Genomic_DNA.
DR   RefSeq; WP_044526937.1; NZ_CP009440.1.
DR   EnsemblBacteria; AJI53234; AJI53234; LA55_1916.
DR   KEGG; fpz:LA55_1916; -.
DR   KO; K04564; -.
DR   Proteomes; UP000031830; 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:UP000031830};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AJI53234.1}.
FT   DOMAIN        2     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       88    187       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;  21883 MW;  B7E4ADC1016A2779 CRC64;
     MKFELPKLPY ALDALEPTIS KETIEYHYGK HHQTYVTNLN NLVEGTEHAG KNLEEIIKTS
     SGGIFNNSAQ VYNHTFYWNC LTPSKTQPSS QLKAAIIETF GSIDNFKDQF SKAAVATFGS
     GWAWLVKNTE GKLEIVTTSN AGCPLTDNKK PLLTFDVWEH AYYIDYRNAR PKYVESLWDI
     VNWEFVSGQF EK
//
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