GenomeNet

Database: UniProt/TrEMBL
Entry: E1RBS5_SEDSS
LinkDB: E1RBS5_SEDSS
Original site: E1RBS5_SEDSS 
ID   E1RBS5_SEDSS            Unreviewed;       202 AA.
AC   E1RBS5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Spirs_0665 {ECO:0000313|EMBL:ADK79805.1};
OS   Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR
OS   4228) (Spirochaeta smaragdinae).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae;
OC   Sediminispirochaeta.
OX   NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK79805.1, ECO:0000313|Proteomes:UP000002318};
RN   [1] {ECO:0000313|EMBL:ADK79805.1, ECO:0000313|Proteomes:UP000002318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC   {ECO:0000313|Proteomes:UP000002318};
RX   DOI=10.4056/sigs.1143106;
RA   Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S.,
RA   Nolan M., Glavina Del Rio T., Tice H., Cheng J., Pitluck S.,
RA   Liolios K., Ivanova N., Tapia R., Han C., Bruce D., Goodwin L.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Detter J., Rohde M., Brambilla E., Spring S., Goker M.,
RA   Sikorski J., Woyke T., Bristow J., Eisen J., Markowitz V.,
RA   Hugenholtz P., Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT   4228).";
RL   Stand. Genomic Sci. 3:136-144(2010).
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; CP002116; ADK79805.1; -; Genomic_DNA.
DR   RefSeq; WP_013253269.1; NC_014364.1.
DR   ProteinModelPortal; E1RBS5; -.
DR   STRING; 573413.Spirs_0665; -.
DR   EnsemblBacteria; ADK79805; ADK79805; Spirs_0665.
DR   KEGG; ssm:Spirs_0665; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; SSMA573413:GI0C-655-MONOMER; -.
DR   Proteomes; UP000002318; 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   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:UP000002318};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ADK79805.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002318}.
FT   DOMAIN        3     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  22267 MW;  9D583C50CF9B46C7 CRC64;
     MSFITPDLPY AYDALEPYID ERTMRVHHDK HHAGYTAKLN NAVEGTVYAG KSIEELLAGL
     DALPENIRTG VRNNGGGHYN HSLFWKVMGP KGGGKPEGAL AEKIDSSFGG FDVFISEFSA
     AAASRFGSGW AWLAVDPNGS LSVLSTANQD SPLTQGLVPI LGLDVWEHAY YLKYQNRRPE
     YIESFFKVIN WPKVAELYKA AI
//
DBGET integrated database retrieval system