GenomeNet

Database: UniProt/TrEMBL
Entry: S5TMJ2_9CORY
LinkDB: S5TMJ2_9CORY
Original site: S5TMJ2_9CORY 
ID   S5TMJ2_9CORY            Unreviewed;       200 AA.
AC   S5TMJ2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 27.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=B841_12155 {ECO:0000313|EMBL:AGS35903.1};
OS   Corynebacterium maris DSM 45190.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS35903.1, ECO:0000313|Proteomes:UP000015388};
RN   [1] {ECO:0000313|EMBL:AGS35903.1, ECO:0000313|Proteomes:UP000015388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT   45190).";
RL   Submitted (NOV-2012) 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: 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; CP003924; AGS35903.1; -; Genomic_DNA.
DR   RefSeq; WP_020936484.1; NC_021915.1.
DR   EnsemblBacteria; AGS35903; AGS35903; B841_12155.
DR   KEGG; cmd:B841_12155; -.
DR   PATRIC; fig|1224163.3.peg.2455; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000015388; 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:UP000015388};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015388}.
FT   DOMAIN        4     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       92    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22460 MW;  61E38ACF2D59AE17 CRC64;
     MAVYELPELD YAYDALEPHI SAEIMELHHS KHHANYVAGA NAALEALEKL REEGTNQDAV
     RALSKNLAFN LGGHTNHTIF WKNLSPNGGG EPTGELAEAI NRDFGSFEKF KDHFSNAALA
     LHGSGWAVLG YDHIADRLII QQLTDQQGNV SVDFTPLLML DMWEHAFYLQ YKNVKADYVK
     AVWNVFNWDD VAARYADAKK
//
DBGET integrated database retrieval system