GenomeNet

Database: UniProt/TrEMBL
Entry: A4SYN5_POLAQ
LinkDB: A4SYN5_POLAQ
Original site: A4SYN5_POLAQ 
ID   A4SYN5_POLAQ            Unreviewed;       192 AA.
AC   A4SYN5;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   25-OCT-2017, entry version 64.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Pnuc_1385 {ECO:0000313|EMBL:ABP34599.1};
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP34599.1, ECO:0000313|Proteomes:UP000000231};
RN   [1] {ECO:0000313|EMBL:ABP34599.1, ECO:0000313|Proteomes:UP000000231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1
RC   {ECO:0000313|Proteomes:UP000000231};
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34599.1; -; Genomic_DNA.
DR   RefSeq; WP_011903224.1; NC_009379.1.
DR   ProteinModelPortal; A4SYN5; -.
DR   STRING; 312153.Pnuc_1385; -.
DR   EnsemblBacteria; ABP34599; ABP34599; Pnuc_1385.
DR   GeneID; 31481776; -.
DR   KEGG; pnu:Pnuc_1385; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; PNEC312153:GH50-1415-MONOMER; -.
DR   Proteomes; UP000000231; 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:UP000000231};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ABP34599.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000231}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       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   192 AA;  21384 MW;  B900F078BBD23A81 CRC64;
     MEHTLPPLPY ALDALAPHIS KETLEYHYGK HHQAYVTNLN NLIKGTEFEA LSLEDIIKKS
     AAGVFNNAAQ VWNHTFYWNS LKPNGGGAPT GPLADAINAK WGSFDKFKEE FNKCAVGTFG
     SGWAWLVKKA DGSLDLVSTS NAATPLTTDA KPLLTCDVWE HAYYIDTRNA RPKYLENFWN
     VVNWDFASSN FA
//
DBGET integrated database retrieval system