GenomeNet

Database: UniProt
Entry: B4S837_PROA2
LinkDB: B4S837_PROA2
Original site: B4S837_PROA2 
ID   B4S837_PROA2            Unreviewed;       201 AA.
AC   B4S837;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 65.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Paes_1195 {ECO:0000313|EMBL:ACF46224.1};
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF46224.1, ECO:0000313|Proteomes:UP000002725};
RN   [1] {ECO:0000313|EMBL:ACF46224.1, ECO:0000313|Proteomes:UP000002725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM
RT   271.";
RL   Submitted (JUN-2008) 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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={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 https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001108; ACF46224.1; -; Genomic_DNA.
DR   RefSeq; WP_012505759.1; NC_011059.1.
DR   ProteinModelPortal; B4S837; -.
DR   STRING; 290512.Paes_1195; -.
DR   EnsemblBacteria; ACF46224; ACF46224; Paes_1195.
DR   KEGG; paa:Paes_1195; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; PAES290512:G1GCD-1221-MONOMER; -.
DR   Proteomes; UP000002725; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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:UP000002725};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACF46224.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002725}.
FT   DOMAIN        3     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       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   201 AA;  22118 MW;  85F576AFCAE081EA CRC64;
     MAYQQPSLPY AENALEPYIS ANTISFHYGK HHATYVKKFN EMVAGTPLDQ QSIEEVVKTV
     AGDASKAGIF NNGAQAWNHS FYWNCLSPDG GGKPSGSLAD KIDQDFGSYD TFREELANAA
     ATQFGSGWAW LVLDNGTLKV TKTANAQTPV TEGMTPILTI DVWEHAYYLD YQNRRPDYVA
     SLIDNLVNWD FATSNFEAAG A
//
DBGET integrated database retrieval system