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Database: UniProt
Entry: A0A221AFZ0_9BURK
LinkDB: A0A221AFZ0_9BURK
Original site: A0A221AFZ0_9BURK 
ID   A0A221AFZ0_9BURK        Unreviewed;       248 AA.
AC   A0A221AFZ0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-DEC-2018, entry version 6.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
DE   Flags: Precursor;
GN   Name=sodB {ECO:0000313|EMBL:ASL47389.1};
GN   ORFNames=bAD24_III08335 {ECO:0000313|EMBL:ASL47389.1};
OS   Burkholderia sp. AD24.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1528693 {ECO:0000313|EMBL:ASL47389.1, ECO:0000313|Proteomes:UP000198392};
RN   [1] {ECO:0000313|EMBL:ASL47389.1, ECO:0000313|Proteomes:UP000198392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD24 {ECO:0000313|EMBL:ASL47389.1,
RC   ECO:0000313|Proteomes:UP000198392};
RA   Tyc O., de Jager V., van den Berg M., Gerards S., Janssens T.,
RA   Zagman N., Kai M., Svatos A., Zweer H., Hordijk C., Besselink H.,
RA   de Boer W., Garbeva P.;
RT   "Exploring bacterial inter-specific interactions for discovery of
RT   novel antimicrobial compounds.";
RL   Submitted (JUL-2016) 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}.
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DR   EMBL; CP016435; ASL47389.1; -; Genomic_DNA.
DR   Proteomes; UP000198392; Chromosome ii sequence.
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:UP000198392};
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:UP000198392};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     28       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        29    248       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012668488.
FT   DOMAIN       54    136       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      143    243       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       129    129       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       210    210       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       214    214       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   248 AA;  27002 MW;  CE2248137E512A91 CRC64;
     MLNSLISRRR LIATGSLASV GVALSRFAFG QTVPSGAKPT LSVVPAYLGV SPQTLPALPY
     AENALEPTIS ARTVGIHYGK HHRAYFDNLH KLLVGTPLEQ ASLEQIIVQS HDQPMLADVF
     NNAAQAWNHN FYWNSLTPAA TTPSAKLQAA IERKFGSIEA LSKALVATSA SQFGSGWGWL
     VVDRGELAVV KTGNAETPFT AGLAPLLTVD VWEHAYYLDY QNRRPDYLVA TVSRHLNWAF
     ASANFERV
//
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