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Database: UniProt
Entry: A0A0X8FKJ2_9LACT
LinkDB: A0A0X8FKJ2_9LACT
Original site: A0A0X8FKJ2_9LACT 
ID   A0A0X8FKJ2_9LACT        Unreviewed;       202 AA.
AC   A0A0X8FKJ2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AWM75_02445 {ECO:0000313|EMBL:AMB98922.1};
OS   Aerococcus urinaehominis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae;
OC   Aerococcus.
OX   NCBI_TaxID=128944 {ECO:0000313|EMBL:AMB98922.1, ECO:0000313|Proteomes:UP000062260};
RN   [1] {ECO:0000313|EMBL:AMB98922.1, ECO:0000313|Proteomes:UP000062260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG42038B {ECO:0000313|EMBL:AMB98922.1,
RC   ECO:0000313|Proteomes:UP000062260};
RX   PubMed=27103727;
RA   Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA   Christensen J.J.;
RT   "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT   Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT   Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038
RT   BT, and Aerococcus viridans CCUG 4311T.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000062260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG42038B {ECO:0000313|Proteomes:UP000062260};
RA   Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA   Christensen J.J.;
RT   "Six Aerococcus type strain genome sequencing and assembly using
RT   PacBio and Illumina Hiseq.";
RL   Submitted (JAN-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; CP014163; AMB98922.1; -; Genomic_DNA.
DR   RefSeq; WP_067977811.1; NZ_FNHJ01000015.1.
DR   EnsemblBacteria; AMB98922; AMB98922; AWM75_02445.
DR   KEGG; auh:AWM75_02445; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000062260; 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:UP000062260};
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:UP000062260}.
FT   DOMAIN        2     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    197       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;  22774 MW;  61999B17ED141D1A CRC64;
     MSFTLPDLPY AYDALEPYID EETMKLHHDK HHNTYVTNAN KAIEGTDLDN KSAEEILRNF
     DQVPADIQTA VRNNVGGHAN HAFFWELLAP NAGGQPEGEI KAAIEAKFGS FADFQEAFNG
     AATGRFGSGW AWLVVNAEGE LEITSTPNQD SPYMNDQTPI IGLDVWEHAY YLKYQNVRAD
     YVKAFWNLVN WEQVNKNYQA AK
//
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