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Database: UniProt
Entry: A0A060QAQ6_9PROT
LinkDB: A0A060QAQ6_9PROT
Original site: A0A060QAQ6_9PROT 
ID   A0A060QAQ6_9PROT        Unreviewed;       202 AA.
AC   A0A060QAQ6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SACS_1444 {ECO:0000313|EMBL:CDG34182.1};
OS   Saccharibacter sp. AM169.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Saccharibacter.
OX   NCBI_TaxID=1343158 {ECO:0000313|EMBL:CDG34182.1, ECO:0000313|Proteomes:UP000027590};
RN   [1] {ECO:0000313|EMBL:CDG34182.1, ECO:0000313|Proteomes:UP000027590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM169 {ECO:0000313|Proteomes:UP000027590};
RX   PubMed=24682158; DOI=10.1093/gbe/evu062;
RA   Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA   Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT   "Acetic acid bacteria genomes reveal functional traits for adaptation
RT   to life in insect guts.";
RL   Genome Biol. Evol. 6:912-920(2014).
RN   [2] {ECO:0000313|EMBL:CDG34182.1, ECO:0000313|Proteomes:UP000027590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM169 {ECO:0000313|Proteomes:UP000027590};
RX   PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA   Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA   Lievens P.M., Daffonchio D., Bandi C.;
RT   "Evolution of mitochondria reconstructed from the energy metabolism of
RT   living bacteria.";
RL   PLoS ONE 9:e96566-e96566(2014).
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDG34182.1}.
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DR   EMBL; CBLY010000006; CDG34182.1; -; Genomic_DNA.
DR   RefSeq; WP_043560695.1; NZ_CBLY010000006.1.
DR   EnsemblBacteria; CDG34182; CDG34182; SACS_1444.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000027590; Unassembled WGS 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:UP000027590};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CDG34182.1}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       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;  22275 MW;  70EF557879A43491 CRC64;
     MAFELPKLPY AENALADAGM CQETLELHHG KHHQAYVTAL NGFVESKPEL AGKALEEIIA
     LSHADSSLAP VFNNAGQHWN HCIFWNCLSP NGGRIPGALE KKLTEDFGSV DAFKAAFKQA
     ATTQFGSGWA WLVLGSDGKL KVTKTANAAN PLSEDEGRTL LGLDVWEHSY YLDFRNRRPD
     YVTNFLDRLA NYEYAESCLK GA
//
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