ID R5M4F1_9BACE Unreviewed; 194 AA.
AC R5M4F1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 16-JAN-2019, entry version 20.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=BN711_02307 {ECO:0000313|EMBL:CCY86413.1};
OS Bacteroides intestinalis CAG:564.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides; environmental samples.
OX NCBI_TaxID=1263049 {ECO:0000313|EMBL:CCY86413.1};
RN [1] {ECO:0000313|EMBL:CCY86413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units
RT of genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CCY86413.1}.
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DR EMBL; CAYY010000216; CCY86413.1; -; Genomic_DNA.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 2 81 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 91 192 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 75 75 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 159 159 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 163 163 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 194 AA; 21814 MW; B5AABF2AB4DB8C0A CRC64;
MTYEMPKLPY ANNALEPVIS QQTIDYHYGK HLQTYVNNLN NLVPGTEYEN KDLVTIVATA
PDGAIFNNAG QVLNHTLYFL QFSPKPAHSE PTGKLAEAIK RDFGSFDNFK KEFTAAAVGL
FGSGWAWLSV DKNGKLHITK EANGSNPVRA GLIPLLGFDV WEHSYYLDYQ NRRADHVNAL
WSIIDWDVVG NRLK
//
