ID A2RPL4_9ENTE Unreviewed; 155 AA.
AC A2RPL4;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE Flags: Fragment;
GN Name=sodA {ECO:0000313|EMBL:CAM32437.1};
OS Vagococcus salmoninarum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=2739 {ECO:0000313|EMBL:CAM32437.1};
RN [1] {ECO:0000313|EMBL:CAM32437.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JIP 27-01 {ECO:0000313|EMBL:CAM32437.1};
RX PubMed=17337536; DOI=10.1128/AEM.01852-06;
RA Michel C., Pelletier C., Boussaha M., Douet D.G., Lautraite A.,
RA Tailliez P.;
RT "Diversity of lactic acid bacteria associated with fish and the fish farm
RT environment, established by amplified rRNA gene restriction analysis.";
RL Appl. Environ. Microbiol. 73:2947-2955(2007).
RN [2] {ECO:0000313|EMBL:CAM32437.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JIP 27-01 {ECO:0000313|EMBL:CAM32437.1};
RA Michel C.M.;
RL Submitted (JAN-2007) 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 family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR EMBL; AM490326; CAM32437.1; -; Genomic_DNA.
DR AlphaFoldDB; A2RPL4; -.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
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 PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 8..78
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 85..155
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAM32437.1"
FT NON_TER 155
FT /evidence="ECO:0000313|EMBL:CAM32437.1"
SQ SEQUENCE 155 AA; 16805 MW; 545C3961BF6726C3 CRC64;
ALEATYLIVE TMHLHHDKHH NTYVTNLNAA IEKYPELGEK SIEELVADLA NVPADIRGAV
QNNGGGHVNH TFFWEIMAPN AGGEPTGAVK EEIEATFGSF ADFKEKFAAA GTGRFGSGWA
WLVVTDGKLE IMSTPNQDSP LTDGKTPILG LDVWD
//