ID Q59133_ACTPL Unreviewed; 213 AA.
AC Q59133;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 98.
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};
GN Name=sodA {ECO:0000313|EMBL:AAB03279.1};
GN ORFNames=NCTC10976_00260 {ECO:0000313|EMBL:VEJ16183.1}, OYG11_01330
GN {ECO:0000313|EMBL:MCY6522896.1};
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715 {ECO:0000313|EMBL:AAB03279.1};
RN [1] {ECO:0000313|EMBL:AAB03279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4074 {ECO:0000313|EMBL:AAB03279.1};
RA Helie M.-C., Sirois M., Ouellet C., Boissinot M.;
RT "Cloning, sequencing and overproduction of Mn-SOD and Cu,Zn-SOD.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEJ16183.1, ECO:0000313|Proteomes:UP000275510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10976 {ECO:0000313|EMBL:VEJ16183.1,
RC ECO:0000313|Proteomes:UP000275510};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MCY6522896.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=84/14 {ECO:0000313|EMBL:MCY6522896.1};
RX PubMed=35051085;
RA Byun J.W., Moon B.Y., Do K.H., Lee K., Lee H.Y., Kim W.I., So B., Lee W.K.;
RT "O-Serogroups and Pathovirotypes of Escherichia coli Isolated from Post-
RT Weaning Piglets Showing Diarrhoea and/or Oedema in South Korea.";
RL Vet Sci 5 (2) 9:0-0(2021).
RN [4] {ECO:0000313|EMBL:MCY6522896.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=84/14 {ECO:0000313|EMBL:MCY6522896.1};
RA Kardos G., Sarkozi R., Laczko L., Marton S., Makrai L., Banyai K.,
RA Fodor L.;
RL Submitted (DEC-2022) 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; U51441; AAB03279.1; -; Genomic_DNA.
DR EMBL; JAPQFC010000001; MCY6522896.1; -; Genomic_DNA.
DR EMBL; LR134515; VEJ16183.1; -; Genomic_DNA.
DR RefSeq; WP_005596109.1; NZ_LS483358.1.
DR GeneID; 69417417; -.
DR OMA; YEGWKGE; -.
DR Proteomes; UP000275510; Chromosome 1.
DR Proteomes; UP001077788; 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; 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; 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 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.
DR PROSITE; PS00088; SOD_MN; 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 3..89
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 96..201
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 213 AA; 23757 MW; 55186DEBB91F1C5B CRC64;
MAYQLPELGY AYDALEPHFD KATMEIHHTK HHQTYVNNAN AALEAHPELL EKCPGALIKD
LSQVPAEKRT AVRNNVGGHV NHTLFWKGLK TGTTLQGALK DAIVRDFGSV EAFQAEFEKA
AATRFGSGWA WLVVEGGKLA VVSTANQDNP IMGKEVAGVS GFPILALDVW EHAYYLHYQN
RRPDYIKAFW NVVNWDEAAR RFEEHASHCG CAK
//