ID A0A068YYY4_9GAMM Unreviewed; 206 AA.
AC A0A068YYY4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:MXR54736.1};
GN ORFNames=GPZ83_002405 {ECO:0000313|EMBL:NYV28955.1}, GPZ83_08810
GN {ECO:0000313|EMBL:MXR54736.1}, SYMBAF_00550
GN {ECO:0000313|EMBL:QLH61729.1};
OS Serratia symbiotica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=138074 {ECO:0000313|EMBL:MXR54736.1};
RN [1] {ECO:0000313|EMBL:QLH61729.1, ECO:0000313|Proteomes:UP000042738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWBI-2.3 {ECO:0000313|EMBL:QLH61729.1};
RX PubMed=25146134;
RA Foray V., Grigorescu A.S., Sabri A., Haubruge E., Lognay G., Francis F.,
RA Fauconnier M.L., Hance T., Thonart P.;
RT "Whole-Genome Sequence of Serratia symbiotica Strain CWBI-2.3T, a Free-
RT Living Symbiont of the Black Bean Aphid Aphis fabae.";
RL Genome Announc. 2:e00767-e00714(2014).
RN [2] {ECO:0000313|EMBL:QLH61729.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CWBI-2.3 {ECO:0000313|EMBL:QLH61729.1};
RA Foray V.V.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MXR54736.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24.1 {ECO:0000313|EMBL:MXR54736.1};
RA Renoz F., Ambroise J., Gala J.-L., Hance T.;
RT "Draft genome sequence of Serratia symbiotica strain 24.1.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:NYV28955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=24.1 {ECO:0000313|EMBL:NYV28955.1}, and CWBI-2.3
RC {ECO:0000313|EMBL:QLH61729.1};
RA Renoz F., Foray V., Ambroise J., Baa-Puyoulet P., Bearzatto B.,
RA Mendez G.L., Vanderpoorten A., Mahillon J., Gala J.-L., Calevro F.,
RA Hance T.;
RT "Genomic Insight into Nascent Stage of Mutualistic Insect Bacterial
RT Symbioses through the Bacterial Symbiont Serratia symbiotica.";
RL Submitted (APR-2020) 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 -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00002170}.
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|ARBA:ARBA00001605,
CC 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; WSPN01000020; MXR54736.1; -; Genomic_DNA.
DR EMBL; WSPN02000001; NYV28955.1; -; Genomic_DNA.
DR EMBL; CP050855; QLH61729.1; -; Genomic_DNA.
DR STRING; 138074.SYMBAF_160297; -.
DR Proteomes; UP000042738; 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; 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 2..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 206 AA; 23435 MW; 73C2EE164B242CE8 CRC64;
MSYSLPSLPY AYDALEPHFD KQTMEIHHSK HHQAYVNNAN TVLEAYPELA KYSVEELIEH
LDKVPTDKRT FMRNNAGGHA NHSFFWKNLK TGTTLSGDLK AAIERDFGSV EQFKEEFEKT
AATRFGSGWA WLVLQGDKLV VVSTANQDSP LMGEAATGTS GFPIIVLDVW EHAYYLKYQN
KRPDYIKAFW NVVNWDEAAA RFAAKK
//
