ID A0A0H5BAM4_BLAVI Unreviewed; 238 AA.
AC A0A0H5BAM4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:CUU41260.1};
GN ORFNames=BV133_521 {ECO:0000313|EMBL:BAR98114.1}, BVIRIDIS_02490
GN {ECO:0000313|EMBL:CUU41260.1};
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079 {ECO:0000313|EMBL:CUU41260.1, ECO:0000313|Proteomes:UP000065734};
RN [1] {ECO:0000313|EMBL:BAR98114.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 133 {ECO:0000313|EMBL:BAR98114.1};
RA Tsukatani Y., Hirose Y., Harada J., Misawa N., Mori K., Inoue K.,
RA Tamiaki H.;
RT "Complete Genome Sequence of the Bacteriochlorophyll b-Producing
RT Photosynthetic Bacterium Blastochloris viridis.";
RL Genome Announc. 3:e01006-15(2015).
RN [2] {ECO:0000313|EMBL:CUU41260.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:CUU41260.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000065734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000313|Proteomes:UP000065734};
RX PubMed=26798090; DOI=10.1128/genomeA.01520-15;
RA Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.;
RT "Revised genome sequence of the purple photosynthetic bacterium
RT Blastochloris viridis.";
RL Genome Announc. 4:0-0(2016).
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; AP014854; BAR98114.1; -; Genomic_DNA.
DR EMBL; LN907867; CUU41260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5BAM4; -.
DR STRING; 1079.BVIR_804; -.
DR KEGG; bvr:BVIR_804; -.
DR PATRIC; fig|1079.6.peg.834; -.
DR Proteomes; UP000065734; Chromosome I.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000065734};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..238
FT /note="Superoxide dismutase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014229089"
FT DOMAIN 36..122
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 131..231
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 238 AA; 26119 MW; C0F8D82D91617ED9 CRC64;
MNRRDTLQTL ATVMAVGLAG RSGFAFAQST APSGPFTLPP LGYDYAALEP HIDAQTMMIH
HQRHHAGYVA KANALAADVP LLRTRSVEQI LADLAAVPEA SRTAVRNNVG GHWNHSFFWI
LMQPGGAREP VGALKAAIDR DFGGLQQLKE RINAAGEGRF GSGWAWLVVG KDKKLAVLSS
PNQDSPLMDG TPGVVLGVDV WEHAYYLKYQ NRRPEYLTAW WNTVNWDNAE SNYRKAVA
//
