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Database: UniProt
Entry: I3I513_9GAMM
LinkDB: I3I513_9GAMM
Original site: I3I513_9GAMM 
ID   I3I513_9GAMM            Unreviewed;       249 AA.
AC   I3I513;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   ORFNames=O59_003941 {ECO:0000313|EMBL:EIK43148.1};
OS   Cellvibrio sp. BR.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK43148.1, ECO:0000313|Proteomes:UP000003395};
RN   [1] {ECO:0000313|EMBL:EIK43148.1, ECO:0000313|Proteomes:UP000003395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR {ECO:0000313|EMBL:EIK43148.1,
RC   ECO:0000313|Proteomes:UP000003395};
RA   Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIK43148.1}.
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DR   EMBL; AICM01000010; EIK43148.1; -; Genomic_DNA.
DR   RefSeq; WP_007645336.1; NZ_JH668206.1.
DR   AlphaFoldDB; I3I513; -.
DR   STRING; 1134474.O59_003941; -.
DR   PATRIC; fig|1134474.3.peg.3755; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_2_2_6; -.
DR   OrthoDB; 9811849at2; -.
DR   Proteomes; UP000003395; 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; 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; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
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; PS51318; TAT; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..249
FT                   /note="superoxide dismutase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003671352"
FT   DOMAIN          138..239
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         74
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         124
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         206
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         210
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   249 AA;  27407 MW;  28777BCD08CB24A8 CRC64;
     MNDFNQNKRD FLATSATAAA GLLIASASNV SAAESSSQAA PKGANWMITE IKPKPLSFNA
     AKLKGLSANL IESHWTNNYS GSVKTLNAVN DQLSQALANP DTPAFLYNDL KREHLIRTGS
     VILHELYFDN LGGNGKADGE LRSAFAKQFG TFDRWETEFR KIAQGLGGGS GWVVLGYNTH
     FNKLENYWMG DHAHFPVGTV PLLVMDMYEH SYHMDFGAAA GKYIDAFFNN INWDEVAHRL
     QATHTKTTS
//
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