GenomeNet

Database: UniProt
Entry: Q9FA87_VIBPR
LinkDB: Q9FA87_VIBPR
Original site: Q9FA87_VIBPR 
ID   Q9FA87_VIBPR            Unreviewed;       139 AA.
AC   Q9FA87;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
DE   Flags: Fragment;
GN   Name=sodB {ECO:0000313|EMBL:BAB17870.1};
OS   Vibrio proteolyticus (Aeromonas proteolytica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=671 {ECO:0000313|EMBL:BAB17870.1};
RN   [1] {ECO:0000313|EMBL:BAB17870.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IAM14410 {ECO:0000313|EMBL:BAB17870.1};
RA   Yamada Y.;
RT   "sodB gene for iron-containing superoxide disumutase, partial cds.";
RL   Submitted (NOV-2000) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB050798; BAB17870.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9FA87; -.
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; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 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|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN          2..62
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          69..139
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAB17870.1"
FT   NON_TER         139
FT                   /evidence="ECO:0000313|EMBL:BAB17870.1"
SQ   SEQUENCE   139 AA;  14927 MW;  146EF5376395A6B9 CRC64;
     AETLDYHHGK HHNTYVVKLN GLIPGTEFEG KTLEEIIKTS TGGVFNNAAQ IWNHTFYWHC
     LSPNGGGEPT GAVADAINAA FGSFEEFKAK FTDSAINNFG SSWTWLVKNA DGSLAITNTS
     NAGTPLTEEG VTPLLTVDL
//
DBGET integrated database retrieval system