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Database: UniProt
Entry: Q6QF33_MYCAV
LinkDB: Q6QF33_MYCAV
Original site: Q6QF33_MYCAV 
ID   Q6QF33_MYCAV            Unreviewed;       137 AA.
AC   Q6QF33;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   28-JUN-2023, entry version 58.
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};
DE   Flags: Fragment;
GN   Name=sod {ECO:0000313|EMBL:AAS59446.1};
OS   Mycobacterium avium subsp. avium.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=44454 {ECO:0000313|EMBL:AAS59446.1};
RN   [1] {ECO:0000313|EMBL:AAS59446.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIP 104244 {ECO:0000313|EMBL:AAS59446.1};
RX   PubMed=15653890; DOI=10.1099/ijs.0.63222-0;
RA   Devulder G., Perouse de Montclos M., Flandrois J.P.;
RT   "A multigene approach to phylogenetic analysis using the genus
RT   Mycobacterium as a model.";
RL   Int. J. Syst. Evol. Microbiol. 55:293-302(2005).
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; AY544802; AAS59446.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6QF33; -.
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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 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          1..58
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          65..137
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAS59446.1"
FT   NON_TER         137
FT                   /evidence="ECO:0000313|EMBL:AAS59446.1"
SQ   SEQUENCE   137 AA;  14992 MW;  2277D00463981279 CRC64;
     LHHSKHHATY VKGVNDALAK LEEARANEDH AAIFLNEKNL AFHLGGHVNH SIWWKNLSPD
     GGDKPTGELA AAIDDAFGSF DKFRAQFSAA ANGLQGSGWA VLGYDTLGSR LLTFQLYDQQ
     ANVPLGIIPL LQVDMWE
//
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