ID A0A0U1AVW0_9MYCO Unreviewed; 207 AA.
AC A0A0U1AVW0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 53.
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_2 {ECO:0000313|EMBL:CPV68018.1};
GN ORFNames=D2E76_06845 {ECO:0000313|EMBL:RIT41076.1}, ERS075579_04335
GN {ECO:0000313|EMBL:CPV68018.1}, ERS075604_04516
GN {ECO:0000313|EMBL:CPX20951.1};
OS Mycobacteroides abscessus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides.
OX NCBI_TaxID=36809 {ECO:0000313|EMBL:CPV68018.1, ECO:0000313|Proteomes:UP000045782};
RN [1] {ECO:0000313|EMBL:CPX20951.1, ECO:0000313|Proteomes:UP000042347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAP113 {ECO:0000313|EMBL:CPX20951.1,
RC ECO:0000313|Proteomes:UP000042347};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CPV68018.1, ECO:0000313|Proteomes:UP000045782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAP088 {ECO:0000313|EMBL:CPV68018.1,
RC ECO:0000313|Proteomes:UP000045782};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RIT41076.1, ECO:0000313|Proteomes:UP000284557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G143 {ECO:0000313|EMBL:RIT41076.1,
RC ECO:0000313|Proteomes:UP000284557};
RA Ye M., Xu L., Zou Y., Li B., Guo Q., Zhang Y., Zhan M., Xu B., Yu F.,
RA Zhang Z., Chu H.;
RT "Linezolid Resistance in Mycobacterium abscessus: MIC Distribution and
RT Comprehensive Investigation of Resistance Mechanisms.";
RL Submitted (AUG-2018) 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; CSWP01000010; CPV68018.1; -; Genomic_DNA.
DR EMBL; CSXT01000012; CPX20951.1; -; Genomic_DNA.
DR EMBL; QXBN01000004; RIT41076.1; -; Genomic_DNA.
DR RefSeq; WP_005062831.1; NZ_UGQJ01000002.1.
DR RefSeq; YP_001700872.1; NC_010397.1.
DR GeneID; 66970503; -.
DR PATRIC; fig|36809.44.peg.76; -.
DR OMA; DSLINWD; -.
DR Proteomes; UP000042347; Unassembled WGS sequence.
DR Proteomes; UP000045782; Unassembled WGS sequence.
DR Proteomes; UP000284557; 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; 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; 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 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 3..84
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 91..193
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 28
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 207 AA; 23026 MW; 5FC80FFE430CADEB CRC64;
MAEYTLPDLD YDYGALEPHI SGQINELHHS KHHATYVKGV NDAVAKLEEA REKGDHAAIF
LNEKNLAFHL GGHVNHSIWW KNLSPNGGDK PTGDLAAAID DQFGSFDKFQ AQFTAAANGL
QGSGWAVLGY DSLGQKLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
FWNVVNWADV QDRYTAATTK TSGLIFG
//
