GenomeNet

Database: UniProt/TrEMBL
Entry: B1MEF4_MYCA9
LinkDB: B1MEF4_MYCA9
Original site: B1MEF4_MYCA9 
ID   B1MEF4_MYCA9            Unreviewed;       207 AA.
AC   B1MEF4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 83.
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   OrderedLocusNames=MAB_0118c {ECO:0000313|EMBL:CAM60218.1};
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS   104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS   abscessus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM60218.1, ECO:0000313|Proteomes:UP000007137};
RN   [1] {ECO:0000313|EMBL:CAM60218.1, ECO:0000313|Proteomes:UP000007137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC   TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
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}.
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; CU458896; CAM60218.1; -; Genomic_DNA.
DR   RefSeq; WP_005062831.1; NZ_MLCG01000005.1.
DR   AlphaFoldDB; B1MEF4; -.
DR   GeneID; 66970503; -.
DR   KEGG; mab:MAB_0118c; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000007137; Chromosome.
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
//
DBGET integrated database retrieval system