ID A0A075ULK6_9PSEU Unreviewed; 207 AA.
AC A0A075ULK6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=sodB {ECO:0000313|EMBL:AIG73459.1};
GN ORFNames=AJAP_02665 {ECO:0000313|EMBL:AIG73459.1};
OS Amycolatopsis japonica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX NCBI_TaxID=208439 {ECO:0000313|EMBL:AIG73459.1, ECO:0000313|Proteomes:UP000028492};
RN [1] {ECO:0000313|EMBL:AIG73459.1, ECO:0000313|Proteomes:UP000028492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG417-CF17 (DSM 44213) {ECO:0000313|Proteomes:UP000028492};
RX PubMed=25193710; DOI=10.1016/j.jbiotec.2014.08.034;
RA Stegmann E., Albersmeier A., Spohn M., Gert H., Weber T., Wohlleben W.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Amycolatopsis japonica
RT MG417-CF17(T) (=DSM 44213T) producing (S,S)-N,N'-ethylenediaminedisuccinic
RT acid.";
RL J. Biotechnol. 189:46-47(2014).
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}.
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DR EMBL; CP008953; AIG73459.1; -; Genomic_DNA.
DR RefSeq; WP_016337537.1; NZ_CP008953.1.
DR AlphaFoldDB; A0A075ULK6; -.
DR STRING; 208439.AJAP_02665; -.
DR KEGG; aja:AJAP_02665; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_2_2_11; -.
DR Proteomes; UP000028492; 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 4..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; 22889 MW; AD8CF400A200BBAD CRC64;
MARYVLPDLD YDYSALAPHI SGEINELHHS KHHATYVKGA NDTLDKIAEA REAGNFGDIV
GLQTTLAFHL AGHANHVVWW KILSPEGGDK PTGELASAID EAFGSFDKFK AQFTAVATTI
QGNGWAALSW DPIGKTLITQ QLRDHHNNLV LPTTPILLVD VWEHAFYLDY KNVKPDYVKA
LWNIFNWAEI SKRFDNAVAG GNGLLLG
//