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Database: UniProt/TrEMBL
Entry: A0A1B0ZJ16_9MICO
LinkDB: A0A1B0ZJ16_9MICO
Original site: A0A1B0ZJ16_9MICO 
ID   A0A1B0ZJ16_9MICO        Unreviewed;       209 AA.
AC   A0A1B0ZJ16;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=DAD186_13870 {ECO:0000313|EMBL:ANP27937.1};
OS   Dermabacter vaginalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Dermabacter.
OX   NCBI_TaxID=1630135 {ECO:0000313|EMBL:ANP27937.1, ECO:0000313|Proteomes:UP000092596};
RN   [1] {ECO:0000313|EMBL:ANP27937.1, ECO:0000313|Proteomes:UP000092596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD1-86 {ECO:0000313|EMBL:ANP27937.1,
RC   ECO:0000313|Proteomes:UP000092596};
RA   Kim B.-C., Lim S.;
RT   "Investigation of pathophysiology for high-risk pregnancy and development
RT   of treatment modality based on it.";
RL   Submitted (JUN-2015) 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}.
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DR   EMBL; CP012117; ANP27937.1; -; Genomic_DNA.
DR   RefSeq; WP_065248043.1; NZ_CP012117.1.
DR   AlphaFoldDB; A0A1B0ZJ16; -.
DR   STRING; 1630135.DAD186_13870; -.
DR   KEGG; dva:DAD186_13870; -.
DR   PATRIC; fig|1630135.4.peg.1386; -.
DR   Proteomes; UP000092596; 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   209 AA;  23317 MW;  1CEBFD451F0282C0 CRC64;
     MAEYTLPDLG YDYAALEPSI SGRIMELHHD KHHQTYVNGA NQALEQLAEA RDKNDFGTIN
     QLQKNLAFNL AGHVNHTIFW ENLSPEGGDK PEGELAQAVE EFFGSFDGLR AQFTAAALGI
     QGSGWAILAW DSLGEKLIIE QFYDHQGNLA AATVPLLLLD MWEHAFYLDY QNAKADYVKA
     FWNIVDWADV AERFSRATSQ TKGLITPVA
//
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