ID C7LRC1_DESBD Unreviewed; 207 AA.
AC C7LRC1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=Dbac_1163 {ECO:0000313|EMBL:ACU89267.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU89267.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU89267.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(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 -!- 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}.
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; CP001629; ACU89267.1; -; Genomic_DNA.
DR RefSeq; WP_015773364.1; NC_013173.1.
DR AlphaFoldDB; C7LRC1; -.
DR STRING; 525897.Dbac_1163; -.
DR KEGG; dba:Dbac_1163; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_0_7; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000002216; 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; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002216}.
FT DOMAIN 14..95
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 106..203
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 207 AA; 23104 MW; A21D0E357F4DFBAB CRC64;
MSNGILKSES LQVLPFLPYA ENALEPVISA KTIGFHYDKH HKGYVDNLKK LVAGTRFADM
TLEKIMSETA GKSDNIAIFN NAAQTWNHNF YWQSLRPSGG AELAAVLQKK IEVSFGSLDA
CKKELAAAAM AQFGSGWAWL VMDSDMLKVV KTANAEVPMT MSMKPLLTID VWEHAYYLDY
QNRRADYVKA VLDTLINWEF AAENLGC
//
