ID F2NCX7_DESAR Unreviewed; 216 AA. AC F2NCX7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 60. DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682}; GN OrderedLocusNames=Desac_1710 {ECO:0000313|EMBL:AEB09551.1}; OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2). OC Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales; OC Desulfobaccaceae; Desulfobacca. OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB09551.1, ECO:0000313|Proteomes:UP000000483}; RN [1] {ECO:0000313|EMBL:AEB09551.1, ECO:0000313|Proteomes:UP000000483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2 RC {ECO:0000313|Proteomes:UP000000483}; RX PubMed=21886866; RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K., RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of the acetate-degrading sulfate reducer RT Desulfobacca acetoxidans type strain (ASRB2)."; RL Stand. Genomic Sci. 4:393-401(2011). RN [2] {ECO:0000313|Proteomes:UP000000483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2 RC {ECO:0000313|Proteomes:UP000000483}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfobacca acetoxidans DSM 11109."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714}. 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; CP002629; AEB09551.1; -; Genomic_DNA. DR RefSeq; WP_013706661.1; NC_015388.1. DR AlphaFoldDB; F2NCX7; -. DR STRING; 880072.Desac_1710; -. DR KEGG; dao:Desac_1710; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_2_2_7; -. DR Proteomes; UP000000483; 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; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019832; Mn/Fe_SOD_C. 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 PIRSF; PIRSF000349; SODismutase; 1. DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1. DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000000483}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..216 FT /note="superoxide dismutase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003282525" FT DOMAIN 113..213 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 52 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 97 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 180 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 184 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 216 AA; 24163 MW; C369640E1C384150 CRC64; MPITMKSVLA FLTILTLFVV TTAAAAPVTY QAKDFSRLRG MKGFSDQALE LHFVLYQGYV KNTNAMLETL AQIASSTPAY AEMKRRLGWE YNGMRLHELY FGNLGGDGKI PPDSKIAKRL TEQFGSLESW ANDFKATGAM RGIGWVVLYE DQASGRLINT WINEHDLGHL AGGQPLLVMD VFEHAFIPDY GLKKGDYIEA FFQNIDWKAV DARLGK //