ID SODF_PORGI Reviewed; 191 AA. AC P19665; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 2. DT 27-MAR-2024, entry version 155. DE RecName: Full=Superoxide dismutase [Mn/Fe]; DE EC=1.15.1.1 {ECO:0000305|PubMed:2307656}; GN Name=sodB; Synonyms=sod {ECO:0000303|PubMed:1840572}; GN OrderedLocusNames=PG_1545; OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; OC Porphyromonas. OX NCBI_TaxID=242619; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2265754; DOI=10.1016/0378-1119(90)90357-w; RA Nakayama K.; RT "The superoxide dismutase-encoding gene of the obligately anaerobic RT bacterium Bacteroides gingivalis."; RL Gene 96:149-150(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 53977; RX PubMed=1840572; DOI=10.1128/iai.59.4.1564-1566.1991; RA Choi J.I., Takahashi N., Kato T., Kuramitsu H.K.; RT "Isolation, expression, and nucleotide sequence of the sod gene from RT Porphyromonas gingivalis."; RL Infect. Immun. 59:1564-1566(1991). RN [3] RP PROTEIN SEQUENCE. RC STRAIN=381; RX PubMed=2226833; DOI=10.1016/0014-5793(90)80488-5; RA Amano A., Shizukuishi S., Tsunemitsu A., Maekawa K., Tsunasawa S.; RT "The primary structure of superoxide dismutase purified from anaerobically RT maintained Bacteroides gingivalis."; RL FEBS Lett. 272:217-220(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-308 / W83; RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003; RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., RA Fraser C.M.; RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas RT gingivalis strain W83."; RL J. Bacteriol. 185:5591-5601(2003). RN [5] RP PROTEIN SEQUENCE OF 1-12, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY RP REGULATION, AND SUBUNIT. RC STRAIN=381; RX PubMed=2307656; DOI=10.1128/jb.172.3.1457-1463.1990; RA Amano A., Shizukuishi S., Tamagawa H., Iwakura K., Tsunasawa S., RA Tsunemitsu A.; RT "Characterization of superoxide dismutases purified from either RT anaerobically maintained or aerated Bacteroides gingivalis."; RL J. Bacteriol. 172:1457-1463(1990). RN [6] {ECO:0007744|PDB:1QNN} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR. RX PubMed=10848964; DOI=10.1046/j.1432-1327.2000.01373.x; RA Sugio S., Hiraoka B.Y., Yamakura F.; RT "Crystal structure of cambialistic superoxide dismutase from Porphyromonas RT gingivalis."; RL Eur. J. Biochem. 267:3487-3495(2000). RN [7] {ECO:0007744|PDB:1UER, ECO:0007744|PDB:1UES} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT THR-155 IN RP COMPLEX WITH IRON OR MANGANESE, COFACTOR, AND MUTAGENESIS OF GLY-155. RX PubMed=12962504; DOI=10.1021/bi0349625; RA Yamakura F., Sugio S., Hiraoka B.Y., Ohmori D., Yokota T.; RT "Pronounced conversion of the metal-specific activity of superoxide RT dismutase from Porphyromonas gingivalis by the mutation of a single amino RT acid (Gly155Thr) located apart from the active site."; RL Biochemistry 42:10790-10799(2003). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological systems. CC Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 CC by successive reduction and oxidation of the transition metal ion at CC the active site. 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:0000305|PubMed:2307656}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697; CC Evidence={ECO:0000305|PubMed:2307656}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10848964, ECO:0000269|PubMed:2307656}; CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000269|PubMed:10848964, ECO:0000269|PubMed:12962504, CC ECO:0000269|PubMed:2307656}; CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit. CC {ECO:0000269|PubMed:10848964, ECO:0000269|PubMed:12962504}; CC -!- ACTIVITY REGULATION: Inhibited by hydrogen peroxide. CC {ECO:0000269|PubMed:2307656}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2307656}. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000305}. 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; D90152; BAA14182.1; -; Genomic_DNA. DR EMBL; M60401; AAA25651.1; -; Genomic_DNA. DR EMBL; AE015924; AAQ66583.1; -; Genomic_DNA. DR PIR; A43585; A43585. DR RefSeq; WP_004585361.1; NC_002950.2. DR PDB; 1QNN; X-ray; 1.80 A; A/B/C/D=1-191. DR PDB; 1UER; X-ray; 1.60 A; A/B/C/D=1-191. DR PDB; 1UES; X-ray; 1.60 A; A/B/C/D=1-191. DR PDBsum; 1QNN; -. DR PDBsum; 1UER; -. DR PDBsum; 1UES; -. DR AlphaFoldDB; P19665; -. DR SMR; P19665; -. DR STRING; 242619.PG_1545; -. DR EnsemblBacteria; AAQ66583; AAQ66583; PG_1545. DR GeneID; 29255789; -. DR KEGG; pgi:PG_1545; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_0_10; -. DR EvolutionaryTrace; P19665; -. DR Proteomes; UP000000588; 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 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Iron; Manganese; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..191 FT /note="Superoxide dismutase [Mn/Fe]" FT /id="PRO_0000159993" FT BINDING 27 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER" FT BINDING 27 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1UES" FT BINDING 74 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER" FT BINDING 74 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1UES" FT BINDING 157 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER" FT BINDING 157 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1UES" FT BINDING 161 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER" FT BINDING 161 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12962504, FT ECO:0007744|PDB:1UES" FT MUTAGEN 155 FT /note="G->T: Converts the metal-specific activity of the FT enzyme from a cambialistic type (showing the same activity FT with Fe and Mn) to an Fe-specific type." FT /evidence="ECO:0000269|PubMed:12962504" FT CONFLICT 13 FT /note="D -> Y (in Ref. 2; AAA25651)" FT /evidence="ECO:0000305" FT CONFLICT 29 FT /note="G -> E (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="N -> D (in Ref. 2; AAA25651)" FT /evidence="ECO:0000305" FT TURN 12..19 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 21..27 FT /evidence="ECO:0007829|PDB:1UER" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 31..42 FT /evidence="ECO:0007829|PDB:1UER" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:1UER" FT TURN 47..50 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 53..59 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 62..79 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 91..101 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 104..117 FT /evidence="ECO:0007829|PDB:1UER" FT STRAND 120..128 FT /evidence="ECO:0007829|PDB:1UER" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:1UER" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 171..178 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:1UER" FT HELIX 184..190 FT /evidence="ECO:0007829|PDB:1UER" SQ SEQUENCE 191 AA; 21501 MW; AA53419397BF6BA1 CRC64; MTHELISLPY AVDALAPVIS KETVEFHHGK HLKTYVDNLN KLIIGTEFEN ADLNTIVQKS EGGIFNNAGQ TLNHNLYFTQ FRPGKGGAPK GKLGEAIDKQ FGSFEKFKEE FNTAGTTLFG SGWVWLASDA NGKLSIEKEP NAGNPVRKGL NPLLGFDVWE HAYYLTYQNR RADHLKDLWS IVDWDIVESR Y //