Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P19665

- SODF_PORGI

UniProt

P19665 - SODF_PORGI

Protein

Superoxide dismutase [Mn/Fe]

Gene

sodB

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 May 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.

    Cofactori

    Binds 1 manganese or iron ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi27 – 271Manganese or iron
    Metal bindingi74 – 741Manganese or iron
    Metal bindingi157 – 1571Manganese or iron
    Metal bindingi161 – 1611Manganese or iron

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. superoxide dismutase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciPGIN242619:GHX8-1394-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Mn/Fe] (EC:1.15.1.1)
    Gene namesi
    Name:sodB
    Ordered Locus Names:PG_1545
    OrganismiPorphyromonas gingivalis (strain ATCC BAA-308 / W83)
    Taxonomic identifieri242619 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
    ProteomesiUP000000588: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 191191Superoxide dismutase [Mn/Fe]PRO_0000159993Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi242619.PG1545.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni12 – 198
    Helixi21 – 277
    Turni28 – 303
    Helixi31 – 4212
    Turni43 – 453
    Turni47 – 504
    Helixi53 – 597
    Helixi62 – 7918
    Helixi91 – 10111
    Helixi104 – 11714
    Beta strandi120 – 1289
    Beta strandi134 – 1407
    Helixi145 – 1484
    Beta strandi151 – 1577
    Helixi160 – 1623
    Helixi164 – 1674
    Helixi171 – 1788
    Helixi179 – 1813
    Helixi184 – 1907

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QNNX-ray1.80A/B/C/D1-191[»]
    1UERX-ray1.60A/B/C/D1-191[»]
    1UESX-ray1.60A/B/C/D1-191[»]
    ProteinModelPortaliP19665.
    SMRiP19665. Positions 1-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19665.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0605.
    KOiK04564.
    OMAiHANRELQ.
    OrthoDBiEOG63NMNT.

    Family and domain databases

    InterProiIPR001189. Mn/Fe_SOD.
    IPR019833. Mn/Fe_SOD_BS.
    IPR019832. Mn/Fe_SOD_C.
    IPR019831. Mn/Fe_SOD_N.
    [Graphical view]
    PANTHERiPTHR11404. PTHR11404. 1 hit.
    PfamiPF02777. Sod_Fe_C. 1 hit.
    PF00081. Sod_Fe_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000349. SODismutase. 1 hit.
    PRINTSiPR01703. MNSODISMTASE.
    SUPFAMiSSF46609. SSF46609. 1 hit.
    SSF54719. SSF54719. 1 hit.
    PROSITEiPS00088. SOD_MN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19665-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHELISLPY AVDALAPVIS KETVEFHHGK HLKTYVDNLN KLIIGTEFEN    50
    ADLNTIVQKS EGGIFNNAGQ TLNHNLYFTQ FRPGKGGAPK GKLGEAIDKQ 100
    FGSFEKFKEE FNTAGTTLFG SGWVWLASDA NGKLSIEKEP NAGNPVRKGL 150
    NPLLGFDVWE HAYYLTYQNR RADHLKDLWS IVDWDIVESR Y 191
    Length:191
    Mass (Da):21,501
    Last modified:May 1, 1991 - v2
    Checksum:iAA53419397BF6BA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131D → Y in AAA25651. (PubMed:1840572)Curated
    Sequence conflicti29 – 291G → E AA sequence (PubMed:2226833)Curated
    Sequence conflicti112 – 1121N → D in AAA25651. (PubMed:1840572)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90152 Genomic DNA. Translation: BAA14182.1.
    M60401 Genomic DNA. Translation: AAA25651.1.
    AE015924 Genomic DNA. Translation: AAQ66583.1.
    PIRiA43585.
    RefSeqiNP_905684.1. NC_002950.2.

    Genome annotation databases

    EnsemblBacteriaiAAQ66583; AAQ66583; PG_1545.
    GeneIDi2553021.
    KEGGipgi:PG1545.
    PATRICi22974068. VBIPorGin26334_0556.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90152 Genomic DNA. Translation: BAA14182.1 .
    M60401 Genomic DNA. Translation: AAA25651.1 .
    AE015924 Genomic DNA. Translation: AAQ66583.1 .
    PIRi A43585.
    RefSeqi NP_905684.1. NC_002950.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QNN X-ray 1.80 A/B/C/D 1-191 [» ]
    1UER X-ray 1.60 A/B/C/D 1-191 [» ]
    1UES X-ray 1.60 A/B/C/D 1-191 [» ]
    ProteinModelPortali P19665.
    SMRi P19665. Positions 1-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 242619.PG1545.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ66583 ; AAQ66583 ; PG_1545 .
    GeneIDi 2553021.
    KEGGi pgi:PG1545.
    PATRICi 22974068. VBIPorGin26334_0556.

    Phylogenomic databases

    eggNOGi COG0605.
    KOi K04564.
    OMAi HANRELQ.
    OrthoDBi EOG63NMNT.

    Enzyme and pathway databases

    BioCyci PGIN242619:GHX8-1394-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P19665.

    Family and domain databases

    InterProi IPR001189. Mn/Fe_SOD.
    IPR019833. Mn/Fe_SOD_BS.
    IPR019832. Mn/Fe_SOD_C.
    IPR019831. Mn/Fe_SOD_N.
    [Graphical view ]
    PANTHERi PTHR11404. PTHR11404. 1 hit.
    Pfami PF02777. Sod_Fe_C. 1 hit.
    PF00081. Sod_Fe_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000349. SODismutase. 1 hit.
    PRINTSi PR01703. MNSODISMTASE.
    SUPFAMi SSF46609. SSF46609. 1 hit.
    SSF54719. SSF54719. 1 hit.
    PROSITEi PS00088. SOD_MN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The superoxide dismutase-encoding gene of the obligately anaerobic bacterium Bacteroides gingivalis."
      Nakayama K.
      Gene 96:149-150(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation, expression, and nucleotide sequence of the sod gene from Porphyromonas gingivalis."
      Choi J.I., Takahashi N., Kato T., Kuramitsu H.K.
      Infect. Immun. 59:1564-1566(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The primary structure of superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis."
      Amano A., Shizukuishi S., Tsunemitsu A., Maekawa K., Tsunasawa S.
      FEBS Lett. 272:217-220(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: 381.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-308 / W83.
    5. "Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis."
      Amano A., Shizukuishi S., Tamagawa H., Iwakura K., Tsunasawa S., Tsunemitsu A.
      J. Bacteriol. 172:1457-1463(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
    6. "Crystal structure of cambialistic superoxide dismutase from Porphyromonas gingivalis."
      Sugio S., Hiraoka B.Y., Yamakura F.
      Eur. J. Biochem. 267:3487-3495(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiSODF_PORGI
    AccessioniPrimary (citable) accession number: P19665
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3