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Protein

Superoxide dismutase [Mn/Fe]

Gene

sodB

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Mn2+, Fe2+Note: Binds 1 Mn2+ or Fe2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27Manganese or iron1
Metal bindingi74Manganese or iron1
Metal bindingi157Manganese or iron1
Metal bindingi161Manganese or iron1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Manganese, Metal-binding

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
Proteomesi
  • UP000000588 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001599931 – 191Superoxide dismutase [Mn/Fe]Add BLAST191

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi242619.PG1545.

Structurei

Secondary structure

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni12 – 19Combined sources8
Helixi21 – 27Combined sources7
Turni28 – 30Combined sources3
Helixi31 – 42Combined sources12
Turni43 – 45Combined sources3
Turni47 – 50Combined sources4
Helixi53 – 59Combined sources7
Helixi62 – 79Combined sources18
Helixi91 – 101Combined sources11
Helixi104 – 117Combined sources14
Beta strandi120 – 128Combined sources9
Beta strandi134 – 140Combined sources7
Helixi145 – 148Combined sources4
Beta strandi151 – 157Combined sources7
Helixi160 – 162Combined sources3
Helixi164 – 167Combined sources4
Helixi171 – 178Combined sources8
Helixi179 – 181Combined sources3
Helixi184 – 190Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19665.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.
KOiK04564.
OMAiCMKPAGG.

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

        10         20         30         40         50
MTHELISLPY AVDALAPVIS KETVEFHHGK HLKTYVDNLN KLIIGTEFEN
60 70 80 90 100
ADLNTIVQKS EGGIFNNAGQ TLNHNLYFTQ FRPGKGGAPK GKLGEAIDKQ
110 120 130 140 150
FGSFEKFKEE FNTAGTTLFG SGWVWLASDA NGKLSIEKEP NAGNPVRKGL
160 170 180 190
NPLLGFDVWE HAYYLTYQNR RADHLKDLWS IVDWDIVESR Y
Length:191
Mass (Da):21,501
Last modified:May 1, 1991 - v2
Checksum:iAA53419397BF6BA1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13D → Y in AAA25651 (PubMed:1840572).Curated1
Sequence conflicti29G → E AA sequence (PubMed:2226833).Curated1
Sequence conflicti112N → D in AAA25651 (PubMed:1840572).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90152 Genomic DNA. Translation: BAA14182.1.
M60401 Genomic DNA. Translation: AAA25651.1.
AE015924 Genomic DNA. Translation: AAQ66583.1.
PIRiA43585.
RefSeqiWP_004585361.1. NC_002950.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90152 Genomic DNA. Translation: BAA14182.1.
M60401 Genomic DNA. Translation: AAA25651.1.
AE015924 Genomic DNA. Translation: AAQ66583.1.
PIRiA43585.
RefSeqiWP_004585361.1. NC_002950.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi242619.PG1545.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.
KOiK04564.
OMAiCMKPAGG.

Miscellaneous databases

EvolutionaryTraceiP19665.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.