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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Photobacterium leiognathi
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Copper; catalytic
Metal bindingi69 – 691Copper; catalytic
Metal bindingi92 – 921Copper; catalytic
Metal bindingi92 – 921Zinc; structural
Metal bindingi101 – 1011Zinc; structural
Metal bindingi110 – 1101Zinc; structural
Metal bindingi113 – 1131Zinc; structural
Metal bindingi147 – 1471Copper; catalytic

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:sodC
OrganismiPhotobacterium leiognathi
Taxonomic identifieri553611 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 173151Superoxide dismutase [Cu-Zn]PRO_0000032836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 169

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi1001530.PMSV_2027.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 318Combined sources
Turni32 – 343Combined sources
Beta strandi37 – 4610Combined sources
Beta strandi49 – 568Combined sources
Beta strandi61 – 644Combined sources
Beta strandi66 – 727Combined sources
Beta strandi77 – 793Combined sources
Beta strandi82 – 843Combined sources
Helixi87 – 893Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi129 – 1313Combined sources
Helixi136 – 1394Combined sources
Beta strandi143 – 1497Combined sources
Beta strandi153 – 1586Combined sources
Helixi159 – 1624Combined sources
Beta strandi165 – 1717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZOX-ray2.10A23-173[»]
1IB5X-ray2.45A23-173[»]
1IBBX-ray2.10A23-173[»]
1IBDX-ray2.00A23-173[»]
1IBFX-ray2.20A23-173[»]
1IBHX-ray2.00A23-173[»]
1OAJX-ray1.73A23-173[»]
1OALX-ray1.50A23-173[»]
1YAIX-ray1.90A/B/C23-173[»]
ProteinModelPortaliP00446.
SMRiP00446. Positions 23-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00446.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKAKTLLFT ALAFGLSHQA LAQDLTVKMT DLQTGKPVGT IELSQNKYGV
60 70 80 90 100
VFTPELADLT PGMHGFHIHQ NGSCASSEKD GKVVLGGAAG GHYDPEHTNK
110 120 130 140 150
HGFPWTDDNH KGDLPALFVS ANGLATNPVL APRLTLKELK GHAIMIHAGG
160 170
DNHSDMPKAL GGGGARVACG VIQ
Length:173
Mass (Da):18,109
Last modified:April 1, 1988 - v1
Checksum:i5931576F1E2A8F47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02658 Genomic DNA. Translation: AAA25632.1.
PIRiA26689. DSFOCL.
RefSeqiWP_023934797.1. NZ_JZSL01000044.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02658 Genomic DNA. Translation: AAA25632.1.
PIRiA26689. DSFOCL.
RefSeqiWP_023934797.1. NZ_JZSL01000044.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZOX-ray2.10A23-173[»]
1IB5X-ray2.45A23-173[»]
1IBBX-ray2.10A23-173[»]
1IBDX-ray2.00A23-173[»]
1IBFX-ray2.20A23-173[»]
1IBHX-ray2.00A23-173[»]
1OAJX-ray1.73A23-173[»]
1OALX-ray1.50A23-173[»]
1YAIX-ray1.90A/B/C23-173[»]
ProteinModelPortaliP00446.
SMRiP00446. Positions 23-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1001530.PMSV_2027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.

Miscellaneous databases

EvolutionaryTraceiP00446.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_PHOLE
AccessioniPrimary (citable) accession number: P00446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: September 7, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.