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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)DescriptionActionsGraphical viewLength
Metal bindingi67Copper; catalytic1
Metal bindingi69Copper; catalytic1
Metal bindingi92Copper; catalytic1
Metal bindingi92Zinc; structural1
Metal bindingi101Zinc; structural1
Metal bindingi110Zinc; structural1
Metal bindingi113Zinc; structural1
Metal bindingi147Copper; catalytic1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000003283623 – 173Superoxide dismutase [Cu-Zn]Add BLAST151

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi74 ↔ 169

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi1001530.PMSV_2027.

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 31Combined sources8
Turni32 – 34Combined sources3
Beta strandi37 – 46Combined sources10
Beta strandi49 – 56Combined sources8
Beta strandi61 – 64Combined sources4
Beta strandi66 – 72Combined sources7
Beta strandi77 – 79Combined sources3
Beta strandi82 – 84Combined sources3
Helixi87 – 89Combined sources3
Beta strandi107 – 109Combined sources3
Beta strandi117 – 119Combined sources3
Beta strandi129 – 131Combined sources3
Helixi136 – 139Combined sources4
Beta strandi143 – 149Combined sources7
Beta strandi153 – 158Combined sources6
Helixi159 – 162Combined sources4
Beta strandi165 – 171Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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: November 2, 2016
This is version 112 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.