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Protein

Superoxide dismutase [Cu-Zn] B

Gene

sod1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi45Copper; catalytic1
Metal bindingi47Copper; catalytic1
Metal bindingi62Copper; catalytic1
Metal bindingi62Zinc; structural1
Metal bindingi70Zinc; structural1
Metal bindingi79Zinc; structural1
Metal bindingi82Zinc; structural1
Metal bindingi118Copper; 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] B (EC:1.15.1.1)
Short name:
XSODB
Gene namesi
Name:sod1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254670. sod1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001640772 – 151Superoxide dismutase [Cu-Zn] BAdd BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi6S-palmitoyl cysteineBy similarity1
Disulfide bondi56 ↔ 144

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homodimer, and heterodimer of Superoxide dismutase [Cu-Zn] A and B.1 Publication

Structurei

Secondary structure

1151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi11 – 13Combined sources3
Beta strandi15 – 23Combined sources9
Beta strandi28 – 36Combined sources9
Beta strandi39 – 48Combined sources10
Helixi55 – 59Combined sources5
Beta strandi76 – 78Combined sources3
Beta strandi82 – 89Combined sources8
Beta strandi92 – 101Combined sources10
Beta strandi103 – 106Combined sources4
Beta strandi113 – 120Combined sources8
Beta strandi127 – 129Combined sources3
Helixi132 – 135Combined sources4
Beta strandi141 – 146Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XSOX-ray1.49A/B2-151[»]
ProteinModelPortaliP15107.
SMRiP15107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15107.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

HOVERGENiHBG000062.
KOiK04565.

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]
PRINTSiPR00068. CUZNDISMTASE.
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.

P15107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKAVCVLAG SGDVKGVVHF EQQDEGAVSV EGKIEGLTDG LHGFHIHVFG
60 70 80 90 100
DNTNGCMSAG SHFNPENKNH GAPGDTDRHV GDLGNVTAEG GVAQFKITDS
110 120 130 140 150
LISLKGPNSI IGRTAVVHEK ADDLGKGGND ESLKTGNAGG RLACGVIGYS

P
Length:151
Mass (Da):15,418
Last modified:January 23, 2007 - v3
Checksum:i8DA6A8FDA1C7FB36
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61S → P AA sequence (PubMed:2751312).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51518 mRNA. Translation: CAA35890.1.
BC070696 mRNA. Translation: AAH70696.1.
PIRiS09568.
RefSeqiNP_001080933.1. NM_001087464.1.
UniGeneiXl.42.

Genome annotation databases

GeneIDi394274.
KEGGixla:394274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51518 mRNA. Translation: CAA35890.1.
BC070696 mRNA. Translation: AAH70696.1.
PIRiS09568.
RefSeqiNP_001080933.1. NM_001087464.1.
UniGeneiXl.42.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XSOX-ray1.49A/B2-151[»]
ProteinModelPortaliP15107.
SMRiP15107.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi394274.
KEGGixla:394274.

Organism-specific databases

CTDi394274.
XenbaseiXB-GENE-6254670. sod1.

Phylogenomic databases

HOVERGENiHBG000062.
KOiK04565.

Miscellaneous databases

EvolutionaryTraceiP15107.

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]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSOD1B_XENLA
AccessioniPrimary (citable) accession number: P15107
Secondary accession number(s): Q5D025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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.