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Protein

Epidermin decarboxylase

Gene

epiD

Organism
Staphylococcus epidermidis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of two reducing equivalents (oxidative decarboxylation) from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond.

Cofactori

FMNNote: Binds 1 FMN per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei671

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermin decarboxylase (EC:4.1.1.-)
Alternative name(s):
Epidermin-modifying enzyme EpiD
Gene namesi
Name:epiD
Encoded oniPlasmid pTu 320 Publication
OrganismiStaphylococcus epidermidis
Taxonomic identifieri1282 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43F → L: Binds FMN, but activity is significantly decreased. 1 Publication1
Mutagenesisi67H → N: Retains less than 1% activity, binds FMN. 1 Publication1
Mutagenesisi75E → D or Q: Binds FMN. 1 Publication1
Mutagenesisi81P → D: Loss of FMN binding. 1 Publication1
Mutagenesisi83S → A: Loss of FMN binding. 1 Publication1
Mutagenesisi83S → T: Binds FMN. 1 Publication1
Mutagenesisi84A → V: Binds FMN. 1 Publication1
Mutagenesisi85N → D or H: Loss of FMN binding. 1 Publication1
Mutagenesisi93G → A or D: Loss of FMN binding. 1 Publication1
Mutagenesisi95C → A: Binds FMN. 1 Publication1
Mutagenesisi96D → N: Loss of FMN binding. 1 Publication1
Mutagenesisi98L → V: Binds FMN. 1 Publication1
Mutagenesisi103C → A: Binds FMN. 1 Publication1
Mutagenesisi114P → A: Loss of FMN binding. 1 Publication1
Mutagenesisi115N → D: Retains less than 1% activity, binds FMN. 1 Publication1
Mutagenesisi117N → D: Binds FMN. 1 Publication1
Mutagenesisi120M → L: Retains less than 1% activity, binds FMN. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001820341 – 181Epidermin decarboxylaseAdd BLAST181

Interactioni

Subunit structurei

Homododecamer.

Structurei

Secondary structure

1181
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi13 – 17Combined sources5
Helixi18 – 25Combined sources8
Turni26 – 28Combined sources3
Beta strandi32 – 36Combined sources5
Helixi38 – 42Combined sources5
Helixi46 – 51Combined sources6
Turni59 – 61Combined sources3
Helixi67 – 72Combined sources6
Beta strandi75 – 82Combined sources8
Helixi84 – 91Combined sources8
Helixi98 – 105Combined sources8
Helixi107 – 109Combined sources3
Beta strandi110 – 114Combined sources5
Helixi118 – 121Combined sources4
Helixi124 – 134Combined sources11
Turni135 – 137Combined sources3
Beta strandi144 – 150Combined sources7
Beta strandi151 – 157Combined sources7
Helixi165 – 173Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G5QX-ray2.57A/D/G/L1-181[»]
1G63X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliP30197.
SMRiP30197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30197.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1950. 1 hit.
InterProiIPR003382. Flavoprotein.
[Graphical view]
PfamiPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF52507. SSF52507. 1 hit.

Sequencei

Sequence statusi: Complete.

P30197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYGKLLICAT ASINVININH YIVELKQHFD EVNILFSPSS KNFINTDVLK
60 70 80 90 100
LFCDNLYDEI KDPLLNHINI VENHEYILVL PASANTINKI ANGICDNLLT
110 120 130 140 150
TVCLTGYQKL FIFPNMNIRM WGNPFLQKNI DLLKNNDVKV YSPDMNKSFE
160 170 180
ISSGRYKNNI TMPNIENVLN FVLNNEKRPL D
Length:181
Mass (Da):20,825
Last modified:April 1, 1993 - v1
Checksum:i126830E0B987CE2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62386 Genomic DNA. Translation: CAA44255.1.
PIRiS23418.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62386 Genomic DNA. Translation: CAA44255.1.
PIRiS23418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G5QX-ray2.57A/D/G/L1-181[»]
1G63X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliP30197.
SMRiP30197.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP30197.

Family and domain databases

Gene3Di3.40.50.1950. 1 hit.
InterProiIPR003382. Flavoprotein.
[Graphical view]
PfamiPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF52507. SSF52507. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEPID_STAEP
AccessioniPrimary (citable) accession number: P30197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 69 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, Plasmid

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.