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Protein
Submitted name:

Ferulic acid decarboxylase

Gene
N/A
Organism
Enterobacter sp. Px6-4
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Ferulic acid decarboxylaseImported
OrganismiEnterobacter sp. Px6-4Imported
Taxonomic identifieri418698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NX1X-ray2.40A/B1-168[»]
3NX2X-ray2.01A/B1-168[»]
4UU2X-ray1.49A/B1-168[»]
4UU3X-ray1.15A/B1-168[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiC6F3U5.

Family & Domainsi

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR008729. PA_de_COase_bac.
[Graphical view]
PfamiPF05870. PA_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF011561. PAD. 1 hit.
ProDomiPD022010. PA_de_COase_bac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

C6F3U5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTFDKHDLS GFVGKHLVYT YDNGWEYEIY VKNENTLDYR IHSGLVGNRW
60 70 80 90 100
VKDQQAYIVR VGESIYKISW TEPTGTDVSL IVNLGDSLFH GTIFFPRWVM
110 120 130 140 150
NNPEKTVCFQ NDHIPLMNSY RDAGPAYPTE VIDEFATITF VRDCGANNES
160
VIACAASELP KNFPDNLK
Length:168
Mass (Da):19,195
Last modified:September 1, 2009 - v1
Checksum:i56964F5CCB56996C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU853825 Genomic DNA. Translation: ACJ26748.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU853825 Genomic DNA. Translation: ACJ26748.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NX1X-ray2.40A/B1-168[»]
3NX2X-ray2.01A/B1-168[»]
4UU2X-ray1.49A/B1-168[»]
4UU3X-ray1.15A/B1-168[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiC6F3U5.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR008729. PA_de_COase_bac.
[Graphical view]
PfamiPF05870. PA_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF011561. PAD. 1 hit.
ProDomiPD022010. PA_de_COase_bac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylase."
    Gu W., Li X., Huang J., Duan Y., Meng Z., Zhang K.Q., Yang J.
    Appl. Microbiol. Biotechnol. 89:1797-1805(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Px6-4Imported.
  2. "Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4."
    Gu W., Yang J., Lou Z., Liang L., Sun Y., Huang J., Li X., Cao Y., Meng Z., Zhang K.Q.
    PLoS ONE 6:e16262-e16262(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).
  3. "Regioselective Enzymatic beta-Carboxylation of para-Hydroxy- styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases."
    Wuensch C., Pavkov-Keller T., Steinkellner G., Gross J., Fuchs M., Hromic A., Lyskowski A., Fauland K., Gruber K., Glueck S.M., Faber K.
    Adv. Synth. Catal. 357:1909-1918(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS).

Entry informationi

Entry nameiC6F3U5_9ENTR
AccessioniPrimary (citable) accession number: C6F3U5
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: February 17, 2016
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.