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Reviewed, UniProtKB/Swiss-Prot P14912 (4CL1_PETCR)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    4-coumarate--CoA ligase 1
      Short name=4CL 1
    EC=6.2.1.12
Alternative name(s):
    4-coumaroyl-CoA synthase 1
Gene names
Name: 4CL1
Synonyms: 4CL-1
OrganismPetroselinum crispum (Parsley) (Petroselinum hortense)
Taxonomic identifier4043 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsApialesApiaceaeApioideaeapioid supercladeApium cladePetroselinum

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA.

Pathway

Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from 4-coumaric acid: step 1/2.

Induction

By fungal elicitor and UV irradiation.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processPhenylpropanoid metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological processphenylpropanoid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function4-coumarate-CoA ligase activity

Inferred from electronic annotation. Source: EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5445444-coumarate--CoA ligase 1
PRO_0000193033

Sequences

Sequence LengthMass (Da)Tools
P14912-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 22BBAD78F255D0C8

FASTA54459,825
        10         20         30         40         50         60 
MGDCVAPKED LIFRSKLPDI YIPKHLPLHT YCFENISKVG DKSCLINGAT GETFTYSQVE 

        70         80         90        100        110        120 
LLSRKVASGL NKLGIQQGDT IMLLLPNSPE YFFAFLGASY RGAISTMANP FFTSAEVIKQ 

       130        140        150        160        170        180 
LKASQAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVIN 

       190        200        210        220        230        240 
SDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGDNP NLYMHSEDVM ICILPLFHIY 

       250        260        270        280        290        300 
SLNAVLCCGL RAGVTILIMQ KFDIVPFLEL IQKYKVTIGP FVPPIVLAIA KSPVVDKYDL 

       310        320        330        340        350        360 
SSVRTVMSGA APLGKELEDA VRAKFPNAKL GQGYGMTEAG PVLAMCLAFA KEPYEIKSGA 

       370        380        390        400        410        420 
CGTVVRNAEM KIVDPETNAS LPRNQRGEIC IRGDQIMKGY LNDPESTRTT IDEEGWLHTG 

       430        440        450        460        470        480 
DIGFIDDDDE LFIVDRLKEI IKYKGFQVAP AELEALLLTH PTISDAAVVP MIDEKAGEVP 

       490        500        510        520        530        540 
VAFVVRTNGF TTTEEEIKQF VSKQVVFYKR IFRVFFVDAI PKSPSGKILR KDLRARIASG 


DLPK 

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References

[1]"Primary structures and catalytic properties of isoenzymes encoded by the two 4-coumarate:CoA ligase genes in parsley."
Lozoya E., Hoffmann H., Douglas C., Schulz W., Scheel D., Hahlbrock K.
Eur. J. Biochem. 176:661-667(1988) [PubMed: 3169018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Structure and elicitor or U.V.-light-stimulated expression of two 4-coumarate:CoA ligase genes in parsley."
Douglas C., Hoffmann H., Schulz W., Hahlbrock K.
EMBO J. 6:1189-1195(1987) [PubMed: 16453765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-8.

Cross-references

Sequence databases

X13324 mRNA. Translation: CAA31696.1.
X05350 Genomic DNA. Translation: CAA28959.1.
PIRS01667.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.2.1.12. 2662.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name4CL1_PETCR
AccessionPrimary (citable) accession number: P14912
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents