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P14913 (4CL2_PETCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:4CL2
Synonyms:4CL-2
OrganismPetroselinum crispum (Parsley) (Petroselinum hortense)
Taxonomic identifier4043 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsApialesApiaceaeApioideaeapioid supercladeApieaePetroselinum

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
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 trans-4-coumarate: 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_0000193034

Sequences

Sequence LengthMass (Da)Tools
P14913 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: B477965C68F8C534

FASTA54459,783
        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 
LKASLAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVID 

       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 KDLRAKIASG 


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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13325 mRNA. Translation: CAA31697.1.
X05351 Genomic DNA. Translation: CAA28960.1.
PIRS15695.

3D structure databases

ProteinModelPortalP14913.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00372; UER00547.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name4CL2_PETCR
AccessionPrimary (citable) accession number: P14913
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families