Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P31685 (4CL2_SOLTU)

Last modified June 16, 2009. Version 44. 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 2
      Short name=4CL 2
    EC=6.2.1.12
Alternative name(s):
    4-coumaroyl-CoA synthase 2
Gene names
Name: 4CL2
Synonyms: 4CL-2
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

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 – 5455454-coumarate--CoA ligase 2
PRO_0000193037

Sequences

Sequence LengthMass (Da)Tools
P31685-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 5481F0B0AFEA39E0

FASTA54559,625
        10         20         30         40         50         60 
MPMDIETKQS GDLIFRSKLP DIYIPKHLPL HSYCFENLSE FNSRPCLIDG ANDRIYTYAE 

        70         80         90        100        110        120 
VELTSRKVAV GLNKLGIQQK DTIMILLPNC PEFVFAFIGA SYLGAISTMA NPLFTPAEVV 

       130        140        150        160        170        180 
KQAKASSAKI VITQACFAGK VKDYAIENDL KVICVDSAPE GCVHFSELIQ SDEHEIPDVK 

       190        200        210        220        230        240 
IQPDDVVALP YSSGTTGLPK GVMLTHKGLV TSVAQQVDGE NANLYMHSDD VLMCVLPLFH 

       250        260        270        280        290        300 
IYSLNSVLLC ALRVGAAILI MQKFDIAQFL ELIPKHKVTI GPFVPPIVLA IAKSPLVHNY 

       310        320        330        340        350        360 
DLSSVRTVMS GAAPLGKELE DAVRAKFPNA KLGQGYGMTE AGPVLAMCLA FAKEPFDIKS 

       370        380        390        400        410        420 
GACGTVVRNA EMKIVDPDTG CSLPRNQPGE ICIRGDQIMK GYLNDPEATA RTIEKEGWLH 

       430        440        450        460        470        480 
TGDIGFIDDD DELFIVDRLK ELIKYKGFQV APAELEALLI NHPDISDAAV VPMIDEQAGE 

       490        500        510        520        530        540 
VPVAFVVRSN GSTITEDEVK DFISKQVIFY KRIKRVFFVE TVPKSPSGKI LRKDLRARLA 


AGISN 

« Hide

References

[1]"Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate: CoA ligase genes in potato."
Becker-Andre M., Schulze-Lefert P., Hahlbrock K.
J. Biol. Chem. 266:8551-8559(1991) [PubMed: 2022667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

PIRB39827.

3D structure databases

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

Enzyme and pathway databases

BRENDA6.2.1.12. 296.

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 name4CL2_SOLTU
AccessionPrimary (citable) accession number: P31685
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 44 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