Skip Header

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

Reviewed, UniProtKB/Swiss-Prot P31686 (4CL1_SOYBN)

Last modified June 16, 2009. Version 45. 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
    Clone 4CL14
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IFabalesFabaceaePapilionoideaePhaseoleaeGlycine

Protein attributes

Sequence length293 AA.
Sequence statusFragment.
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.

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

Chain‹1 – 293›2934-coumarate--CoA ligase 1
PRO_0000193038

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P31686-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 25868497FCC022EC

FASTA29332,027
        10         20         30         40         50         60 
AKATILLMPK FDINSLLALI HKHKVTIAPV VPPIVLAISK SPDLHKYDLS SIRVLKSGGA 

        70         80         90        100        110        120 
PLGKELEDTL RAKFPNAKLG QGYGMTEAGP VLTMSLAFAK EPIDVKPGAC GTVVRNAEMK 

       130        140        150        160        170        180 
IVDPETGHSL PRNQSGEICI RGDQIMKGYL NDGEATERTI DKDGWLHTGD IGYIDDDDEL 

       190        200        210        220        230        240 
FIVDRLKELI KYKGFQVAPA ELEALLLTHP KISDAAVVPM KDEAAGEVPV AFVVISNGYT 

       250        260        270        280        290 
DTTEDEIKQF ISKQVVFYKR INRVFFIDAI PKSPSGKILR KDLRAKIAAS VPK 

« Hide

References

[1]"Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an enzyme involved in the resistance response of soybean (Glycine max L.) against pathogen attack."
Uhlmann A., Ebel J.
Plant Physiol. 102:1147-1156(1993) [PubMed: 8278545] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Harosoy 63.

Cross-references

Sequence databases

X69954 mRNA. Translation: CAA49575.1.
PIRS31705.

3D structure databases

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

Enzyme and pathway databases

BRENDA6.2.1.12. 299.

Family and domain databases

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

Entry information

Entry name4CL1_SOYBN
AccessionPrimary (citable) accession number: P31686
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 45 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