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P31687 (4CL2_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Clone 4CL16
OrganismGlycine max (Soybean) (Glycine hispida)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycine

Protein attributes

Sequence length562 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.

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 – 5625624-coumarate--CoA ligase 2
PRO_0000193039

Sequences

Sequence LengthMass (Da)Tools
P31687 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 2AB4652DDA5160B2

FASTA56260,963
        10         20         30         40         50         60 
MITLAPSLDT PKTDQNQVSD PQTSHVFKSK LPDIPISNHL PLHSYCFQNL SQFAHRPCLI 

        70         80         90        100        110        120 
VGPASKTFTY ADTHLISSKI AAGLSNLGIL KGDVVMILLQ NSADFVFSFL AISMIGAVAT 

       130        140        150        160        170        180 
TANPFYTAPE IFKQFTVSKA KLIITQAMYV DKLRNHDGAK LGEDFKVVTV DDPPENCLHF 

       190        200        210        220        230        240 
SVLSEANESD VPEVEIHPDD AVAMPFSSGT TGLPKGVILT HKSLTTSVAQ QVDGENPNLY 

       250        260        270        280        290        300 
LTTEDVLLCV LPLFHIFSLN SVLLCALRAG SAVLLMQKFE IGTLLELIQR HRVSVAMVVP 

       310        320        330        340        350        360 
PLVLALAKNP MVADFDLSSI RLVLSGAAPL GKELEEALRN RMPQAVLGQG YGMTEAGPVL 

       370        380        390        400        410        420 
SMCLGFAKQP FQTKSGSCGT VVRNAELKVV DPETGRSLGY NQPGEICIRG QQIMKGYLND 

       430        440        450        460        470        480 
EAATASTIDS EGWLHTGDVG YVDDDDEIFI VDRVKELIKY KGFQVPPAEL EGLLVSHPSI 

       490        500        510        520        530        540 
ADAAVVPQKD VAAGEVPVAF VVRSNGFDLT EEAVKEFIAK QVVFYKRLHK VYFVHAIPKS 

       550        560 
PSGKILRKDL RAKLETAATQ TP 

« Hide

References

[1]Lindermayr C.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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] OF 140-562.
Strain: cv. Harosoy 63.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69955 mRNA. Translation: CAC36095.1.
PIRPQ0772.
UniGeneGma.8472.

3D structure databases

ProteinModelPortalP31687.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA6.2.1.12. 2483.

Gene expression databases

GenevestigatorP31687.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. 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_SOYBN
AccessionPrimary (citable) accession number: P31687
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: August 14, 2001
Last modified: September 21, 2011
This is version 60 of the entry and version 2 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