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UniProtKB/Swiss-Prot entry P31686


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 4CL1_SOYBN
Primary accession number P31686
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 42)
Name and origin of the protein
Protein name 4-coumarate--CoA ligase 1 [Fragment]
Synonyms 4CL 1
EC 6.2.1.12
4-coumaroyl-CoA synthase 1
Clone 4CL14
Gene name None
From
Glycine max (Soybean) [TaxID: 3847] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Harosoy 63;
DOI=10.1104/pp.102.4.1147; PubMed=8278545 [NCBI, ExPASy, EBI, Israel, Japan]
Uhlmann A., Ebel J.;
"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.";
Plant Physiol. 102:1147-1156(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X69954; CAA49575.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S31705; S31705.
3D structure databases
HSSP P08659; 1LCI. [HSSP ENTRY / PDB]
ModBase P31686.
Ontologies
GO
GO:0016207; Molecular function: 4-coumarate-CoA ligase activity (inferred from electronic annotation from EC).
GO:0009698; Biological process: phenylpropanoid metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.
Pfam PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.
PROSITE PS00455; AMP_BINDING; PARTIAL.
BLOCKS P31686.
ProtoNet P31686.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Ligase; Phenylpropanoid metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   <1   293  >293     4-coumarate--CoA ligase 1. PRO_0000193038
NON_TER   1     1         
Sequence information
Length: 293 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 32027 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 25868497FCC022EC [This is a checksum on the sequence]
        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 

P31686 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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