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

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 .
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

B39827; B39827.

3D structure databases

HSSP

P08659; 1LCI. [HSSP ENTRY / PDB]

ModBase

P31685.

Ontologies

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.

PRINTS

PR00154; AMPBINDING.

PROSITE

PS00455; AMP_BINDING; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Ligase; Phenylpropanoid metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 545`	`545`		`4-coumarate--CoA ligase 2.`	`PRO_0000193037`

Sequence information

Length: 545 AA [This is the length of the unprocessed precursor]

Molecular weight: 59625 Da [This is the MW of the unprocessed precursor]

CRC64: 5481F0B0AFEA39E0 [This is a checksum on the sequence]

        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

P31685 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools