[1]	NUCLEOTIDE SEQUENCE [MRNA]. Lindermayr C.; Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 140-562. 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

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

EMBL

X69955; CAC36095.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

PQ0772; PQ0772.

UniGene

Gma.8472

3D structure databases

HSSP

P08659; 1LCI. [HSSP ENTRY / PDB]

ModBase

P31687.

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`	`1 562`	`562`		`4-coumarate--CoA ligase 2.`	`PRO_0000193039`

Sequence information

Length: 562 AA [This is the length of the unprocessed precursor]

Molecular weight: 60963 Da [This is the MW of the unprocessed precursor]

CRC64: 2AB4652DDA5160B2 [This is a checksum on the sequence]

        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

P31687 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