[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/18.20.6144; PubMed=2235510 [NCBI, ExPASy, EBI, Israel, Japan] Zhao Y., Kung S.D., Dube S.K.; "Nucleotide sequence of rice 4-coumarate:CoA ligase gene, 4-CL.1."; Nucleic Acids Res. 18:6144-6144(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1038/nature03895; PubMed=16100779 [NCBI, ExPASy, EBI, Israel, Japan] International rice genome sequencing project (IRGSP); "The map-based sequence of the rice genome."; Nature 436:793-800(2005).
[3]	GENOME REANNOTATION. STRAIN=cv. Nipponbare; DOI=10.1101/gr.5509507; PubMed=17210932 [NCBI, ExPASy, EBI, Israel, Japan] The rice annotation project (RAP); "Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana."; Genome Res. 17:175-183(2007).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Nipponbare; DOI=10.1126/science.1081288; PubMed=12869764 [NCBI, ExPASy, EBI, Israel, Japan] The rice full-length cDNA consortium; "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."; Science 301:376-379(2003).
[5]	GENE FAMILY. DOI=10.1111/j.1469-8137.2008.02534.x; PubMed=18627494 [NCBI, ExPASy, EBI, Israel, Japan] de Azevedo Souza C., Barbazuk B., Ralph S.G., Bohlmann J., Hamberger B., Douglas C.J.; "Genome-wide analysis of a land plant-specific acyl:coenzyme A synthetase (ACS) gene family in Arabidopsis, poplar, rice and Physcomitrella."; New Phytol. 179:987-1003(2008).

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 .
INDUCTION: By fungal elicitor and UV irradiation.
DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
SEQUENCE CAUTION:
- Sequence=CAA36850.1; Type=Erroneous gene model prediction;
- Sequence=CAA36850.1; Type=Frameshift; Positions=496;

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

X52623; CAA36850.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003859; BAD05189.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008214; BAF23267.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK069932; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

JU0311; JU0311.

NP_001061353.1; -.

3D structure databases

HSSP

P08659; 1LCI. [HSSP ENTRY / PDB]

ModBase

P17814.

Organism-specific databases

Gramene

P17814; -.

Ontologies

GO:0016207;	Molecular function: 4-coumarate-CoA ligase activity (inferred from electronic annotation from EC).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
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; 1.

Genome annotation databases

GeneID

4345054; -.

KEGG

osa:4345054; -.

Other

ProtoNet

P17814.

UniRef

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

Keywords

ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 564`	`564`	`Probable 4-coumarate--CoA ligase 1.`	`PRO_0000193031`
`NP_BIND`	`209 217`	`9`	`ATP (By similarity).`
`NP_BIND`	`352 357`	`6`	`ATP (By similarity).`
`REGION`	`282 351`	`70`	`SBD1.`
`REGION`	`352 419`	`68`	`SBD2.`
`BINDING`	`440 440`		`ATP (By similarity).`
`BINDING`	`455 455`		`ATP (By similarity).`
`BINDING`	`547 547`		`ATP (By similarity).`
`CONFLICT`	`405 405`		`P -> R (in Ref. 1; CAA36850).`
`CONFLICT`	`477 477`		`I -> N (in Ref. 1; CAA36850).`

Sequence information

Length: 564 AA [This is the length of the unprocessed precursor]

Molecular weight: 60902 Da [This is the MW of the unprocessed precursor]

CRC64: 9725A4B4A72F8C6E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSMEQQQPE SAAPATEASP EIIFRSKLQD IAITNTLPLH RYCFERLPEV AARPCLIDGA 

        70         80         90        100        110        120 
TGGVLTYADV DRLSRRLAAA LRRAPLGLRR GGVVMSLLRN SPEFVLSFFA ASRVGAAVTT 

       130        140        150        160        170        180 
ANPMSTPHEI ESQLAAAGAT VVITESMAAD KLPSHSHGAL TVVLIDERRD GCLHFWDDLM 

       190        200        210        220        230        240 
SEDEASPLAG DEDDEKVFDP DDVVALPYSS GTTGLPKGVM LTHRSLSTSV AQQVDGENPN 

       250        260        270        280        290        300 
IGLHAGDVIL CALPMFHIYS LNTIMMCGLR VGAAIVVMRR FDLAAMMDLV ERHRVTIAPL 

       310        320        330        340        350        360 
VPPIVVAVAK SEAAAARDLS SVRMVLSGAA PMGKDIEDAF MAKLPGAVLG QGYGMTEAGP 

       370        380        390        400        410        420 
VLSMCLAFAK EPFKVKSGAC GTVVRNAELK IIDPDTGKSL GRNLPGEICI RGQQIMKGYL 

       430        440        450        460        470        480 
NNPEATKNTI DAEGWLHTGD IGYVDDDDEI FIVDRLKEII KYRGFQVAPA ELEALLITHP 

       490        500        510        520        530        540 
SIADAAVVGK QIEPEIGEIP VAFVAKTEGS ELSEDDVKQF VAKEVIYYKK IREVFFVDKI 

       550        560 
PKAPSGKILR KELRKQLQHL QQEA

P17814 in FASTA 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