Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P17814 (4CL1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 4-coumarate--CoA ligase 1

Short name=4CL 1
Short name=Os4CL1
EC=6.2.1.12
Alternative name(s):
4-coumaroyl-CoA synthase 1
Gene names
Name:4CL1
Synonyms:4CL
Ordered Locus Names:Os08g0245200, LOC_Os08g14760
ORF Names:OJ1033_B09.16
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length564 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.

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.

Sequence similarities

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

Sequence caution

The sequence BAD05189.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA36850.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA36850.1 differs from that shown. Reason: Frameshift at position 496.

Ontologies

Keywords
   Biological processPhenylpropanoid metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
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: UniProtKB-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 – 564564Probable 4-coumarate--CoA ligase 1
PRO_0000193031

Regions

Nucleotide binding209 – 2179ATP By similarity
Nucleotide binding352 – 3576ATP By similarity
Region282 – 35170SBD1
Region352 – 41968SBD2

Sites

Binding site4401ATP By similarity
Binding site4551ATP By similarity
Binding site5471ATP By similarity

Experimental info

Sequence conflict4051P → R in CAA36850. Ref.1
Sequence conflict4771I → N in CAA36850. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17814 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 9725A4B4A72F8C6E

FASTA56460,902
        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 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of rice 4-coumarate:CoA ligase gene, 4-CL.1."
Zhao Y., Kung S.D., Dube S.K.
Nucleic Acids Res. 18:6144-6144(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
The rice full-length cDNA consortium
Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.
[5]"Genome-wide analysis of a land plant-specific acyl:coenzyme A synthetase (ACS) gene family in Arabidopsis, poplar, rice and Physcomitrella."
de Azevedo Souza C., Barbazuk B., Ralph S.G., Bohlmann J., Hamberger B., Douglas C.J.
New Phytol. 179:987-1003(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52623 Genomic DNA. Translation: CAA36850.1. Sequence problems.
AP003859 Genomic DNA. Translation: BAD05189.1. Different initiation.
AP008214 Genomic DNA. Translation: BAF23267.1.
AK069932 mRNA. No translation available.
PIRJU0311.
RefSeqNP_001061353.1. NM_001067888.1.
UniGeneOs.52921.

3D structure databases

ProteinModelPortalP17814.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP17814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsOS08T0245200-01; OS08T0245200-01; OS08G0245200.
GeneID4345054.
KEGGosa:4345054.

Organism-specific databases

GrameneP17814.

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000230009.
KOK01904.
OMAAGTNKID.

Enzyme and pathway databases

UniPathwayUPA00372; UER00547.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name4CL1_ORYSJ
AccessionPrimary (citable) accession number: P17814
Secondary accession number(s): Q0J6Z8, Q6ZKV9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: September 27, 2005
Last modified: May 14, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PATHWAY comments

Index of metabolic and biosynthesis pathways