Reviewed, UniProtKB/Swiss-Prot P31687 (4CL2_SOYBN)

Names and origin

Protein names	Recommended name:     4-coumarate--CoA ligase 2       Short name=4CL 2     EC=6.2.1.12 Alternative name(s):     4-coumaroyl-CoA synthase 2     Clone 4CL16
Organism	Glycine max (Soybean)
Taxonomic identifier	3847 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 4-coumaric acid: step 1/2.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	phenylpropanoid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-coumarate-CoA ligase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 562	562	4-coumarate--CoA ligase 2		PRO_0000193039

Sequences

	Sequence		Length	Mass (Da)
	P31687-1 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 2AB4652DDA5160B2	FASTA	562	60,963
	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

References

[1]	Lindermayr C. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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." Uhlmann A., Ebel J. Plant Physiol. 102:1147-1156(1993) [PubMed: 8278545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-562. Strain: cv. Harosoy 63.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X69955 mRNA. Translation: CAC36095.1.
PIR	PQ0772.
UniGene	Gma.8472
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Enzyme and pathway databases
BRENDA	6.2.1.12. 299.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

4CL2_SOYBN

Accession

Primary (citable) accession number: P31687

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	August 14, 2001
Last modified:	June 16, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)