4CL2_SOYBN
ID 4CL2_SOYBN Reviewed; 562 AA.
AC P31687;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=4-coumarate--CoA ligase 2;
DE Short=4CL 2;
DE EC=6.2.1.12;
DE AltName: Full=4-coumaroyl-CoA synthase 2;
DE AltName: Full=Clone 4CL16;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lindermayr C.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-562.
RC STRAIN=cv. Harosoy 63;
RX PubMed=8278545; DOI=10.1104/pp.102.4.1147;
RA Uhlmann A., Ebel J.;
RT "Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an
RT enzyme involved in the resistance response of soybean (Glycine max L.)
RT against pathogen attack.";
RL Plant Physiol. 102:1147-1156(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC 1/2.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; X69955; CAC36095.1; -; mRNA.
DR PIR; PQ0772; PQ0772.
DR RefSeq; NP_001236236.1; NM_001249307.1.
DR AlphaFoldDB; P31687; -.
DR SMR; P31687; -.
DR STRING; 3847.GLYMA01G44270.1; -.
DR GeneID; 547930; -.
DR KEGG; gmx:547930; -.
DR eggNOG; KOG1176; Eukaryota.
DR OrthoDB; 298283at2759; -.
DR BRENDA; 6.2.1.12; 2483.
DR UniPathway; UPA00372; UER00547.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism;
KW Reference proteome.
FT CHAIN 1..562
FT /note="4-coumarate--CoA ligase 2"
FT /id="PRO_0000193039"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 60963 MW; 2AB4652DDA5160B2 CRC64;
MITLAPSLDT PKTDQNQVSD PQTSHVFKSK LPDIPISNHL PLHSYCFQNL SQFAHRPCLI
VGPASKTFTY ADTHLISSKI AAGLSNLGIL KGDVVMILLQ NSADFVFSFL AISMIGAVAT
TANPFYTAPE IFKQFTVSKA KLIITQAMYV DKLRNHDGAK LGEDFKVVTV DDPPENCLHF
SVLSEANESD VPEVEIHPDD AVAMPFSSGT TGLPKGVILT HKSLTTSVAQ QVDGENPNLY
LTTEDVLLCV LPLFHIFSLN SVLLCALRAG SAVLLMQKFE IGTLLELIQR HRVSVAMVVP
PLVLALAKNP MVADFDLSSI RLVLSGAAPL GKELEEALRN RMPQAVLGQG YGMTEAGPVL
SMCLGFAKQP FQTKSGSCGT VVRNAELKVV DPETGRSLGY NQPGEICIRG QQIMKGYLND
EAATASTIDS EGWLHTGDVG YVDDDDEIFI VDRVKELIKY KGFQVPPAEL EGLLVSHPSI
ADAAVVPQKD VAAGEVPVAF VVRSNGFDLT EEAVKEFIAK QVVFYKRLHK VYFVHAIPKS
PSGKILRKDL RAKLETAATQ TP
