ID C4J009_MAIZE Unreviewed; 722 AA.
AC C4J009;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN ORFNames=ZEAMMB73_Zm00001d020343 {ECO:0000313|EMBL:ONM54732.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACR34509.1};
RN [1] {ECO:0000313|EMBL:ACR34509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACR34509.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EMBL:ONM54732.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb311650_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM54732.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb311650_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb311650_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00034252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000256|ARBA:ARBA00034252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP +
CC diphosphate; Xref=Rhea:RHEA:72419, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:192348; Evidence={ECO:0000256|ARBA:ARBA00034219};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420;
CC Evidence={ECO:0000256|ARBA:ARBA00034219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+);
CC Xref=Rhea:RHEA:72423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:192348, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; BT084156; ACR34509.1; -; mRNA.
DR EMBL; CM007650; ONM54732.1; -; Genomic_DNA.
DR EMBL; CM007650; ONM54733.1; -; Genomic_DNA.
DR RefSeq; NP_001152332.1; NM_001158860.1.
DR AlphaFoldDB; C4J009; -.
DR PaxDb; 4577-GRMZM2G472376_P02; -.
DR EnsemblPlants; Zm00001eb311650_T001; Zm00001eb311650_P001; Zm00001eb311650.
DR EnsemblPlants; Zm00001eb311650_T002; Zm00001eb311650_P002; Zm00001eb311650.
DR GeneID; 100285971; -.
DR Gramene; Zm00001eb311650_T001; Zm00001eb311650_P001; Zm00001eb311650.
DR Gramene; Zm00001eb311650_T002; Zm00001eb311650_P002; Zm00001eb311650.
DR KEGG; zma:100285971; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_8_1; -.
DR OMA; TGWIMYM; -.
DR OrthoDB; 760232at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; C4J009; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR44378; ACYL-ACTIVATING ENZYME 17, PEROXISOMAL-RELATED; 1.
DR PANTHER; PTHR44378:SF2; ACYL-ACTIVATING ENZYME 17, PEROXISOMAL-RELATED; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:C4J009};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 241..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..174
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 182..549
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 722 AA; 78337 MW; BCD3C3C3039038F8 CRC64;
MATTLHKPLG AITVDDLAAA APGSDATALH AALRRALDSH GPTEVWGELC RSVLCPSVPF
AVHRMLYYGC FAGFPSPTPP AWTPDPKESV LTNVGRVLEA RGRNLIGDAY KDPITSFPDL
HKFSNENPEA YWKMVFEDMG IQFSVEPSCI WRENTAYPGG EWLPGAELNA AVNCLTAKPG
RSSDGPAIVW RDEGKDSDPL NFMSLEDLRK KVCLVANAID ALELPKGSAI AIDMPMDVNA
VVIYLAIVLA GYVVVSIADS FAAPAISMRL KLSEAKAIFT QDYILRDDKE LPLYSRVVEA
KAPMAIVIPV RGSLLIKGLR VDDLSWQDFL GRVNYTEAEN YTAVNQPAYA FTNILFSSGT
TGEPKAIPWT HITPLKAAAD GWCHMDIRKG DVVAWPTNLG WMMGPWLVYA SLLNGASMAL
YNGSPNSSGF AKFVQDAKVT MLGLVPSIVR TWKNTDCTAG LDWSSIRCFS SSGEASSVDD
YLWLMGRAGY KPVIEYCGGT EIGGGFVTGS MLQPQALSAF STPAMGCNLF ILDSSGNPLP
QDSVGIGELA LDPTLFGSST TLLNADHQEV YFNGMPEWHG KILRRHGDEF ERTSDGYYRA
HGRADDTMNL GGIKVSSIEI ERICNRVHDA ILETAAIGVP PVGGGPEQLT IAVVLKDQSS
QIEDLNQLKL ACNMALKKLN PLFKVSSVVI VPSLPRTASN KVMRRVLRKE FSQAAQAKHS
KI
//
