ID B6SV29_MAIZE Unreviewed; 578 AA.
AC B6SV29;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN Name=100281397 {ECO:0000313|EnsemblPlants:Zm00001eb002380_P001};
GN ORFNames=ZEAMMB73_Zm00001d027499 {ECO:0000313|EMBL:ONL93287.1};
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:ACG28712.1};
RN [1] {ECO:0000313|EMBL:ACG28712.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [2] {ECO:0000313|EMBL:ONL93287.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb002380_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONL93287.1};
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:Zm00001eb002380_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb002380_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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; EU956594; ACG28712.1; -; mRNA.
DR EMBL; CM007647; ONL93287.1; -; Genomic_DNA.
DR RefSeq; NP_001147787.1; NM_001154315.1.
DR AlphaFoldDB; B6SV29; -.
DR SMR; B6SV29; -.
DR STRING; 4577.B6SV29; -.
DR PaxDb; 4577-GRMZM2G092813_P01; -.
DR EnsemblPlants; Zm00001eb002380_T001; Zm00001eb002380_P001; Zm00001eb002380.
DR GeneID; 100281397; -.
DR Gramene; Zm00001eb002380_T001; Zm00001eb002380_P001; Zm00001eb002380.
DR KEGG; zma:100281397; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; B6SV29; -.
DR OMA; RDGWCHT; -.
DR OrthoDB; 2596785at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B6SV29; baseline and differential.
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 CDD; cd12118; ttLC_FACS_AEE21_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR43859:SF2; BUTYRATE--COA LIGASE AAE11, PEROXISOMAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B6SV29};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 22..404
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 454..530
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 578 AA; 62669 MW; ABEE3BC1A3937CA3 CRC64;
MDQLPKRPAN YVPLSPVGFL PRANAVYGDR TSVIYRGVRF TWRQTYARCR RLASALLSLG
VVRRGDVVSV LAPNVPAMYE MHFAVPMAGA VLNTINTRLD AAAVATILRH SGAKLFFVDY
DYVRLASDAL RLLDAADVPL VAVIDDIHSP TGARLGELEY EALLAHGDPD ADLPPLQDEW
DAVTLSYTSG TTSAPKGVVY SHRGAYLSTT SLLLQWGVPA EPVYLWTLPM FHCNGWTFTW
GMAARGGVNV CIRDARPADI YRAIARHRVT HMCCAPVVFS ILLDGDGDSD GAARQLQAPV
HVLTGGAPPP AALLERVERI GFNVTHAYGL TEATGPALAC EWRDQWDRLP LPERARLKAR
QGVSVLSLAD ADVKNADTML SVPRDGRTVG EIVLRGSSVM KGYLNNPEAN ESAFRAGWFL
TGDVGVVHPD GYIEIKDRSK DVIISGGENI CSKELEEVLF RHPAVADAAV VAMPHPRWGE
TPCAFVVPRD KAAVLSEGDV LAFCSKRMAR FMVPKKVEVV GALPRNALGK VEKVKLREAA
RKLAPTVAAA QKPKAKTTTV GGRRDGQPVA HVMAVSRL
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