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Database: UniProt
Entry: B6SV29_MAIZE
LinkDB: B6SV29_MAIZE
Original site: B6SV29_MAIZE 
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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