ID B8AND5_ORYSI Unreviewed; 587 AA.
AC B8AND5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN ORFNames=OsI_10054 {ECO:0000313|EMBL:EEC74534.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC74534.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC74534.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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; CM000128; EEC74534.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AND5; -.
DR STRING; 39946.B8AND5; -.
DR EnsemblPlants; BGIOSGA011432-TA; BGIOSGA011432-PA; BGIOSGA011432.
DR Gramene; BGIOSGA011432-TA; BGIOSGA011432-PA; BGIOSGA011432.
DR HOGENOM; CLU_000022_59_2_1; -.
DR OMA; AVWSGDT; -.
DR Proteomes; UP000007015; Chromosome 3.
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; cd05904; 4CL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
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; PTHR24096:SF423; 4-COUMARATE--COA LIGASE-LIKE 7; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007015}.
FT DOMAIN 40..345
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 380..447
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 497..572
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 587 AA; 63042 MW; 447BEA529A42ABA1 CRC64;
MASASVPAAG YGADGVYRSL RPPAPVASDP GLSLTDLLLR RADACPSALA LADAAAGGRA
LTFAELRSAV LSTAVALSSR AGVRPGDAVL LLAPNCVLYP VCFFAVTALG AVGTTVNPDY
TPREIAKQVS DARAKLVITI SALVPKIAGL RLPVILLDDD ANAAAASLPP DATVTLYTNL
VAGVKEADYS RPPIKQSDTA ALLYSSGTTG DSKGVILTHR NFIAAARMVT SDQDERREGP
NVFLCFLPMF HIFGLSVITY AQLHRGNAII AMSRFDINSL MEAVQRHRVT HLFCVPPVII
ALAKHGKAGK YDLSSLKFIG SGAAPLGKDV MEVVAKKFPD SEIVQWALNW FIRKLVLSDL
FGSIWYIPTV LDSRGVQAFL GYGMTETCGI MSLEYPEKGQ AREFGSTGTL VSGVEAKIVD
IKTLKHLPPN QVGEICVRGP NVMQGYFNNV QATEFTIKQG WLHTGDLGYF DGGGQLFVVD
RLKELIKYKG FQIAPAELEG LLLSHPEILD AVVIPFPDAK AGEVPIAYVV RSPDSSLTEV
DVQKFIEKQV AYYKRLKRVT FVGSVPKSAS GKILRRQLIA QVRSSKL
//
