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Database: UniProt
Entry: A0A0E0MB80_ORYPU
LinkDB: A0A0E0MB80_ORYPU
Original site: A0A0E0MB80_ORYPU 
ID   A0A0E0MB80_ORYPU        Unreviewed;       528 AA.
AC   A0A0E0MB80;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE            EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G18190.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC10G18190.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC10G18190.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   AlphaFoldDB; A0A0E0MB80; -.
DR   STRING; 4537.A0A0E0MB80; -.
DR   EnsemblPlants; OPUNC10G18190.1; OPUNC10G18190.1; OPUNC10G18190.
DR   Gramene; OPUNC10G18190.1; OPUNC10G18190.1; OPUNC10G18190.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_2_1; -.
DR   OMA; HADSVGY; -.
DR   Proteomes; UP000026962; Chromosome 10.
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; 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:SF261; 4-COUMARATE--COA LIGASE-LIKE 6; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        101..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..386
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          434..508
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   528 AA;  56360 MW;  F3DB7CE99B7BF7B6 CRC64;
     MAQTPQPQCS PTAAPPSAIP ASTPAPAAST AASTLPCPSP PTPPSPSSPT SFARLPLHLH
     HHSLLVDAAT AATLSCADLR RLVSSLAAAL RHRLHIAKGS LVLLLLPNSV TFPIAFLAVL
     ATGAVATTMN PSSAPAEIAA RLRDTAPSLV LASTHNAAKL PPLAAPLVLV PDTFQQLEAD
     DQFDLFYHAL LDPDPAGAET PEVDVGQDDA AAVLYSSGTS GRSKGVVLTH RNLIAMVELF
     VRFEASQYTR PACDNVYLAA LPMFHVYGLS LFAVGLLSLG CTVVVMRRFH VGDAVRAIRR
     YKVTHLPLVP PIMSALLRAK APLESLLQVS SGAAPLNSNL IHDFLHAFPH VDFIQGYGMT
     ESTAVGTRGF NTCNHNKYAS VGYLNDDDDA FTIKDGWLRT GDIAYFDSDG YLFIVGRLKD
     TIKYKGFQIA PADLEAVLIR HPEIVDVAVT SDEDEEAGEI PVAFVVRKSG STLSCTHVME
     YVGKQVASYK RVRKVIFVEA IPKSAAGKVL RRLLKDSLVD ASSGRSRL
//
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