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Database: UniProt
Entry: I1QNJ5_ORYGL
LinkDB: I1QNJ5_ORYGL
Original site: I1QNJ5_ORYGL 
ID   I1QNJ5_ORYGL            Unreviewed;       731 AA.
AC   I1QNJ5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE            EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA09G0062400.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA09G0062400.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   AlphaFoldDB; I1QNJ5; -.
DR   STRING; 4538.I1QNJ5; -.
DR   EnsemblPlants; ORGLA09G0062400.1; ORGLA09G0062400.1; ORGLA09G0062400.
DR   Gramene; ORGLA09G0062400.1; ORGLA09G0062400.1; ORGLA09G0062400.
DR   eggNOG; KOG1175; Eukaryota.
DR   HOGENOM; CLU_000022_3_8_1; -.
DR   OMA; TGWIMYM; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        252..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          130..185
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          192..560
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   731 AA;  78745 MW;  B46FA24CD5C9F425 CRC64;
     MGHAAAAAAA AHVPLGAITV DDLLAAGVAG GAAAELHEAV RRAVGARGGD GDAAAVWGEL
     CRAALRPGVP FAVHRMLYYG CFAGFPSATP PAWTPDPEEA VLTNVGRVLE ARGREFLGDK
     YKDPIASFTD FHKFSIENPE AYWKMVFEEM GITFSVEPSC ILRENDAYPG GEWLPGAVLN
     AAANCLTAKP GRSSDDVAIV WRDEGKDSEP LNFVTLEELR KKVCLVANAL DALNLAKGSA
     IAIDMPMNVN AVVIYLAIVL AGYVVVSIAD SFAAPAISMR LKISEAKAIF TQDYILRDDK
     ELPLYSRVVE AKAPMTIVIP VRGSTPIKGM RADDLSWEDF LAKVNHAKAD NYTAVEQPAY
     AFTNILFSSG TTGEPKAIPW THLTPLKSAA DGWCHMDIRR GDVVAWPTNL GWMMGPWLVY
     ASLLNGASMA LYNGSLNSSG FAKFVQDAKV TMLGLVPSIA RSWKSTDCTA GFDWSTIRCF
     SSSGEASSVD DYLWLMGRVC YKPVIEYCGG TEIGGGFVAG SLLQPQALSA FSTPAMGCNL
     FILDNNGNPL PQDSVGTGEL ALDPTFLGAS TTLLNADHHE VYFSGMPEWN GKVLRRHGDE
     FERTPDGYYR AHGRADDTMN LGGIKVSSIE IERICNRVND AILETAAIGV PPLGGGPEQL
     TIAVVFKDQS SQTEDLNQLK LAFNTALKKL NPLFKVSSVV AVPSLPRTAS NKVMRRVLRK
     EFTQQPKHSK I
//
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