GenomeNet

Database: UniProt
Entry: A0A0E0IIP2_ORYNI
LinkDB: A0A0E0IIP2_ORYNI
Original site: A0A0E0IIP2_ORYNI 
ID   A0A0E0IIP2_ORYNI        Unreviewed;       731 AA.
AC   A0A0E0IIP2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE            EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA09G07520.1};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA09G07520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA09G07520.1};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA09G07520.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA09G07520.1};
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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0E0IIP2; -.
DR   STRING; 4536.A0A0E0IIP2; -.
DR   EnsemblPlants; ONIVA09G07520.1; ONIVA09G07520.1; ONIVA09G07520.
DR   Gramene; ONIVA09G07520.1; ONIVA09G07520.1; ONIVA09G07520.
DR   eggNOG; KOG1175; Eukaryota.
DR   HOGENOM; CLU_000022_3_8_1; -.
DR   OMA; TGWIMYM; -.
DR   Proteomes; UP000006591; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
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;  78755 MW;  E5203672BBA8923E 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 VRGSTPIKGL 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 VVPSLPRTAS NKVMRRVLRK
     EFTQQPKHSK I
//
DBGET integrated database retrieval system