CCL1_HUMLU
ID CCL1_HUMLU Reviewed; 548 AA.
AC M4ISH0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=4-coumarate--CoA ligase CCL1 {ECO:0000303|PubMed:23300257};
DE Short=HlCCL1 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.12 {ECO:0000269|PubMed:23300257};
GN Name=CCL1 {ECO:0000303|PubMed:23300257};
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Nugget;
RX PubMed=23300257; DOI=10.1093/mp/sst004;
RA Xu H., Zhang F., Liu B., Huhman D.V., Sumner L.W., Dixon R.A., Wang G.;
RT "Characterization of the formation of branched short-chain fatty acid:CoAs
RT for bitter acid biosynthesis in hop glandular trichomes.";
RL Mol. Plant 6:1301-1317(2013).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=29760092; DOI=10.1073/pnas.1802223115;
RA Ban Z., Qin H., Mitchell A.J., Liu B., Zhang F., Weng J.-K., Dixon R.A.,
RA Wang G.;
RT "Noncatalytic chalcone isomerase-fold proteins in Humulus lupulus are
RT auxiliary components in prenylated flavonoid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E5223-E5232(2018).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of prenylated phenolics natural
CC products which contribute to the bitter taste of beer and display broad
CC biological activities (Probable). Catalyzes the ligation of CoA on (E)-
CC 4-coumarate to produce (E)-4-coumaroyl-CoA (PubMed:23300257).
CC {ECO:0000269|PubMed:23300257, ECO:0000305|PubMed:30468448}.
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:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29760092}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in glandular trichomes (lupulin
CC glands) after flowering, and, to a lower extent, in stems, leaves,
CC cones and flowers. {ECO:0000269|PubMed:23300257}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively in glandular trichomes
CC (lupulin glands) after flowering. {ECO:0000269|PubMed:23300257}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; JQ740203; AGA17918.1; -; mRNA.
DR AlphaFoldDB; M4ISH0; -.
DR SMR; M4ISH0; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IDA:UniProtKB.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..548
FT /note="4-coumarate--CoA ligase CCL1"
FT /id="PRO_0000452946"
FT REGION 268..337
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 338..405
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 195..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 337..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 438..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 548 AA; 60011 MW; C916B9BE039AD4A6 CRC64;
MENNKQDDHQ EEFIFRSKLP DIYIPNHLPL HSYCFENISQ FKDRPCLING ATGEIITYAD
VDLTSRKVAA GLDKLGIKQG DVIMLLLQNS PEFVYAFLAA SYIGAIITTA NPFYTPAEVA
KQAAASKTKL VITLAGYIDK VKEFTGGESG VKVMCVDAPP PESECLHFSE LTQADETEIP
AVKIHPDDVV ALPYSSGTTG LPKGVMLTHK GLVTSVAQQV DGDNPNLYFH QNDVILCVLP
LFHIYSLNSI LLCGLRVGAA ILIMQKFEIS KLLELIEKFK VTIAPFVPPI VLSVAKCPDL
HRYDLSSIRT VMSGGAPMGK ELEDAVKEKL PHAKLGQGYG MTEAGPVLSM CLAFAKEPFP
IKSGACGTVV RNAEMKIVDP DTGASLPRNQ SGEICIRGKQ IMKGYINDAE ATKGTIDEGG
WLHTGDIGFI DNDDELFIVD RLKELIKYKG FQVAPAELES MLISHPNITD AAVVPMKDEA
AGEVPVAFVV RSNGSKITEE DIKQYISKQV VFYKRINKAF FIEEIPKNPS GKILRKILRA
KLVTEQAI
