CCL3_HUMLU
ID CCL3_HUMLU Reviewed; 568 AA.
AC M4IS88;
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=Acetate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE Short=HlCCL3 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.1 {ECO:0000269|PubMed:23300257};
DE AltName: Full=2-methylbutanoate--CoA ligase CCL4 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=2-methylpropanoate--CoA ligase CCL4 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Butanoate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Hexanoate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Isovalerate--CoA ligase CCL3 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Pentanoate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Propionate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.17 {ECO:0000269|PubMed:23300257};
GN Name=CCL3 {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 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
CC propanoate to produce propanoyl-CoA (PubMed:23300257). Can also use 2-
CC methylpropanoate (isobutyric acid), acetate, butanoate, isovalerate,
CC pentanoate, hexanoate, 2-methylbutanoate, 2-methylpentanoate, 3-
CC methylpentanoate and 4-methylpentanoate as substrates with a lower
CC efficiency (PubMed:23300257). Triggers the formation of very short
CC chain acyl-CoAs from the corresponding fatty acids, including acetic
CC acid, propanoic acid, butyric acid and its isomer (PubMed:23300257).
CC {ECO:0000269|PubMed:23300257, ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + isovalerate = 3-methylbutanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:46184, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:48942, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57345, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46185;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + pentanoate = AMP + diphosphate + pentanoyl-CoA;
CC Xref=Rhea:RHEA:46168, ChEBI:CHEBI:30616, ChEBI:CHEBI:31011,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46169;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoate + ATP + CoA = 2-methylpropanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:46176, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57338, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46177;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:46180, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:48946, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57336, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpentanoate + ATP + CoA = 2-methylpentanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:66996, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:167611,
CC ChEBI:CHEBI:167615, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66997;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylpentanoate + ATP + CoA = 3-methylpentanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:66992, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:167610,
CC ChEBI:CHEBI:167613, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66993;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylpentanoate + ATP + CoA = 4-methylpentanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:66988, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74904,
CC ChEBI:CHEBI:131445, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66989;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:M4IRL4}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in glandular trichomes (lupulin
CC glands) after flowering and in old leaves, and, to a lower extent, in
CC stems, young leaves, 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; JQ740205; AGA17920.1; -; mRNA.
DR AlphaFoldDB; M4IS88; -.
DR SMR; M4IS88; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0016405; F:CoA-ligase activity; IDA:UniProtKB.
DR GO; GO:0043759; F:methylbutanoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0050218; F:propionate-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; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..568
FT /note="Acetate--CoA ligase CCL3"
FT /id="PRO_0000452948"
FT REGION 272..340
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 341..417
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 204..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 340..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 449..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 568 AA; 62015 MW; 0938F0248D4631B2 CRC64;
MGMVGRDIDD LPKNAANYTA LTPLWFLERA ATVHPTRTSV IHGSRHYTWL QTYHRCRQFA
SALNNHSIGL GSTVAVIAPN VPALYEAHFA VPMAGAVVNC VNIRLNASTI AFLLGHSSAA
AVMVDQEFFS LAEEALKILA QESKSHYKPP LLVVIGDESC DPKTLEYALK TGAIEYEKFL
EGGDPEFDWK PPEDEWQSIS LGYTSGTTAS PKGVVLSHRG AYLMSLSASV VWGINEGAIY
LWTLPMFHCN GWCYTWGMAA FCGTNICLRQ VTAKGVYSAI AKYGVTHFCA APVVLNTIVN
APPEEAIIPL PHLVHVMTAG AAPPPSVLFA MSEKGFKVAH TYGLSETYGP STICAWKPEW
DSLPPIKQAR LNARQGVRYI ALEGLDVVDT KTMKPVPADG TTMGEIVMRG NAVMKGYLKN
PKANEESFAD GWFHSGDLAV KHPDGYIEIK DRSKDIIISG GENISSLEVE NTLYLHPAVL
EVSVVARPDE RWGESPCAFV TLKPNIDKSN EQVLAEDIIK FCKSKMPAYW VPKSVVFGPL
PKTATGKIQK HVLRAKAKEM GALKKSNL
