ID   CCL6_HUMLU              Reviewed;         658 AA.
AC   M4ISH1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Probable CoA ligase CCL6 {ECO:0000305|PubMed:23300257};
DE            Short=HlCCL6 {ECO:0000303|PubMed:23300257};
DE            EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN   Name=CCL6 {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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE
RP   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).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:M4IRL4}.
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}.
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   EMBL; JQ740208; AGA17923.1; -; mRNA.
DR   AlphaFoldDB; M4ISH1; -.
DR   SMR; M4ISH1; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016405; F:CoA-ligase activity; ISS:UniProtKB.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045311; LC-FACS_euk.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..658
FT                   /note="Probable CoA ligase CCL6"
FT                   /id="PRO_0000452951"
FT   REGION          298..411
FT                   /note="SBD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   REGION          412..477
FT                   /note="SBD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   BINDING         226..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         411..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         509..512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ   SEQUENCE   658 AA;  73911 MW;  476D002028233B77 CRC64;
     MSYTVKVEEA RPATEKMPSA GPVYRSIYAR DGLLELPEGL QSPWEFLSGS VKRSPKTPML
     GRRQIKDSEA GPYVWLTYQE VHDEAIRMAS AMRSRGVNPG DRCGIYGTNC PQWIVAMQAC
     YSHAITYVPL YDTLGPNAVE FIINHGEVSI AFVQENKISA ILSCLPNCSS LLKTIVSFGN
     ITSVQKKETE ALGVSCFSWE EFSQLGNLSG ELPEKHRTDI CTLMYTSGAT GEPKGVILTN
     EAIMAEILST DNMLELTDKV FSEEDVYFSY LPLAHVYDQI VENYCIYKGS AIGYWRGDIR
     FLMDDLQELK PTIFCGVPRV YDRIYAGIFH KVSSGGTLKK MLFQYAYNYK MANMEKGLPH
     GQAAPLMDKL FFDKIKQGFG GRIRLMFSGA APLPHHVEEY LRVTSCAALS QGYGLTESCG
     GCLTSIANIF PMIGTVGVPM TTIEARLESV PEMGYDALSD KPRGEICLRG TTLFSGYHKR
     EDLTKDVLVD GWFHTGDIGE WQPNGAMKII DRKKNIFKLS QGEYVPVENI EGIYLQCPLI
     ASIWVYGNSF ESFLVAVVVP ERLALENWAA NRNLTDDFKS LCENPKASKY ILDELNSTAK
     KHQLRGFEML KAVYLEPNPF DMERDLITPT FKLKRPQLLK YYKDHVDKLY SEAKEARV