CCL11_HUMLU
ID CCL11_HUMLU Reviewed; 563 AA.
AC M4ISH2;
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=Probable CoA ligase CCL11 {ECO:0000305|PubMed:23300257};
DE Short=HlCCL11 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN Name=CCL11 {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], 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:M4IRL4}.
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; JQ740213; AGA17928.1; -; mRNA.
DR AlphaFoldDB; M4ISH2; -.
DR SMR; M4ISH2; -.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..563
FT /note="Probable CoA ligase CCL11"
FT /id="PRO_0000452956"
FT REGION 263..328
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 329..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 328..333
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 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 563 AA; 62176 MW; 85CFF342005F142C CRC64;
MEELKPRFAN SCPLTPLGFL ERAATVYGDC ISVVYDDLSY TWSQTHTRCL RVASCIESCL
GVKKGQVVSV VAPNVPAMYE LNFAVPMAGV VLNNINTRLN AVTISVMLRH SESKLVFVDQ
LSVRLVLDAV SLFPKNTPTP LLVLIADNIT GENLTVEDRE HFVCCYEDLV EKGDDKTFKW
VRPISEWDPI VLNYTSGTTS SPKGVVHSHR SVFVVTLDSL IDWGVPKQPV YLWTLPMFHA
NGWGYTWGIA AVGGTNICLR RFDGEIIFNL IRRHRVTHMC AAPIVLNMLS NSPNAEPLPN
PVHVMTGGAP PPAAVLLRTE SLGFVISHGY GMTEMLGVVV SCAWKREWNR LPATEQARLK
SRQGVRTAAM MEVDVVDPNS GVSVKRDGLT MGEIVLKGSS IMLGYLKNSA ATAKCIRADG
WFYTGDMAVM HPDGYLEIKD RSKDVIISGG ENVSSVEVES ALYSHPAVDE AAVVACPDEY
WGETPFAFVT LKKGMRVRPT EKEILEYCRE KLAHFMVPKV VVFRDKLPKT STGKIQKFTL
KEIVKTMGYS SSSSSYGVGR ARM