CCL13_HUMLU
ID CCL13_HUMLU Reviewed; 573 AA.
AC M4IS92;
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 CCL13 {ECO:0000305|PubMed:23300257};
DE Short=HlCCL13 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN Name=CCL13 {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; JQ740215; AGA17930.1; -; mRNA.
DR AlphaFoldDB; M4IS92; -.
DR SMR; M4IS92; -.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..573
FT /note="Probable CoA ligase CCL13"
FT /id="PRO_0000452958"
FT REGION 284..352
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 353..429
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 216..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 352..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 461..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 573 AA; 63221 MW; F382ED039585DBC7 CRC64;
MDNYRRLHTP VALCVASPPA PPTTSWKSME GLVQCSANHV PLSPITFLER SSKAYRDNTS
LVYGSVRYTW AQTHHRCLKL ASALTTHFGI SPGDVVATFS YNIPEIYELH FAVPMAGGIL
CTLNARNDSA MVSTLLAHSE AKLIFVEPQL LETARAALDL LAQKDIKPPT LVLLTDSESF
TSSSYDHYNH LLANGSDDFE IRRPKNECDP ISINYTSGTT ARPKAVVYSH RGAYLNSIAT
VLLHGMGTRS VYLWSVPMFH CNGWCFPWGA AAQGATNICI RKVSPKAIFD NIHLHKVTHF
GAAPTVLNMI VNSPEGNLHT PLPHKVEVMT GGSPPPPKVI ARMEEMGFQV NHIYGLTETH
GPATNCVCKP EWDALQPEER YALKARQGLN HLAMEEMDVR DPVSMESVRA DGTTIGEVMF
RGNTVMSGYF KDLKATEEAF EGGWFRTGDL GVKHEDGYIQ LKDRKKDVVI SGGENVSTVE
VETVLYSHEA VLEAAVVARP DKLWGETPCA FVTLKEGFDN GVSADQIIKF CRDRLPHYMA
PKTVVFEELP KTSTGKIQKY ILKEKAKAMG SLS