CCL12_HUMLU
ID CCL12_HUMLU Reviewed; 723 AA.
AC M4IRL9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Probable CoA ligase CCL12 {ECO:0000305|PubMed:23300257};
DE Short=HlCCL12 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN Name=CCL12 {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; JQ740214; AGA17929.1; -; mRNA.
DR AlphaFoldDB; M4IRL9; -.
DR SMR; M4IRL9; -.
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; 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 PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..723
FT /note="Probable CoA ligase CCL12"
FT /id="PRO_0000452957"
FT REGION 429..498
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 499..558
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 360..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 498..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 603..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 723 AA; 79958 MW; 280FA28E9A207CE2 CRC64;
MCEVGVEDLV KAGLSTEEAK YFQRVLEDIV NGAKGLDPSE VWREVVARRL LKPSHPHELH
QLLYHSVYAN WDVSTRGPPL YWFPSLHQSK KTNLGRLMEK YGSEVLGPLY KDPITSFSLF
RKFSVQQPEA YWSIVLKELS VSFQEAPKCI LDSADKSKRS GSLLPGSVLN IAECCLLPTS
YPMKRDDSPA IVWRDEGYDD SEVNVLTLKE LREKVMLVAN ALDAMFSKGD AIAIDMPMTV
NAVVIYLAII LSGFVVVSIA DSFAAKEIAT RLRVSNAKAI FTQDFILRGG RKFSLYSRVV
DAAPHKAIVL PVNGSNLGLQ LREQDISWEK FISNVSNQAR SNHYTPFYQP VDSLINILFS
SGTTGEPKAI PWTQLSPLRC AADTWAHIDA QVGDVFCWPT NLGWVMGPVL LFSSFLSGAT
LALYHGSPLG HGFGKFVQDS GVTILGTVPS LVKAWKNTQC MKGLDWTKIK VFASTGEASN
VDDDLWLSSQ AYYQPIIECC GGTELASSYI QGSLVQPQAF GAFSTAAMTV GLVILDENGI
PYPDKQECTG EVGLFPLYLG ATDRLLNADN EKVYFKGMPL YNGMSLRRHG DILKRTAGGF
FIVHGRADDT MNLGGIKTSS IEIERVCNRA DESVMETTAV SVAPVSGGPE QLVMFVVLKS
GHNNEAERLK KKFSKAIQSN LNPLFKVSFV KIVEEFPRTA SNKLLRRVLR DQMKHELLVR
SKI