CCL9_HUMLU
ID CCL9_HUMLU Reviewed; 525 AA.
AC M4IQQ7;
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 CCL9 {ECO:0000305|PubMed:23300257};
DE Short=HlCCL9 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN Name=CCL9 {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; JQ740211; AGA17926.1; -; mRNA.
DR AlphaFoldDB; M4IQQ7; -.
DR SMR; M4IQQ7; -.
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 CDD; cd05926; FACL_fum10p_like; 1.
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 InterPro; IPR045310; Pcs60-like.
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..525
FT /note="Probable CoA ligase CCL9"
FT /id="PRO_0000452954"
FT REGION 242..311
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 312..375
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 171..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 311..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 407..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 525 AA; 56105 MW; E7BD3190A687F1FA CRC64;
MANNITLTGL LKKAAAEFSD RRAILVSGEF HLTHARLQEI VDHAASLLLA SGVGHGDVVA
LTFPNTIEYI VMFLAVIRCR AVAAPLNSAY TAEEFEFYLS DSESKLLITP PKGIEAARAA
ASKLNITHVT ATLPGGDGLI ALSPSPNNES SLDAVAELTN DPSDVSLFLH TSGTTSRPKG
VPLTQLNLAS SVQNIKSVYK LSESDSTVVV LPLFHVHGMI AGLLSSLIAG SAVTLPAAGR
FSASTFWSDM IACNATWYTA VPTIHQIILD RHLNKPEPTY PKLRFIRSCS ASLAPTIMGR
LEESFGAPVL EAYAMTEAAH LMASNPLPED GGHKPGSVGK PVGQEMAILD LNGSAQLPGF
SGEVCIRGPN VTKGYKNNPE ANKAAFQFGW FHTGDVGYFD EDGYLHLVGR IKELINRGGE
KISPIEVDAV LLSHPDLAQA VAFGVPDDKY GEEINCAVIP REGSEVDEDG VLRFCKKNLA
AFKVPKKVFI TDSLPKTATG KIQRRIVAEH FLAQISTAKV PKFGA