TE4_HUMLU
ID TE4_HUMLU Reviewed; 527 AA.
AC S4TF94;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Acyl-coenzyme A thioesterase 4, mitochondrial {ECO:0000303|PubMed:23300257};
DE Short=Acyl-CoA thioesterase 4 {ECO:0000303|PubMed:23300257};
DE Short=HlTE4 {ECO:0000303|PubMed:23300257};
DE EC=3.1.2.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=2-methylbutanoyl-CoA hydrolase TE4 {ECO:0000305|PubMed:23300257};
DE EC=3.1.2.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=2-methylpropanoyl-CoA hydrolase TE4 {ECO:0000305|PubMed:23300257};
DE EC=3.1.2.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=3-methylbutanoyl-CoA hydrolase TE4 {ECO:0000305|PubMed:23300257};
DE EC=3.1.2.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Acyl-CoA thioester hydrolase 4 {ECO:0000303|PubMed:23300257};
DE AltName: Full=Butanoyl-CoA hydrolase TE4 {ECO:0000305|PubMed:23300257};
DE EC=3.1.2.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Propanoyl-CoA hydrolase TE4 {ECO:0000305|PubMed:23300257};
DE EC=3.1.2.- {ECO:0000269|PubMed:23300257};
DE Flags: Precursor;
GN Name=TE4 {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], FUNCTION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP 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 -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC (CoASH), providing the potential to regulate intracellular levels of
CC acyl-CoAs, free fatty acids and CoASH (PubMed:23300257). Active on acyl
CC CoAs with short chains (propanoyl-CoA and butanoyl-CoA), branched short
CC chains (2-methylpropanoyl-CoA, 2-methylbutanoyl-CoA and 3-
CC methylbutanoyl-CoA) and medium chains (octanoyl-CoA) (PubMed:23300257).
CC {ECO:0000269|PubMed:23300257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA + H(+);
CC Xref=Rhea:RHEA:40799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:48944, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40800;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate;
CC Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
CC Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+);
CC Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA + H2O = CoA + H(+) + isovalerate;
CC Xref=Rhea:RHEA:66984, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:48942, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66985;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutanoyl-CoA + H2O = 2-methylbutanoate + CoA + H(+);
CC Xref=Rhea:RHEA:66980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:48946, ChEBI:CHEBI:57287, ChEBI:CHEBI:57336;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66981;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=979 uM for 2-methylpropanoyl-CoA {ECO:0000269|PubMed:23300257};
CC KM=513 uM for 3-methylbutanoyl-CoA {ECO:0000269|PubMed:23300257};
CC Note=kcat is 135 min(-1) with 2-methylpropanoyl-CoA as substrate
CC (PubMed:23300257). kcat is 120.6 min(-1) with 3-methylbutanoyl-CoA as
CC substrate (PubMed:23300257). {ECO:0000269|PubMed:23300257};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23300257}.
CC -!- TISSUE SPECIFICITY: Mostly expressed at low levels in glandular
CC trichomes (lupulin glands), and, to a lower extent, in stems, leaves,
CC flowers and cones. {ECO:0000269|PubMed:23300257}.
CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC {ECO:0000305}.
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DR EMBL; JX878394; AGA17934.1; -; mRNA.
DR AlphaFoldDB; S4TF94; -.
DR SMR; S4TF94; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; Repeat; Transit peptide.
FT TRANSIT 1..75
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 76..527
FT /note="Acyl-coenzyme A thioesterase 4, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000452962"
FT DOMAIN 172..294
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 370..487
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
SQ SEQUENCE 527 AA; 59414 MW; EB74F3F49F6976AE CRC64;
MMTPIGIRIR KQIPLSYHYS SIQALLSRFT PTPYNPISNS SSSTQTIPTQ FHESQCTNPI
SRPTVFLFDP PPIRFTHTKS FSTDPSSLDF PSNQPPVVST ISSHHNISQP IDAGSSIRKP
ISLWPGMFNS PVTNALWEAR SNMFEKYGEP TADPPSQSEL VTKSPAQSRT SILYNLSSDY
ALREHYRNPW NMIRIGKLLE DLDALAGTIA FKHCTNEDGM SRPLLLVTAS VDKMVLKKPI
SIDTDLSIVG AVTWVGRSSM EIQLQVLQTT HESSDPSDSV SLVANFTFVA RDSKTGKSAV
INQISPETGE EKLLWREADE RNKMRKMKRK IQKDLELEKQ YIERLNALLA EGRVFCDLPA
LADRNSILMK DTCLENSFIC QPQQRNIYGR IFGGFLMRRA VELAFSTTYS FAGVVTHFLE
VDHVDFLRPV DVGDFLRLKS CVLYTELQNP TEPLINVEVV AHVTRPELRS SEVSNKFYFT
FSVGPEAVKD GLLVRNVVPA TEEEARRVLE RMDAETPHPH SQYENEI
