ACH2_ARATH
ID ACH2_ARATH Reviewed; 427 AA.
AC F4HU51; Q56XD4; Q8GYW7; Q9LQ87; Q9LQ88;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Acyl-CoA hydrolase 2 {ECO:0000303|PubMed:14660652};
DE Short=AtACH2 {ECO:0000303|PubMed:14660652};
DE EC=3.1.2.20 {ECO:0000269|PubMed:11171266, ECO:0000269|PubMed:14660652};
DE AltName: Full=Acyl-CoA thioesterase II {ECO:0000303|PubMed:14660652};
DE Short=ACT-II {ECO:0000303|PubMed:23505340};
DE AltName: Full=Hexadecanoyl-CoA hydrolase ACH2 {ECO:0000305|PubMed:14660652};
DE EC=3.1.2.2 {ECO:0000269|PubMed:14660652};
GN Name=ACH2 {ECO:0000303|PubMed:14660652};
GN OrderedLocusNames=At1g01710 {ECO:0000312|Araport:AT1G01710};
GN ORFNames=T1N6.10 {ECO:0000312|EMBL:AAF78401.1},
GN T1N6.9 {ECO:0000312|EMBL:AAF78421.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=14660652; DOI=10.1074/jbc.m309532200;
RA Tilton G.B., Shockey J.M., Browse J.;
RT "Biochemical and molecular characterization of ACH2, an acyl-CoA
RT thioesterase from Arabidopsis thaliana.";
RL J. Biol. Chem. 279:7487-7494(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11171266; DOI=10.1042/bst0280946;
RA Tilton G., Shockey J., Browse J.;
RT "Two families of acyl-CoA thioesterases in Arabidopsis.";
RL Biochem. Soc. Trans. 28:946-947(2000).
RN [8]
RP REVIEW.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:11171266, PubMed:14660652). Active with both medium
CC chain and long chain acyl-CoAs (e.g. 12:0-CoA, 14:0-CoA, 16:0-CoA,
CC 18:0-CoA, 16:1-CoA, 18:1-CoA, 18:2-CoA and 20:4-CoA) as substrates,
CC palmitoleoyl-CoA (16:1-CoA) being the favorite substrate
CC (PubMed:11171266, PubMed:14660652). {ECO:0000269|PubMed:11171266,
CC ECO:0000269|PubMed:14660652}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+);
CC Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20;
CC Evidence={ECO:0000269|PubMed:11171266, ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate
CC + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383; Evidence={ECO:0000269|PubMed:14660652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC Evidence={ECO:0000269|PubMed:14660652};
CC -!- ACTIVITY REGULATION: Insensitive to feedback inhibition by free
CC coenzyme A (CoASH). {ECO:0000269|PubMed:14660652}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for 18:1-CoA {ECO:0000269|PubMed:14660652};
CC KM=17.8 uM for 12:0-CoA {ECO:0000269|PubMed:14660652};
CC Vmax=13 umol/min/mg enzyme with 18:1-CoA as substrates
CC {ECO:0000269|PubMed:14660652};
CC Vmax=14.5 umol/min/mg enzyme with 12:0-CoA as substrates
CC {ECO:0000269|PubMed:14660652};
CC Vmax=21 umol/min/mg enzyme with 16:1-CoA as substrates
CC {ECO:0000269|PubMed:14660652};
CC pH dependence:
CC Optimum pH is 8.5-9.0.;
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:11171266, ECO:0000269|PubMed:14660652}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14660652}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:O14734}.
CC Note=Predominantly localized in the peroxisome but a localization to
CC the cytosol cannot be excluded. {ECO:0000250|UniProtKB:O14734}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and, to a
CC lower extent, in seedlings and siliques. {ECO:0000269|PubMed:14660652}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78401.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF78421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD93775.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY456749; AAR21571.1; -; mRNA.
DR EMBL; AC009273; AAF78401.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009273; AAF78421.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27325.1; -; Genomic_DNA.
DR EMBL; AK117346; BAC42016.1; -; mRNA.
DR EMBL; BT005354; AAO63418.1; -; mRNA.
DR EMBL; AK221741; BAD93775.1; ALT_FRAME; mRNA.
DR PIR; B86148; B86148.
DR PIR; C86148; C86148.
DR RefSeq; NP_563632.2; NM_100053.4.
DR AlphaFoldDB; F4HU51; -.
DR SMR; F4HU51; -.
DR STRING; 3702.AT1G01710.1; -.
DR PaxDb; F4HU51; -.
DR PRIDE; F4HU51; -.
DR ProteomicsDB; 195868; -.
DR EnsemblPlants; AT1G01710.1; AT1G01710.1; AT1G01710.
DR GeneID; 839254; -.
DR Gramene; AT1G01710.1; AT1G01710.1; AT1G01710.
DR KEGG; ath:AT1G01710; -.
DR Araport; AT1G01710; -.
DR TAIR; locus:2198205; AT1G01710.
DR eggNOG; KOG3016; Eukaryota.
DR HOGENOM; CLU_032690_5_0_1; -.
DR InParanoid; F4HU51; -.
DR OMA; SQVWFRT; -.
DR OrthoDB; 826588at2759; -.
DR BRENDA; 3.1.2.2; 399.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HU51; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.40.160.210; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR042171; Acyl-CoA_hotdog.
DR InterPro; IPR003703; Acyl_CoA_thio.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR11066; PTHR11066; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR TIGRFAMs; TIGR00189; tesB; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Peroxisome;
KW Reference proteome.
FT CHAIN 1..427
FT /note="Acyl-CoA hydrolase 2"
FT /id="PRO_0000454765"
FT MOTIF 425..427
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 337
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT BINDING 15..83
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT CONFLICT 4
FT /note="E -> V (in Ref. 6; BAD93775)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="L -> S (in Ref. 1; AAR21571, 4; BAC42016 and 5;
FT AAO63418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48155 MW; 5465BADD0D3033BF CRC64;
MNTESVVEFL GNVPLLQKLP SSSLKKIAQV VVPKRYGKGD YVVREDQTWD GCYFILQGEA
QVSGPDEEDN RSEFLLKQYD YFGVGLSGNV HSADIVAMSQ LTCLVLPRDH CHLLETNSIW
QSDTSLDKCS LVERILQLDP LELNIFRGIT LPDAPIFGKV FGGQFVGQAL AAASKTVDFL
KVVHSLHSYF LLVGDIDIPI IYQVHRIRDG NNFATRRVDA VQKGNIIFIL LASFQKEQQG
FEHQESTMPS VPDPDTLLSL EELRESRITD PHLPRSYRNK VATRNFVPWP IEIRFCEPSN
STNQTKSPPR LNYWFRAKGR LSDDQALHRC VVAFASDLIF CGVGLNPHRR KGVKSAALSL
DHAMWFHRPL RADEWLLYVI VSPTAHETRG FVTGQMFNRK GELVVSLTQE ALLREARPPK
PSGTSKL
