ACH1_ARATH
ID ACH1_ARATH Reviewed; 425 AA.
AC Q5FYU1; F4JHC9; O65260; O65261;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acyl-CoA hydrolase 1 {ECO:0000303|PubMed:11171266};
DE Short=AtACH1 {ECO:0000303|PubMed:11171266};
DE EC=3.1.2.20 {ECO:0000250|UniProtKB:F4HU51};
DE AltName: Full=Acyl-coA thioesterase I {ECO:0000303|PubMed:11171266, ECO:0000303|PubMed:15644130};
DE Short=ACT-I {ECO:0000303|PubMed:23505340};
DE AltName: Full=Protein CYCLIC NUCLEOTIDE REGULATED THIOESTERASE 1 {ECO:0000303|PubMed:15644130};
DE Short=AtCNTE1 {ECO:0000303|PubMed:15644130};
GN Name=CNTE1 {ECO:0000303|PubMed:15644130};
GN Synonyms=ACH1 {ECO:0000303|PubMed:11171266};
GN OrderedLocusNames=At4g00520 {ECO:0000312|Araport:AT4G00520};
GN ORFNames=F6N23.2 {ECO:0000312|EMBL:AAC13612.1},
GN F6N23.3 {ECO:0000312|EMBL:AAC13635.1};
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].
RX PubMed=15644130; DOI=10.1186/1471-2105-6-6;
RA Bridges D., Fraser M.E., Moorhead G.B.G.;
RT "Cyclic nucleotide binding proteins in the Arabidopsis thaliana and Oryza
RT sativa genomes.";
RL BMC Bioinformatics 6:6-6(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
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 (By similarity). Active with both medium chain and long chain
CC acyl-CoAs as substrates (By similarity).
CC {ECO:0000250|UniProtKB:F4HU51}.
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:0000250|UniProtKB:F4HU51};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:F4HU51}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:F4HU51}.
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 -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC13635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE81892.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80860.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80861.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY874170; AAW69868.1; -; mRNA.
DR EMBL; AF058919; AAC13612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF058919; AAC13635.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80860.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80861.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81892.2; ALT_INIT; Genomic_DNA.
DR EMBL; AK228258; BAF00206.1; -; mRNA.
DR PIR; T01215; T01215.
DR PIR; T01216; T01216.
DR RefSeq; NP_001078340.2; NM_001084871.2.
DR SMR; Q5FYU1; -.
DR STRING; 3702.AT4G00520.2; -.
DR PaxDb; Q5FYU1; -.
DR ProteomicsDB; 203665; -.
DR EnsemblPlants; AT4G00520.2; AT4G00520.2; AT4G00520.
DR GeneID; 827955; -.
DR Gramene; AT4G00520.2; AT4G00520.2; AT4G00520.
DR KEGG; ath:AT4G00520; -.
DR Araport; AT4G00520; -.
DR TAIR; locus:2127078; AT4G00520.
DR eggNOG; KOG3016; Eukaryota.
DR HOGENOM; CLU_032690_5_0_1; -.
DR InParanoid; Q5FYU1; -.
DR OrthoDB; 826588at2759; -.
DR PhylomeDB; Q5FYU1; -.
DR BioCyc; ARA:AT4G00520-MON; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5FYU1; baseline and differential.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051289; P:protein homotetramerization; ISS: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 2: Evidence at transcript level;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Peroxisome;
KW Reference proteome.
FT CHAIN 1..425
FT /note="Acyl-CoA hydrolase 1"
FT /id="PRO_0000454764"
FT MOTIF 423..425
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 335
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 357
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 407
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"
SQ SEQUENCE 425 AA; 48091 MW; E8AFF3C6FF7C7288 CRC64;
MNTESVVEFL GNVTLLQRLP SSSLKRISEV VVFKGYDRGD YVVRENQNVD GVYFLLQGQA
QVLRSAGEEN YQEFPLKRYD FFGHGIFGDV YSADVVAVTE LTCLLLMSDH RALLEIKSVS
DSDKERCLVE DILYLEPLDL NVYRGFTPPN APTYGKVYGG QLVGQALAAA SKTVETMKIV
HNFHCYFLLV GDINIPIIYD VNRLRDGNNF ATRSVDARQK GKTIFTLFAS FQKKQQGFIH
QESTMPHTPA PETLLPREEM LERLVTEPLL PRDYRNQVAT EISVPFPIDI RFCEPNRSTK
QNKSPPRLKY WFRAKGKLSD DDQALHRCVV AFASDLIFAT ISLNPHRREG MSVAALSLDH
SMWFHRPVRA DDWLLFVIVS PTATESRGFA TGKMFNRKGE LVVSLTQEAV LREAVTIKPS
FGAKL
