ECH2_ARATH
ID ECH2_ARATH Reviewed; 309 AA.
AC Q8VYI3; Q9SGR7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Enoyl-CoA hydratase 2, peroxisomal;
DE EC=4.2.1.119;
GN Name=ECH2; OrderedLocusNames=At1g76150; ORFNames=T23E18.38, T23E18.9;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16982622; DOI=10.1074/jbc.m606383200;
RA Goepfert S., Hiltunen J.K., Poirier Y.;
RT "Identification and functional characterization of a monofunctional
RT peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of
RT even cis-unsaturated fatty acids in Arabidopsis thaliana.";
RL J. Biol. Chem. 281:35894-35903(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
CC -!- FUNCTION: Bidirectional monofunctional enoyl-CoA hydratase 2 involved
CC in the degradation of even cis-unsaturated fatty acids. Devoid of 3-
CC hydroxyacyl-CoA dehydrogenase activity. {ECO:0000269|PubMed:16982622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC Evidence={ECO:0000269|PubMed:16982622};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16982622,
CC ECO:0000269|PubMed:17951448}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16982622}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seedlings and senescing
CC leaves. {ECO:0000269|PubMed:16982622}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009978; AAF17647.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35803.1; -; Genomic_DNA.
DR EMBL; AY070763; AAL50100.1; -; mRNA.
DR EMBL; AY093712; AAM10336.1; -; mRNA.
DR RefSeq; NP_177742.2; NM_106264.3.
DR AlphaFoldDB; Q8VYI3; -.
DR SMR; Q8VYI3; -.
DR IntAct; Q8VYI3; 2.
DR STRING; 3702.AT1G76150.1; -.
DR PaxDb; Q8VYI3; -.
DR PRIDE; Q8VYI3; -.
DR ProteomicsDB; 224720; -.
DR EnsemblPlants; AT1G76150.1; AT1G76150.1; AT1G76150.
DR GeneID; 843947; -.
DR Gramene; AT1G76150.1; AT1G76150.1; AT1G76150.
DR KEGG; ath:AT1G76150; -.
DR Araport; AT1G76150; -.
DR TAIR; locus:2199767; AT1G76150.
DR eggNOG; KOG1206; Eukaryota.
DR HOGENOM; CLU_040078_0_0_1; -.
DR InParanoid; Q8VYI3; -.
DR OMA; FKHTDQE; -.
DR OrthoDB; 1120431at2759; -.
DR PhylomeDB; Q8VYI3; -.
DR BioCyc; ARA:AT1G76150-MON; -.
DR BRENDA; 4.2.1.119; 399.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q8VYI3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYI3; baseline and differential.
DR Genevisible; Q8VYI3; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0080023; F:3R-hydroxyacyl-CoA dehydratase activity; IDA:TAIR.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0033542; P:fatty acid beta-oxidation, unsaturated, even number; IMP:TAIR.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Lipid metabolism; Lyase; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..309
FT /note="Enoyl-CoA hydratase 2, peroxisomal"
FT /id="PRO_0000405429"
FT DOMAIN 183..295
FT /note="MaoC-like"
FT MOTIF 307..309
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 95..96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208..213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 309 AA; 34082 MW; FC98938543619B76 CRC64;
MATSDSEFNS DLLLAHKLPE TRYTYNERDV AIYALGIGAC GQDAVDSDEL KFVYHRNGQD
LIQVLPTFAS LFTLGSLTEG LDLPGFKYDP SLLLHGQQYI EIYRPLPSKA SLINKVSLAG
LQDKGKAAIL ELETRSYEEG SGELLCMNRT TVFLRGAGGF SNSSQPFSYK NYPSNQGLAV
KIPQRQPLTV CEERTQPSQA LLYRLSGDYN PLHSDPEFAK LAGFPRPILH GLCTLGFAIK
AIIKCVCKGD PTAVKTISGR FLTTVFPGET LITEMWLEGL RVIYQTKVKE RNKTVLAGYV
DIRGLSSSL
