ID   CXE6_ARATH              Reviewed;         336 AA.
AC   Q9SX25;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Probable carboxylesterase 6;
DE   AltName: Full=AtCXE6;
DE            EC=3.1.1.1;
GN   Name=CXE6; OrderedLocusNames=At1g68620; ORFNames=F24J5.14;
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   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14738307; DOI=10.1007/s00239-003-2492-8;
RA   Marshall S.D., Putterill J.J., Plummer K.M., Newcomb R.D.;
RT   "The carboxylesterase gene family from Arabidopsis thaliana.";
RL   J. Mol. Evol. 57:487-500(2003).
CC   -!- FUNCTION: Carboxylesterase acting on esters with varying acyl chain
CC       length. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC       {ECO:0000269|PubMed:14738307}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AC008075; AAD49980.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34820.1; -; Genomic_DNA.
DR   EMBL; AF370151; AAK43966.1; -; mRNA.
DR   EMBL; AY037242; AAK59842.1; -; mRNA.
DR   EMBL; AY059093; AAL15199.1; -; mRNA.
DR   PIR; F96710; F96710.
DR   RefSeq; NP_564936.1; NM_105534.4.
DR   AlphaFoldDB; Q9SX25; -.
DR   SMR; Q9SX25; -.
DR   STRING; 3702.AT1G68620.1; -.
DR   ESTHER; arath-CXE6; Plant_carboxylesterase.
DR   MEROPS; S09.A15; -.
DR   PaxDb; Q9SX25; -.
DR   PRIDE; Q9SX25; -.
DR   ProteomicsDB; 220327; -.
DR   EnsemblPlants; AT1G68620.1; AT1G68620.1; AT1G68620.
DR   GeneID; 843192; -.
DR   Gramene; AT1G68620.1; AT1G68620.1; AT1G68620.
DR   KEGG; ath:AT1G68620; -.
DR   Araport; AT1G68620; -.
DR   TAIR; locus:2026920; AT1G68620.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_012494_22_0_1; -.
DR   InParanoid; Q9SX25; -.
DR   OMA; NANCVIM; -.
DR   OrthoDB; 1263520at2759; -.
DR   PhylomeDB; Q9SX25; -.
DR   BioCyc; ARA:AT1G68620-MON; -.
DR   PRO; PR:Q9SX25; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SX25; baseline and differential.
DR   Genevisible; Q9SX25; AT.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN           1..336
FT                   /note="Probable carboxylesterase 6"
FT                   /id="PRO_0000402552"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           96..98
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
SQ   SEQUENCE   336 AA;  37150 MW;  4F32CBE2369DF181 CRC64;
     MGGTKLTHVT TTNPNNSNIH GPVVDEVEGL IKVYKDGHVE RSQLLPCVDP SLPLELGVTC
     SDVVIDKLTN VWARLYVPMT TTKSSVSKLP LIVYFHGGGF CVGSASWLCY HEFLARLSAR
     SRCLVMSVNY RLAPENPLPA AYEDGVNAIL WLNKARNDNL WAKQCDFGRI FLAGDSAGGN
     IAQQVAARLA SPEDLALKIE GTILIQPFYS GEERTESERR VGNDKTAVLT LASSDAWWRM
     SLPRGANREH PYCKPVKMII KSSTVTRTLV CVAEMDLLMD SNMEMCDGNE DVIKRVLHKG
     VGHAFHILGK SQLAHTTTLE MLCQIDAFIH HYDPLN