CXE16_ARATH
ID CXE16_ARATH Reviewed; 446 AA.
AC Q8LED9; Q9LY98;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable carboxylesterase 16;
DE AltName: Full=AtCXE16;
DE EC=3.1.1.1;
GN Name=CXE16; OrderedLocusNames=At5g14310; ORFNames=F18O22.100;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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, stems, flowers and
CC siliques. {ECO:0000269|PubMed:14738307}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87770.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163817; CAB87770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92015.1; -; Genomic_DNA.
DR EMBL; BT000439; AAN17416.1; -; mRNA.
DR EMBL; BT001209; AAN65096.1; -; mRNA.
DR EMBL; AY085477; AAM62703.1; -; mRNA.
DR PIR; T48604; T48604.
DR RefSeq; NP_568298.1; NM_121435.2.
DR AlphaFoldDB; Q8LED9; -.
DR SMR; Q8LED9; -.
DR STRING; 3702.AT5G14310.1; -.
DR ESTHER; arath-At5g14310; Plant_carboxylesterase.
DR MEROPS; S09.A08; -.
DR iPTMnet; Q8LED9; -.
DR PaxDb; Q8LED9; -.
DR PRIDE; Q8LED9; -.
DR ProteomicsDB; 220434; -.
DR EnsemblPlants; AT5G14310.1; AT5G14310.1; AT5G14310.
DR GeneID; 831281; -.
DR Gramene; AT5G14310.1; AT5G14310.1; AT5G14310.
DR KEGG; ath:AT5G14310; -.
DR Araport; AT5G14310; -.
DR TAIR; locus:2145608; AT5G14310.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_14_0_1; -.
DR InParanoid; Q8LED9; -.
DR OMA; CYGGYLP; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q8LED9; -.
DR PRO; PR:Q8LED9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LED9; baseline and differential.
DR Genevisible; Q8LED9; AT.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..446
FT /note="Probable carboxylesterase 16"
FT /id="PRO_0000402560"
FT REGION 84..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 158..160
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 COMPBIAS 85..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7"
FT ACT_SITE 378
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7"
FT ACT_SITE 408
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7"
SQ SEQUENCE 446 AA; 49368 MW; 1048FDE084FB4402 CRC64;
MPGVAVKLYS VFFKLLLKHR LQNLISISAA DGLSDSFGVS TRSDESVAAA NPSFTDGVAT
KDIHIDPMTS LTVRIFLPES ALSPEPDSLR HKDNYNHQPR SDRRHSYGPN HNSPAPAERN
ESRRNSYGCN NENLEPYGGY APSAKRNSRK LPVMLQFHGG GWVSGSSDSA ANDFFCRRIA
KVCDVIVLAV GYRLAPENRY PAAFEDGVKV LHWLGKQANL ADCCKSLGNR RVNGVEVKKL
NVQGQIVDAF GASMVEPWLA AHADPSRCVL LGVSCGGNIA DYVARKAVEA GKLLEPVKVV
AQVLMYPFFI GNNPTQSEIK LANSYFYDKP VSVLAWKLFL PEKEFDFDHP AANPLAHNRS
GPPLKLMPPT LTVVAEHDWM RDRAIAYSEE LRKVNVDSPV LEYKDAVHEF ATLDMLLKTP
QAQACAEDIA IWVKKYISLR GHEFSY
