ID PME61_ARATH Reviewed; 587 AA.
AC Q9FK05;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 61;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 61;
DE AltName: Full=Pectin methylesterase inhibitor 61;
DE Includes:
DE RecName: Full=Pectinesterase 61;
DE Short=PE 61;
DE EC=3.1.1.11;
DE AltName: Full=AtPMEpcrF;
DE AltName: Full=Pectin methylesterase 61;
DE Short=AtPME61;
GN Name=PME61; Synonyms=ARATH61; OrderedLocusNames=At5g53370;
GN ORFNames=K19E1.17;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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.
RX PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA Micheli F., Holliger C., Goldberg R., Richard L.;
RT "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT member of a gene family comprising at least 12 genes in Arabidopsis
RT thaliana.";
RL Gene 220:13-20(1998).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
RA Markovic O., Janecek S.;
RT "Pectin methylesterases: sequence-structural features and phylogenetic
RT relationships.";
RL Carbohydr. Res. 339:2281-2295(2004).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
RA Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
RA Guerineau F., Pelloux J.;
RT "Comprehensive expression profiling of the pectin methylesterase gene
RT family during silique development in Arabidopsis thaliana.";
RL Planta 224:782-791(2006).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, floral stems and rosettes
CC leaves. {ECO:0000269|PubMed:16622707, ECO:0000269|PubMed:9767082}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout silique development.
CC {ECO:0000269|PubMed:16622707}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB013388; BAB09799.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96345.1; -; Genomic_DNA.
DR EMBL; AF360340; AAK28637.1; -; mRNA.
DR EMBL; AY051077; AAK93754.1; -; mRNA.
DR RefSeq; NP_200149.1; NM_124716.3.
DR AlphaFoldDB; Q9FK05; -.
DR SMR; Q9FK05; -.
DR STRING; 3702.Q9FK05; -.
DR iPTMnet; Q9FK05; -.
DR PaxDb; 3702-AT5G53370-1; -.
DR ProteomicsDB; 226183; -.
DR EnsemblPlants; AT5G53370.1; AT5G53370.1; AT5G53370.
DR GeneID; 835418; -.
DR Gramene; AT5G53370.1; AT5G53370.1; AT5G53370.
DR KEGG; ath:AT5G53370; -.
DR Araport; AT5G53370; -.
DR TAIR; AT5G53370; PMEPCRF.
DR eggNOG; ENOG502QRD0; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9FK05; -.
DR OMA; LEMNTHI; -.
DR PhylomeDB; Q9FK05; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FK05; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK05; baseline and differential.
DR Genevisible; Q9FK05; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0030599; F:pectinesterase activity; ISS:TAIR.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd15798; PMEI-like_3; 1.
DR Gene3D; 1.20.140.40; Invertase/pectin methylesterase inhibitor family protein; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF400; PECTINESTERASE_PECTINESTERASE INHIBITOR 61-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall biogenesis/degradation; Disulfide bond;
KW Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..587
FT /note="Probable pectinesterase/pectinesterase inhibitor 61"
FT /id="PRO_0000371707"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..223
FT /note="Pectinesterase inhibitor 61"
FT REGION 273..571
FT /note="Pectinesterase 61"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 423
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 349
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 401
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 416..436
FT /evidence="ECO:0000250"
SQ SEQUENCE 587 AA; 64241 MW; A60B9271DE489DBD CRC64;
MGYDRLGPSG PSNPNQKDPA TSLPELQKKT KTKLILFTLA VLVVGVVCFG IFAGIRAVDS
GKTEPKLTRK PTQAISRTCS KSLYPNLCID TLLDFPGSLT ADENELIHIS FNATLQKFSK
ALYTSSTITY TQMPPRVRSA YDSCLELLDD SVDALTRALS SVVVVSGDES HSDVMTWLSS
AMTNHDTCTD GFDEIEGQGG EVKDQVIGAV KDLSEMVSNC LAIFAGKVKD LSGVPVVNNR
KLLGTEETEE LPNWLKREDR ELLGTPTSAI QADITVSKDG SGTFKTIAEA IKKAPEHSSR
RFVIYVKAGR YEEENLKVGR KKTNLMFIGD GKGKTVITGG KSIADDLTTF HTATFAATGA
GFIVRDMTFE NYAGPAKHQA VALRVGGDHA VVYRCNIIGY QDALYVHSNR QFFRECEIYG
TVDFIFGNAA VILQSCNIYA RKPMAQQKIT ITAQNRKDPN QNTGISIHAC KLLATPDLEA
SKGSYPTYLG RPWKLYSRVV YMMSDMGDHI DPRGWLEWNG PFALDSLYYG EYMNKGLGSG
IGQRVKWPGY HVITSTVEAS KFTVAQFISG SSWLPSTGVS FFSGLSQ
//
