PME37_ARATH
ID PME37_ARATH Reviewed; 588 AA.
AC Q5MFV6; Q9M1Q7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor VGDH2;
DE AltName: Full=VANGUARD1-like protein 2;
DE Short=VGD1-like protein 2;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor VGDH2;
DE AltName: Full=Pectin methylesterase inhibitor VGDH2;
DE Includes:
DE RecName: Full=Pectinesterase VGDH2;
DE Short=PE VGDH2;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 37;
DE Short=AtPME37;
DE AltName: Full=Pectin methylesterase VGDH2;
DE Flags: Precursor;
GN Name=VGDH2; Synonyms=ARATH37; OrderedLocusNames=At3g62170;
GN ORFNames=T17J13.130;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15659637; DOI=10.1105/tpc.104.027631;
RA Jiang L., Yang S.-L., Xie L.-F., Puah C.S., Zhang X.-Q., Yang W.-C.,
RA Sundaresan V., Ye D.;
RT "VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth
RT in the Arabidopsis style and transmitting tract.";
RL Plant Cell 17:584-596(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
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 [5]
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 [6]
RP 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: Secreted, cell wall {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds, pollen grains and pollen
CC tubes. {ECO:0000269|PubMed:15659637}.
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}.
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DR EMBL; AY830950; AAV91510.1; -; mRNA.
DR EMBL; AL138651; CAB71877.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80318.1; -; Genomic_DNA.
DR EMBL; AY093237; AAM13236.1; -; mRNA.
DR EMBL; AY084580; AAM61145.1; -; mRNA.
DR PIR; T48009; T48009.
DR RefSeq; NP_191776.1; NM_116082.3.
DR AlphaFoldDB; Q5MFV6; -.
DR SMR; Q5MFV6; -.
DR BioGRID; 10704; 1.
DR STRING; 3702.AT3G62170.1; -.
DR PaxDb; Q5MFV6; -.
DR PRIDE; Q5MFV6; -.
DR ProteomicsDB; 226277; -.
DR EnsemblPlants; AT3G62170.1; AT3G62170.1; AT3G62170.
DR GeneID; 825390; -.
DR Gramene; AT3G62170.1; AT3G62170.1; AT3G62170.
DR KEGG; ath:AT3G62170; -.
DR Araport; AT3G62170; -.
DR TAIR; locus:2098013; AT3G62170.
DR eggNOG; ENOG502QUTX; Eukaryota.
DR HOGENOM; CLU_012243_9_0_1; -.
DR InParanoid; Q5MFV6; -.
DR OMA; CEVYEYA; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q5MFV6; -.
DR BioCyc; ARA:AT3G62170-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q5MFV6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q5MFV6; baseline and differential.
DR Genevisible; Q5MFV6; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..588
FT /note="Probable pectinesterase/pectinesterase inhibitor
FT VGDH2"
FT /id="PRO_0000023478"
FT REGION 42..193
FT /note="Pectinesterase inhibitor VGDH2"
FT REGION 276..574
FT /note="Pectinesterase VGDH2"
FT ACT_SITE 406
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 427
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 353
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 405
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="Q -> L (in Ref. 1; AAV91510)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="D -> G (in Ref. 1; AAV91510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 62958 MW; BAEF057677EA7848 CRC64;
MAVGKVVVSV ASLLLVVGVA IGVITFVNKG GGANGDSNGP INSHQKAVQT ICQSTTDQGS
CAKTLDPVKS DDPSKLVKAF LMATKDAITK SSNFTASTEG GMGTNMNATS KAVLDYCKRV
LMYALEDLET IVEEMGEDLQ QSGTKLDQLK QWLTGVFNYQ TDCLDDIEEV ELKKIMGEGI
SNSKVLTSNA IDIFHSVVTA MAQMGVKVDD MKNITMGAGA GGAARRLLED NDSKGLPKWF
SGKDRKLMAK AGRGAPAGGD DGIGEGGGGG GKIKATHVVA KDGSGQFKTI SEAVMACPDK
NPGRCIIHIK AGIYNEQVRI PKKKNNIFMF GDGATQTIIT FDRSVKLSPG TTTSLSGTVQ
VESEGFMAKW IGFKNTAGPL GHQAVALRVN GDRAVIFNCR FDGYQDTLYV NNGRQFYRNI
VVSGTVDFIF GKSATVIQNS LILVRKGSPG QSNYVTADGN EKGAAMKIGI VLHNCRIIPD
KELEADKLTI KSYLGRPWKK FATTVIIGTE IGDLIKPEGW TEWQGEQNHK TAKYIEFNNR
GPGAATTQRP PWVKVAKSAA EVETYTVANW VGPANWIQEA NVPVQLGL
