ID U5G7D7_POPTR Unreviewed; 595 AA.
AC U5G7D7;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=POPTR_006G134700 {ECO:0000313|EMBL:PNT31507.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT31507.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:PNT31507.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
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 Evidence={ECO:0000256|RuleBase:RU000589};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184,
CC ECO:0000256|RuleBase:RU000589}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000256|ARBA:ARBA00007786}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000256|ARBA:ARBA00006027}.
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DR EMBL; CM009295; PNT31507.1; -; Genomic_DNA.
DR RefSeq; XP_006381543.1; XM_006381481.1.
DR AlphaFoldDB; U5G7D7; -.
DR SMR; U5G7D7; -.
DR STRING; 3694.U5G7D7; -.
DR EnsemblPlants; Potri.006G134700.1.v4.1; Potri.006G134700.1.v4.1; Potri.006G134700.v4.1.
DR GeneID; 18100264; -.
DR Gramene; Potri.006G134700.1.v4.1; Potri.006G134700.1.v4.1; Potri.006G134700.v4.1.
DR KEGG; pop:18100264; -.
DR eggNOG; ENOG502QVHM; Eukaryota.
DR HOGENOM; CLU_012243_9_0_1; -.
DR InParanoid; U5G7D7; -.
DR OMA; GPFLQGE; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000006729; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
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:SF191; PECTINESTERASE_PECTINESTERASE INHIBITOR 45-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 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..227
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT REGION 55..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 595 AA; 66341 MW; 731C8B657846E333 CRC64;
MVFQDFDQLS ERRKLERQQK LRKKIIIGSV SSIAFFVIVG AGVFALVSNH NISSPGSNGG
SPSTVSQPVE SAKPTSHVAR VIKTVCNATT YQDTCQNTLE KGMRKDPSSV QPKDLLKIAI
KAADKEIEKV LKKASSFKFD KPREKAAFDD CLELIEDAKE ELKHCIDRVG NDIGKLTKNA
PDLNNWLSAV MSYQQTCIDG FPEGKLKSDM EKTFKAAREL TSNSLAMVSS LASFLKNFSF
SGTLNRRLLA EEYNSPSLDK DGLPGWTSHE DRRILKGANQ DKPKPHVTVA KDGSGDFKTI
SEALAAMPAK YEGRYVIFVK QGIYDETVTV TKKMVNITMY GDGSQKTIVT GNKNFADGVQ
TFRTATFAVL GEGFLCKAMG FRNTAGPEKH QAVAIRVQAD RAIFLNCRFE GYQDTLYAQT
HRQFYRSCVI TGTVDFIFGD AAAIFQNCLI TVRKPLENQQ NIVTAQGRID GHETTGIVLQ
NCRIEPDKGL VPVKTKIRSY LGRPWKEFSR TVIMDSTIGD FIHPDGWLPW QGDFGLKTLY
YAEYNNKGIG AQTNARIKWR GYHIIKKEEA MKFTVETFYQ VDWISATGSP VRLGL
//
