PME_SITOR
ID PME_SITOR Reviewed; 382 AA.
AC E7CIP7; Q5MB09;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Pectinesterase {ECO:0000305};
DE EC=3.1.1.11 {ECO:0000269|PubMed:16341253};
DE AltName: Full=Pectin methylesterase {ECO:0000303|PubMed:16341253};
DE Flags: Precursor;
GN Name=CE8-1 {ECO:0000312|EMBL:ADU33259.1};
OS Sitophilus oryzae (Rice weevil) (Curculio oryzae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Dryophthorinae; Sitophilus.
OX NCBI_TaxID=7048 {ECO:0000312|EMBL:ADU33259.1};
RN [1] {ECO:0000312|EMBL:AAW28928.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-25, CATALYTIC ACTIVITY,
RP PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=16341253; DOI=10.1093/jis/5.1.21;
RA Shen Z., Pappan K., Mutti N.S., He Q.J., Denton M., Zhang Y., Kanost M.R.,
RA Reese J.C., Reeck G.R.;
RT "Pectinmethylesterase from the rice weevil, Sitophilus oryzae: cDNA
RT isolation and sequencing, genetic origin, and expression of the recombinant
RT enzyme.";
RL J. Insect Sci. 5:21-21(2005).
RN [2] {ECO:0000312|EMBL:ADU33259.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Midgut {ECO:0000312|EMBL:ADU33259.1};
RX PubMed=21179425; DOI=10.1371/journal.pone.0015635;
RA Pauchet Y., Wilkinson P., Chauhan R., Ffrench-Constant R.H.;
RT "Diversity of beetle genes encoding novel plant cell wall degrading
RT enzymes.";
RL PLoS ONE 5:E15635-E15635(2010).
RN [3] {ECO:0007744|PDB:4PMH}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 17-382, AND DISULFIDE BOND.
RX PubMed=25372813; DOI=10.1107/s2053230x14020433;
RA Teller D.C., Behnke C.A., Pappan K., Shen Z., Reese J.C., Reeck G.R.,
RA Stenkamp R.E.;
RT "The structure of rice weevil pectin methylesterase.";
RL Acta Crystallogr. F Struct. Biol. Commun. 70:1480-1484(2014).
CC -!- FUNCTION: Pectinesterase which probably plays an important role in the
CC digestion of plant cell walls. {ECO:0000305|PubMed:16341253}.
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:0000269|PubMed:16341253};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000269|PubMed:16341253}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the midgut with particularly
CC strong expression in the ventriculus. {ECO:0000269|PubMed:16341253}.
CC -!- MISCELLANEOUS: May originate from horizontal gene transfer of a
CC bacterial enzyme to an ancentral weevil genome. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; AY841894; AAW28928.1; -; mRNA.
DR EMBL; HM175754; ADU33259.1; -; mRNA.
DR PDB; 4PMH; X-ray; 1.79 A; A=17-382.
DR PDBsum; 4PMH; -.
DR AlphaFoldDB; E7CIP7; -.
DR SMR; E7CIP7; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000504635; Unplaced.
DR GO; GO:0005615; C:extracellular space; IC:UniProtKB.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IDA:UniProtKB.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
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 Pfam; PF01095; Pectinesterase; 2.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl esterase; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000305|PubMed:16341253"
FT CHAIN 17..382
FT /note="Pectinesterase"
FT /id="PRO_0000449247"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 153..164
FT /evidence="ECO:0000269|PubMed:25372813,
FT ECO:0007744|PDB:4PMH"
FT CONFLICT 77
FT /note="T -> A (in Ref. 1; AAW28928)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..159
FT /note="CASKSGT -> WRSKSGA (in Ref. 1; AAW28928)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> G (in Ref. 1; AAW28928)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="H -> Y (in Ref. 1; AAW28928)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="A -> S (in Ref. 1; AAW28928)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="G -> A (in Ref. 1; AAW28928)"
FT /evidence="ECO:0000305"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:4PMH"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 236..254
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:4PMH"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:4PMH"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:4PMH"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:4PMH"
SQ SEQUENCE 382 AA; 40697 MW; A6E2589668BD245C CRC64;
MKIIVLLLLA VVLASADQTA PGTASRPILT ASESNYFTTA TYLQGWSPPS ISTSKADYTV
GNGYNTIQAA VNAAINTGGT TRKYIKINAG TYQEVVYIPN TKVPLTIYGG GSSPSDTLIT
LNMPAQTTPS AYKSLVGSLF NSADPAYSMY NSCASKSGTI GTSCSTVFWV KAPAVQIVNL
SIENSAKNTG DQQAVALQTN SDQIQIHNAR LLGHQDTLYA GSGSSSVERS YYTNTYIEGD
IDFVFGGGSA IFESCTFYVK ADRRSDTAVV FAPDTDPHKM YGYFVYKSTI TGDSAWSSSK
KAYLGRAWDS GVSSSSAYVP GTSPNGQLII KESTIDGIIN TSGPWTTATS GRTYSGNNAN
SRDLNNDNYN RFWEYNNSGN GA
