ID   Q7X9B1_FRAAN            Unreviewed;       514 AA.
AC   Q7X9B1;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE            EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN   Name=PE1 {ECO:0000313|EMBL:AAQ21124.1};
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747 {ECO:0000313|EMBL:AAQ21124.1};
RN   [1] {ECO:0000313|EMBL:AAQ21124.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Fruit receptacle {ECO:0000313|EMBL:AAQ21124.1};
RX   PubMed=15020638; DOI=10.1093/jxb/erh102;
RA   Castillejo C., de la Fuente J.I., Iannetta P., Botella M.A., Valpuesta V.;
RT   "Pectin esterase gene family in strawberry fruit: study of FaPE1, a
RT   ripening-specific isoform.";
RL   J. Exp. Bot. 55:909-918(2004).
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; AY324809; AAQ21124.1; -; mRNA.
DR   AlphaFoldDB; Q7X9B1; -.
DR   SMR; Q7X9B1; -.
DR   UniPathway; UPA00545; UER00823.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd15799; PMEI-like_4; 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   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   PANTHER; PTHR31707:SF213; PECTINESTERASE_PECTINESTERASE INHIBITOR 44-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 {ECO:0000256|ARBA:ARBA00023085,
KW   ECO:0000256|RuleBase:RU000589};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU000589, ECO:0000313|EMBL:AAQ21124.1};
KW   Signal {ECO:0000256|RuleBase:RU000589}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT   CHAIN           28..514
FT                   /note="Pectinesterase"
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT                   /id="PRO_5005144308"
FT   DOMAIN          29..164
FT                   /note="Pectinesterase inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00856"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ   SEQUENCE   514 AA;  57102 MW;  ED42822419B25F2A CRC64;
     MASDHLMWTP RFLLVLVFLS FPYYAQCGSI SNTIQSECLK VPNSEFGGSI INTINVLQQV
     VSILSDVAKG FGDFRLSNAV DDCLELMDDS TDQLSWTLSA TQNKNGKHNS TGNLSSDLRT
     WLSATLVNQD TCNEGLDGTN SIVKSLVSGS LNQITSLVLE LLGQVHPTSD QHESSNGQTP
     AWFKAEDRKL LQANGVPVDV VVAQDGTGNF TNITAAILSA PDYSLKRYVI YVKKGLYKEY
     VEIKKKKWNI MMIGDGMDAT VISGNHNFVD GWTTFRSATF AVSGRGFIAR DITFENTAGP
     EKHMAVALRS DSDLSAFYRC EFRGYQDTLY THSMRQFYRD CKISGTVDFI FGDGTVMFQN
     CQILARKALP NQKNSITAHG RKYKDEPTGF SFQFCNISAH PDLLATPVNS STPTYLGRPW
     KEYSRTIIMQ SFMSNMIKPA GWLEWNGDMF LKTLFYGEHM NYGPGAGLGS RVTWPGYQKF
     NQSGQAKNYT VAEFIEGNLW LPSTGVKYTS GFGV
//