ID A0A061FYJ8_THECC Unreviewed; 603 AA.
AC A0A061FYJ8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=TCM_045262 {ECO:0000313|EMBL:EOY19879.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY19879.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY19879.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001888; EOY19879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FYJ8; -.
DR STRING; 3641.A0A061FYJ8; -.
DR EnsemblPlants; EOY19879; EOY19879; TCM_045262.
DR Gramene; EOY19879; EOY19879; TCM_045262.
DR eggNOG; ENOG502QVDS; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; A0A061FYJ8; -.
DR OMA; YSEFQNF; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000026915; Chromosome 10.
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:SF272; PECTINESTERASE_PECTINESTERASE INHIBITOR 46-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}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..248
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 603 AA; 66141 MW; 6ADC09969AD9B364 CRC64;
MSSTTFGHRE TALPLTNTSN GSGSHKKEKL SNMFRAYGKV NEADQARLLA RRKTRRRIAI
IGLSFIVLAA IVVAAVFGSR GSGGDSKNGG NGGVQPISSS IKAVCDVTLY KDTCYDSLAP
MANSSQLQPE DIFKLSMKVA IAELSKASQY FSKNGIFKDV ADKMSIAALE NCGELLSLAI
DHLNSSLSSS GEVSVIQAVD DLRTWLSSAS TYQQTCIDAF EELKGDTKAS VHDHLKYSSE
LTSNSLAIIT WISKVASVLN LRRLMSSSPN HEEPEWFHVK DRKLLQSSDL LKKKADIIVA
KDGSGKYKTI SAALKAVPDK SKKRIVIYVK KGVYSENVSV EKKKWNVTMI GDGMESTVVS
GSLNYVDGTP TFSTATFAVF GKGFVARDIG FVNTAGPQKH QAVALMSTAD QSVFYRCRFE
AFQDTLYAHS NRQFYRECNI IGTVDFIFGN SAVVFQNCNI LPRQPLPNQQ NTITAQGKVD
PNQNTGIAIQ NCTILPYGKL DTSLRTYLGR PWKNYSTTIL MHSSLGSVIH PTGWLPWSGT
TAPDTIFYSE YKNTGPGSST KDRVKWKGLR SITDKEAKKF TVKEFLHGDK WISDTGVSYK
SSL
//
