ID R0I6R3_9BRAS Unreviewed; 317 AA.
AC R0I6R3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=CARUB_v10015374mg {ECO:0000313|EMBL:EOA32123.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA32123.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(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}.
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DR EMBL; KB870807; EOA32123.1; -; Genomic_DNA.
DR RefSeq; XP_006299225.1; XM_006299163.1.
DR AlphaFoldDB; R0I6R3; -.
DR STRING; 81985.R0I6R3; -.
DR GeneID; 17892595; -.
DR KEGG; crb:17892595; -.
DR eggNOG; ENOG502RA2Q; Eukaryota.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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 PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF219; PECTINESTERASE 1-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 4: Predicted;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 13..305
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 317 AA; 35162 MW; 064377109A8DA0AF CRC64;
MSRTLANCDL KPDITVANDG SGDFVKITEA ISSIAEKTTP VVIYVKAGIY YENVIVSRDQ
VTMYGDGKQR TIVSGNLNRL DHPDYTTYQT ATFSVTGNEF IVKDMGFVNV AGPTKHQVVA
FHTRSTHSVM FRCAFNGYQD TLYAHEGKQL YRECDIVGTV DFIFGEASAV FEMCRIMPRK
PLSGQYITIT AQNANDNKAR TGFSIIKSRI FPFDENLTAA VYLGRPWGSH ATVAIMESEL
GPCIDPRGWV AWNRSLDPPP PTVSLGEYRN YGPGSTVSKR VKWVGYTPAM TDEEAEACSI
QALINQEGWL NNTCIPY
//
