ID A0A0D3AUY9_BRAOL Unreviewed; 363 AA.
AC A0A0D3AUY9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pectinesterase {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
GN Name=106324991 {ECO:0000313|EnsemblPlants:Bo2g132400.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo2g132400.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo2g132400.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo2g132400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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|ARBA:ARBA00001440,
CC 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: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR RefSeq; XP_013618456.1; XM_013763002.1.
DR AlphaFoldDB; A0A0D3AUY9; -.
DR STRING; 109376.A0A0D3AUY9; -.
DR EnsemblPlants; Bo2g132400.1; Bo2g132400.1; Bo2g132400.
DR GeneID; 106324991; -.
DR Gramene; Bo2g132400.1; Bo2g132400.1; Bo2g132400.
DR KEGG; boe:106324991; -.
DR eggNOG; ENOG502QUGG; Eukaryota.
DR HOGENOM; CLU_012243_3_0_1; -.
DR OMA; NEGRQIY; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000032141; Chromosome C2.
DR ExpressionAtlas; A0A0D3AUY9; baseline.
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; 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; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF19; PECTINESTERASE 68-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 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:UP000032141};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..354
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 363 AA; 40223 MW; AD7FBBCA39C14F32 CRC64;
MAPQLRSLTC SLSYLLSVSL LFFIFHCLCF RFSFVAACSN STEEQHHRHR KWVGPSGHKV
ITVSLNGHAQ FRSVQGAVDS IPKNNNMSIV IKIAPGYYRE KVVVPATKPY ITFKGAGRDV
TVIEWHDRAS DRGPDGQQLR TYQTASVTVY ANHFSARNIS FTNTAPAPMP GMQGWQAVAF
RISGDKAYFS GCGFYGAQDT LCDDAGRHYF KECYIEGSID FIFGNGRSMY KDCELHSIAS
RFGSIAAHGR TCPEEKTGFT FVGCRVTGTG PLYVGRAMGQ YSRIVYAYTY FDALVAHGGW
DDWDHKSNKS KTAFFGVYNC YGPGAAATTT GVSWARALDY ESAHPFIAKS FVNGRHWIAP
RDA
//
