ID A0A087FX23_ARAAL Unreviewed; 687 AA.
AC A0A087FX23;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=AALP_AAs39369U000100 {ECO:0000313|EMBL:KFK22175.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK22175.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin.
CC {ECO:0000256|RuleBase:RU000589}.
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL991733; KFK22175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087FX23; -.
DR EnsemblPlants; KFK22175; KFK22175; AALP_AAs39369U000100.
DR Gramene; KFK22175; KFK22175; AALP_AAs39369U000100.
DR eggNOG; ENOG502QPZF; Eukaryota.
DR OMA; KQECIAS; -.
DR OrthoDB; 657420at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000029120; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF416; PECTINESTERASE_PECTINESTERASE INHIBITOR 43-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; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Cell wall {ECO:0000256|RuleBase:RU000589};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU000589};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW Secreted {ECO:0000256|RuleBase:RU000589}.
FT DOMAIN 30..182
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT REGION 208..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 687 AA; 76710 MW; C7A838787E3C4140 CRC64;
MAMAISAVAD HGNSPSRKTI EIHRQSKLVI RKTAVNLICS STDYKSDCAA SLSSVRSPDP
RNLIRSAFDL AILAIRSGVD RGMIDLKGRA DANVRTRDAL NTCRELMDAA IDDLQKTRDQ
FRGFLFTRFS DFVEDLRVWL SGSITYQQTC IDGFEGIDSE AAAIMERVMR KGQHLTSNGL
AIASDLDNLL KAFRIPFLSA GRDRLGRIFR PDSTQEQPLD SSEIPPQQND SVENPPQQND
SVENSPTKSD SIENSPTTSD SVENSPKNSG PSENQQSDSS QIRPQEFHSN PPSDSSEDNS
KNADSSVIRP LNPLRKDSSE ISPPESSDQP SDSSEDNPRN ADSSVIRPLD PLRALNPLAK
LNPLRKIKDR HLSEEFPPWL GSHSRRLLQA RGRGRRGNNI RANAVVSKDG SGRFKTIAQA
LAMVPKNNRR KFVIHIKQGV YKETVEVTKK MLNVMFVGDG PTKTIITGNI AFLPDRIGTY
RTATVAVNGD NFMAKDIGFE NTAGAARHQA VALRVSADFA VFFNCRMDGY QDTLYVHTHR
QFYRDCRISG TIDFVFGDAK AVFQNCDFVI RRPMDNQQCI VTAQGRKDRR ETTGIVIHNS
RIIGDATYRP VKAKNRAFLG RPWKEFSRTI IMNTEIDDVI DPEGQGRRVR WRGIRRISDR
DAKGFAPGNF LRGSTWIPQT RVPYNAN
//
