ID Q7XAF8_BRANA Unreviewed; 562 AA.
AC Q7XAF8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:AAK84428.1};
RN [1] {ECO:0000313|EMBL:AAK84428.1}
RP NUCLEOTIDE SEQUENCE.
RX AGRICOLA=IND23244727;
RA Kang Y., Nasrallah J.B.;
RT "Use of genetically ablated stigmas for the isolation of genes expressed
RT specifically in the stigma epidermis.";
RL Sex. Plant Reprod. 14:85-94(2001).
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; AY036606; AAK84428.1; -; mRNA.
DR RefSeq; NP_001302792.1; NM_001315863.1.
DR AlphaFoldDB; Q7XAF8; -.
DR GeneID; 106395471; -.
DR KEGG; bna:106395471; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR ExpressionAtlas; Q7XAF8; differential.
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 PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF313; PECTINESTERASE; 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}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 24..562
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005144309"
FT DOMAIN 30..179
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 562 AA; 61857 MW; 2471F0DD5A202D22 CRC64;
MSQIFMFLVT LSFFSILSSP SLAAGPQATG NATSPSNVCR YAPDPSYCRS VLPNQPGDVY
SYGRFSLRRS ISRARRFISM IDYQLNRKGK VDAKSTLRAL EDCKFLASLT IDFLLSSSQT
VDATKTLSVS RADDVHTFLS AAITNEQTCL EGLKSTASEN GLSGDLYNDT KLYGVSLALF
SKGWVPKRKR SRPVWKPEAS FKKFSGFRNG RLPLKMTERT RAVYNTVTRS GRKLLQTGVD
AVQVSDIVTV NQNGTGNFTT INEAVAAAPN KTDGSNGYFL IYVTAGLYEE YVEIPKYKRY
VMMIGDGINQ TVITGNRSVV DGWTTFKSAT FILTGPNFIG VNITIRNTAG PTKGQAVALR
SGGDFSVFYS CSFEAYQDTL YTHSLRQFYR ECDVYGTVDF IFGNAAVVLQ KCNLYPRQPR
QGQANEVTAQ GRTDPNQNTG TVLHGCTIRP ADDLASSNYT VKTYLGRPWK EYSRTVVMQT
YIDGFLDPTG WNAWSGNFAL STLYYAEYNN TGPGSSTTNR VTWPGYHVIN ATDASNFTVT
NFLVGEGWIG QTGVPFVGGM IA
//
