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Database: UniProt
Entry: A0A078HMG8_BRANA
LinkDB: A0A078HMG8_BRANA
Original site: A0A078HMG8_BRANA 
ID   A0A078HMG8_BRANA        Unreviewed;       546 AA.
AC   A0A078HMG8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE            EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN   Name=BnaC03g26730D {ECO:0000313|EMBL:CDY38524.1};
GN   ORFNames=DARMORV10_C03P32290.1 {ECO:0000313|EMBL:CAF1701764.1},
GN   GSBRNA2T00066164001 {ECO:0000313|EMBL:CDY38524.1};
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:CDY38524.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY38524.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
RN   [2] {ECO:0000313|EMBL:CDY38524.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF1701764.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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; HG994367; CAF1701764.1; -; Genomic_DNA.
DR   EMBL; LK032425; CDY38524.1; -; Genomic_DNA.
DR   RefSeq; XP_013683891.1; XM_013828437.1.
DR   STRING; 3708.A0A078HMG8; -.
DR   PaxDb; 3708-A0A078HMG8; -.
DR   EnsemblPlants; CDY38524; CDY38524; GSBRNA2T00066164001.
DR   GeneID; 106388385; -.
DR   Gramene; CDY38524; CDY38524; GSBRNA2T00066164001.
DR   KEGG; bna:106388385; -.
DR   OMA; IPIYKTN; -.
DR   OrthoDB; 668039at2759; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
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:SF156; PECTINESTERASE_PECTINESTERASE INHIBITOR 12-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   Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW   Signal {ECO:0000256|RuleBase:RU000589}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT   CHAIN           23..546
FT                   /note="Pectinesterase"
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT                   /id="PRO_5041001352"
FT   DOMAIN          31..184
FT                   /note="Pectinesterase inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00856"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ   SEQUENCE   546 AA;  60278 MW;  BCA4001A17FBFFBE CRC64;
     MALSSLSFYF LCFLLFTPSI FSYSSPTSPN PNQISATSFC KNAPYPDACF HSLKLSLSIN
     ISPNILSFLL QTLKLALSEA GKLTDLLSGA GISNNLVEGQ RGSLQDCKDL HHITSSVLKR
     SLSKIKEDAN DPRKLADARA YLSAALTNKN TCLEGLDSAS GPLKPKLVIS FTTTYKHVSN
     SLSALSKQRK ANHLKTNSKT KNRRLLGLFP DWVSEKDRRF LEDSGDEYDE YEPSEILIVA
     ADGTGNFTTI NEAISFAPNM SSDRVLIYLR EGEYNENIEI PSYKTNIVLI GDGSDVTFVT
     GNRSVGDGWT TFRSATLAVS GEGFLARDIT IMNTAGPEKH QAVALRVNAD FVALYRCVID
     GYQDTLYTHS FRQFYRECDI YGTIDYIFGN AAVVFQGCNI VSKLPMPGQF TVVTAQSRDS
     PDEDTGISMQ NCSIFATEDL LNSSTRVNSY LGRPWRGYSR TVLIESFIDE FIDGSGWTKW
     AGGEGLDTLY YGEYNNNGPG SDTSKRVNWS GYHIMGYEDA FNFTTTEFIT GDGWLGSTSF
     PYDNGI
//
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