ID V7D0F0_PHAVU Unreviewed; 562 AA.
AC V7D0F0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=PHAVU_001G209300g {ECO:0000313|EMBL:ESW35128.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW35128.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002288; ESW35128.1; -; Genomic_DNA.
DR RefSeq; XP_007163134.1; XM_007163072.1.
DR AlphaFoldDB; V7D0F0; -.
DR STRING; 3885.V7D0F0; -.
DR EnsemblPlants; ESW35128; ESW35128; PHAVU_001G209300g.
DR GeneID; 18642074; -.
DR Gramene; ESW35128; ESW35128; PHAVU_001G209300g.
DR KEGG; pvu:PHAVU_001G209300g; -.
DR eggNOG; ENOG502QUB9; Eukaryota.
DR OMA; ILTNHQT; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000000226; Chromosome 1.
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 NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF437; 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 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 27..562
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005149124"
FT DOMAIN 31..184
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 562 AA; 61794 MW; 48800CEEEA084159 CRC64;
MAFKNLSLVT LCVSLVLSFL SPISIASNSK RDVVPPETIC KSTIDPSYCK SVLANQNGTI
FDYGRISVRK SLSQSRKFLN LVNSFLKDRS SLSLPTIRAL EDCQFLADQT FEYLSNALDN
VDKASGDLPT TQAEDQQTML SAALTNQETC LDGLQTTASD QRVKSGLFSS LSNDTKLHSV
SLDLFTKGWV PEKKISTSWQ PNGRHLGFRN GRLPLKMSDR VRGIYDSARG HGRKLLDDSS
DSVLVNDIVV VSQDGSGNFT TINDAVAAAP NNTAAADGYF LIFITAGVYQ EYVSIIKNKR
YLMMIGDGIN QTIITGDHNV VDNFTTFNSA TFAVVAPWFV AVDITFRNTA GPSKHQAVAL
RSGADNSTFY SCSFEGYQDT LYTHSLRQFY RECDIYGTVD FIFGNAAVVF QTCNMYPRLP
MSGQFNAITA QGRTDPNQNT GTSIQNSTIK AAADLAPVVG TVKTYLGRPW KEYSRTVYMQ
SFMDSLINPA GWHEWSGDFA LNTSYYAEYN NTGPGSSTEN RVTWSGYHVI NATDAVNFTV
SNFLEGDDWL PQTGVPYSSG LI
//
