ID R9QNQ7_GOSHI Unreviewed; 521 AA.
AC R9QNQ7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
DE Flags: Fragment;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|EMBL:AFW03481.1};
RN [1] {ECO:0000313|EMBL:AFW03481.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23755181;
RA Liu Q., Talbot M., Llewellyn D.J.;
RT "Pectin methylesterase and pectin remodelling differ in the fibre walls of
RT two gossypium species with very different fibre properties.";
RL PLoS ONE 8:E65131-E65131(2013).
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; JX003000; AFW03481.1; -; mRNA.
DR AlphaFoldDB; R9QNQ7; -.
DR UniPathway; UPA00545; UER00823.
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:SF180; 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}.
FT DOMAIN 44..206
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT NON_TER 521
FT /evidence="ECO:0000313|EMBL:AFW03481.1"
SQ SEQUENCE 521 AA; 57131 MW; 6A2169F89284280F CRC64;
MAFSGERKKK LFLALFASIL LVTAIVTIAT TVSISKKKSS NTVAAHSIIK SSCSSTLYPE
LCYSTISSAP DAETKVKNPK DVTELSLNLT VTAVQSNYLS IKKLISTQRK SLTEREKAAL
NDCLELVDET LDELFVAEHD LSDYPSFNKS ISQHADVLKS LLSAAMTNQE TCLDGFSHDK
ADKKVRQALL DGQMHVFHMC SNALAMIKNL TDTDMASQGY HPSSGRQLEE QDQTEWPKWL
SEGDRRLLQA TTVIPNVTVA ADGSGDFLTV SEAVAAAPER STTRYIIKIK AGVYRENVDV
PSKKTNLMFV GDGRVNTIIT ASRNVVDGST TFHSATVAAV GDGFLARDIT FQNTAGPSKH
QAVALRVGSD LSAFYRCGIL AYQDTLYVHS LRQFYSQCLV AGSVDFIFGN AAAVLQDCDI
HARRPNPNQR NMVTAQGRSD PNENTGIVIQ KCRIGATSDL EAVKSDFETY LGRPWKTHSR
TVIMQSVISD IIHPAGWFPW DKDFALDTLT YREYQNTGPG A
//
