ID Q17ST4_SALKA Unreviewed; 339 AA. AC Q17ST4; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 02-SEP-2026, entry version 61. DE RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229}; DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229}; DE Flags: Fragment; OS Salsola kali (Prickly saltwort) (Kali turgidum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Amaranthaceae; Salsoloideae; Salsoleae; Salsola. OX NCBI_TaxID=151250 {ECO:0000313|EMBL:AAX11261.1}; RN [1] {ECO:0000313|EMBL:AAX11261.1} RP NUCLEOTIDE SEQUENCE. RA Barderas R., Villalba M., Rodriguez R.; RT "Sal k 1-encoding nucleotide and deduced amino acid sequences."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D- CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}. CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. CC -!- SIMILARITY: Belongs to the pectinesterase family. CC {ECO:0000256|ARBA:ARBA00008891}. 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; AY776248; AAX11261.1; -; mRNA. DR AlphaFoldDB; Q17ST4; -. DR SMR; Q17ST4; -. DR Allergome; 3348; Sal k 1. DR Allergome; 3775; Sal k 1.0302. DR UniPathway; UPA00545; UER00823. DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC. DR GO; GO:0042545; P:cell wall modification; IEA:InterPro. DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway. DR FunFam; 2.160.20.10:FF:000008; Pectinesterase; 1. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR000070; Pectinesterase_cat. DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1. DR PANTHER; PTHR31321:SF87; PECTINESTERASE 63-RELATED; 1. DR Pfam; PF01095; Pectinesterase; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. PE 2: Evidence at transcript level; KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085}; KW Cell wall {ECO:0000256|ARBA:ARBA00022512}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 42..328 FT /note="Pectinesterase catalytic" FT /evidence="ECO:0000259|Pfam:PF01095" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAX11261.1" FT NON_TER 339 FT /evidence="ECO:0000313|EMBL:AAX11261.1" SQ SEQUENCE 339 AA; 36595 MW; A67581A655BF91B4 CRC64; QPIPPNPAEL ESWFQGAVKP VSEQKGLEPS VVQAESGGVE TIEVRQDGSG KFKTISDAVK HVKVGNTKRV IITIGPGEYR EKVKIEGLHP YITLYGIDPK NRPTITFAGT AAEFGTVDSA TLIVESDYFV GANLIVSNSA PRPAGKRKGA QASALRISGD RAAFYNCKFT GFQDTVCDDK GNHLFKDCYI EGTVDLIFGE ARSLYLNTEL HVVPGDPMAM ITAHARKNAD GVGGYSFVHC KVTGTGGTAL LGRAWFEAAR VVFSYCNLSD AVKPEGWSDN NKPAAQKTIF FGEYKNTGPG AAADKRVPYT KQLTEADAKT FTSLEYIEAA KWLPPPPKV //