ID E3RXF4_PYRTT Unreviewed; 382 AA.
AC E3RXF4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
GN ORFNames=PTT_14066 {ECO:0000313|EMBL:EFQ89595.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ89595.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ89595.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; GL535631; EFQ89595.1; -; Genomic_DNA.
DR RefSeq; XP_003302309.1; XM_003302261.1.
DR AlphaFoldDB; E3RXF4; -.
DR STRING; 861557.E3RXF4; -.
DR EnsemblFungi; EFQ89595; EFQ89595; PTT_14066.
DR KEGG; pte:PTT_14066; -.
DR eggNOG; ENOG502R6WA; Eukaryota.
DR HOGENOM; CLU_012243_2_0_1; -.
DR OrthoDB; 561027at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
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 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:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..382
FT /note="pectinesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011121288"
FT DOMAIN 157..340
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
SQ SEQUENCE 382 AA; 41811 MW; CE7C3785A0C24E4A CRC64;
MRWAILTASL LQACTALSGV NRKACQYPTK KPLEGCPEDT LLVGPGQKFS TIQSAVLSLP
NNTTPHTILI LPGNYTEQVN ITRPGPVYLY GQTKYPNDRT FNTVNIIWRN ATGAGLSTLD
NAYTSTLTVA PTFNSSKTGT GPTGDPVPAD TPFGNTDFRA YNLNLINDYA PYSAGPALAI
SISYANSSFY HCGIYSYQDT VYIGKLGNAY FHENEIAGQT DFFYGFGTAW VQSSLVTLRN
CGGGITAWKG TNTTFENKYG VYIHDSTVTK ANSSLAITGK CALGRPWNAL HRSIFANCFL
DDSVRADGYI KWGTTDPRFG VNTTMSEYKN FGPGWNETAR RDGNVTLVLS EDMYKGYDGV
DKVFQYPFEG RFGNTAWIDG DL
//
