ID W6Z8H0_COCMI Unreviewed; 384 AA.
AC W6Z8H0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
GN ORFNames=COCMIDRAFT_30994 {ECO:0000313|EMBL:EUC39986.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC39986.1};
RN [1] {ECO:0000313|EMBL:EUC39986.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC39986.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KI964213; EUC39986.1; -; Genomic_DNA.
DR RefSeq; XP_007693498.1; XM_007695308.1.
DR AlphaFoldDB; W6Z8H0; -.
DR STRING; 930090.W6Z8H0; -.
DR GeneID; 19121783; -.
DR KEGG; bor:COCMIDRAFT_30994; -.
DR eggNOG; ENOG502R6WA; Eukaryota.
DR HOGENOM; CLU_012243_2_0_1; -.
DR OrthoDB; 561027at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000054032; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..384
FT /note="pectinesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011120700"
FT DOMAIN 157..342
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
SQ SEQUENCE 384 AA; 41965 MW; A30AA44CEC637501 CRC64;
MRLAIISTGF LQLCAAIPAA NRKACQYPTE NPLDGCPQNT LLVGPRSNFS TIQSAVLSLP
HDETPYNILI LPGTYTEQVN ITRPGPVYLL GQTAHPENRT KNTVNILWHN ATGAGLSTLD
NAYTSVLTVA PTLNASLTGS GPTGFPVPPS TPFGNTDFRA YNLNFTNDYL PYSSGPSLAI
SVSYANTGFY YCAFHSYQDT LYVGKLGNAY IYASEIAGQT DFLYGFGTAW IQSSLLTLRG
CGGGITAWKG TNTTFENRYG VYIHDSELKK ENATLAIQAK CALGRPWNAL HRSVFANCDM
DDSVLPAGYI KWSAADPRVG VNTTMAEYKS HGPGWDEAAR KRSNVSIVLG EREYRDYKRV
ETVFQYPFSG EFGNTGWIDM DPGR
//
