ID A0A094EJM5_9PEZI Unreviewed; 780 AA.
AC A0A094EJM5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=endo-polygalacturonase {ECO:0000256|ARBA:ARBA00012736};
DE EC=3.2.1.15 {ECO:0000256|ARBA:ARBA00012736};
GN ORFNames=V499_02039 {ECO:0000313|EMBL:KFY78886.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY78886.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY78886.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY78886.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC the smooth region of the plant cell wall.
CC {ECO:0000256|ARBA:ARBA00037707}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00034074};
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 glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY78886.1}.
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DR EMBL; JPKB01000296; KFY78886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EJM5; -.
DR HOGENOM; CLU_354947_0_0_1; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000029295; 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:0004650; F:polygalacturonase activity; IEA:InterPro.
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; 2.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
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 PANTHER; PTHR31884:SF9; ENDOPOLYGALACTURONASE D-RELATED; 1.
DR PANTHER; PTHR31884; POLYGALACTURONASE; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..780
FT /note="endo-polygalacturonase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011111043"
FT DOMAIN 57..318
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 360..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT ACT_SITE 641
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10052"
SQ SEQUENCE 780 AA; 82113 MW; B8FC099F5363B625 CRC64;
MFGYVYLALT TCFAISQALP GYPVSHVPSH TCSGPSARVS PEAGAVIVDN SVHPHLGSFS
TIQEGVNALN HTTTRPQNLF IFPGTYVEQV YIPRLKSNLT VQGYTCNSKG YEHNTATITY
NLALINTTND DLTATLRQWN PNTKVYNLNV VNTFGHIPKN GQNLAVSAET TGQGYYGCQL
IGYQDTLLAE TGSQLYAKSL IVGAVDFIFG QTALAWFENI DIRTIATGSI TASGRSSATN
PSWYIISRSN ITGINDTIPA GTNSLGRPWG SFARVVFQGS YLGNIIDPAG WKQWSQSTPN
IGNVTFGEYG NYGPGSVREE GPRATFSEQL NASIPIRSIL GENFQDEWWV DTTYLDPSDL
HDEGCTPEDH KAPGNTKNTK SSTATTTAST TSTHTSIPTT TLIAPSSASA ASTSETLITS
SANTLTTSAS SGTPCVCTDY SQISAAVASC TNIVLSNIAA PNGSAINLSG LKTGTTVTFD
GLTTFGFTNS STFNPITIGG QSISITANPG AIIDGNGRAY WDGLGSNGGV PKPDHFIVVN
KVTGKSVIKN LHIQNWPVHL FTISGSSDVV FQDLVLNNTA GDAPNSRSNR LAAAHNSDGF
DVSSSSNIVI QRSVVYNQDD CVAITSGNNI TVSNLECHGG HGLSIGSVGG KSNNNVTNIL
FTNSSVFDSQ NGCRIKTNYN TTGYIANVTY SNIAISDTST FGIDVQQDYL NGGATGNPSS
GVLIQNVLFQ NVTGTATDTA KDYYILCGNG SCSNFIFNNV AITGGGVASS CNYPASGCPA
//
