PGLR_ASPFU
ID PGLR_ASPFU Reviewed; 378 AA.
AC Q4WR80;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Probable endopolygalacturonase AFUA_1G17220;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase AFUA_1G17220;
DE AltName: Full=Polygalacturonase AFUA_1G17220;
DE Flags: Precursor;
GN ORFNames=AFUA_1G17220;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AAHF01000004; EAL91052.1; -; Genomic_DNA.
DR RefSeq; XP_753090.1; XM_747997.1.
DR AlphaFoldDB; Q4WR80; -.
DR SMR; Q4WR80; -.
DR STRING; 746128.CADAFUBP00001629; -.
DR EnsemblFungi; EAL91052; EAL91052; AFUA_1G17220.
DR GeneID; 3510122; -.
DR KEGG; afm:AFUA_1G17220; -.
DR VEuPathDB; FungiDB:Afu1g17220; -.
DR eggNOG; ENOG502SHAF; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; Q4WR80; -.
DR OMA; GYCHGGH; -.
DR OrthoDB; 601945at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004650; F:polygalacturonase activity; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..35
FT /evidence="ECO:0000255"
FT /id="PRO_0000393692"
FT CHAIN 36..378
FT /note="Probable endopolygalacturonase AFUA_1G17220"
FT /id="PRO_0000393693"
FT REPEAT 147..169
FT /note="PbH1 1"
FT REPEAT 170..200
FT /note="PbH1 2"
FT REPEAT 201..222
FT /note="PbH1 3"
FT REPEAT 252..273
FT /note="PbH1 4"
FT REPEAT 281..303
FT /note="PbH1 5"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..56
FT /evidence="ECO:0000250"
FT DISULFID 217..233
FT /evidence="ECO:0000250"
FT DISULFID 345..350
FT /evidence="ECO:0000250"
FT DISULFID 369..378
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 38425 MW; BD35BEE28B707357 CRC64;
MLKLMGSLVL LASAAEVIAS PAAEPVAPST TLEKRAPCTF SGSNGAAAAM ASQKACSTIV
LSNVAVPAGT TLDLSDLADG TTVTFEGETT WGYQEWSGPL LKISGKNIKV KGASGATLNP
DGARWWDGQG GNGGKTKPKF FAAHDLTSSS SITDLHILNT PVQAVSINGC DGLTITDITI
DNSAGDTQGG HNTDAFDIGS SSNIIISGAK VYNQDDCVAV NSGTDITFTG GLCSGGHGLS
IGSVGGRSDN TVENVSFTNS QVTNSDNGLR IKATKGKTGT IKGVTYSGIT LSSIRKYGIL
IEQNYDGGDL KGDPTSGIPI TDLTMQNISG KGAVASSGYN IAIVCGSGAC SNWTWKSVEV
TGGKTYGSCK NVPSVAQC
