ID   PGLR_NEOFI              Reviewed;         378 AA.
AC   A1D145;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable endopolygalacturonase NFIA_008150;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase NFIA_008150;
DE   AltName: Full=Polygalacturonase NFIA_008150;
DE   Flags: Precursor;
GN   ORFNames=NFIA_008150;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22138.1; -; Genomic_DNA.
DR   RefSeq; XP_001264035.1; XM_001264034.1.
DR   AlphaFoldDB; A1D145; -.
DR   SMR; A1D145; -.
DR   STRING; 36630.CADNFIAP00001136; -.
DR   EnsemblFungi; EAW22138; EAW22138; NFIA_008150.
DR   GeneID; 4591406; -.
DR   KEGG; nfi:NFIA_008150; -.
DR   VEuPathDB; FungiDB:NFIA_008150; -.
DR   eggNOG; ENOG502SHAF; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; GYCHGGH; -.
DR   OrthoDB; 601945at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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_0000393696"
FT   CHAIN           36..378
FT                   /note="Probable endopolygalacturonase NFIA_008150"
FT                   /id="PRO_0000393697"
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          247..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   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;  38359 MW;  21428D2F33725455 CRC64;
     MLKLIGSLVL LASAAEVIAS PLAESVAPSI TLEKRASCTF SGSNGAAAAM ASQKACSTIV
     LSNVAVPAGT TLDLSDLADG TTVIFEGETT WGYKEWSGPL LQISGKNIKV EGASGATLNP
     DGARWWDGQG GNGGKTKPKF FAAHGLTSSS SITNLHILNT PVQAVSINGC DGLTVTDMTI
     DDSAGDTQGG HNTDAFDIGS SSNIIISGAK VYNQDDCVAV NSGTGITFTG GLCSGGHGLS
     IGSVGGRSDN TVENVSFTNS QVTKSDNGLR IKASKGKTGT IKGITYSGIT LSSIRKYGIL
     IEQNYDGGDL KGDPTSGIPI TDLTMENISG KGAVASSGHN IAIVCGSGAC SNWTWKNVEV
     TGGQTYGSCE NVPSVAQC