ID   PGLRA_NEOFI             Reviewed;         368 AA.
AC   A1CVV8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable endopolygalacturonase A;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase A;
DE   AltName: Full=Polygalacturonase A;
DE   Flags: Precursor;
GN   Name=pgaA; Synonyms=pecA; ORFNames=NFIA_102450;
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; DS027685; EAW24760.1; -; Genomic_DNA.
DR   RefSeq; XP_001266657.1; XM_001266656.1.
DR   AlphaFoldDB; A1CVV8; -.
DR   SMR; A1CVV8; -.
DR   STRING; 36630.CADNFIAP00009335; -.
DR   EnsemblFungi; EAW24760; EAW24760; NFIA_102450.
DR   GeneID; 4594124; -.
DR   KEGG; nfi:NFIA_102450; -.
DR   VEuPathDB; FungiDB:NFIA_102450; -.
DR   eggNOG; ENOG502QST2; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; EGSRWWD; -.
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; 7.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..31
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393642"
FT   CHAIN           32..368
FT                   /note="Probable endopolygalacturonase A"
FT                   /id="PRO_0000393643"
FT   REPEAT          140..162
FT                   /note="PbH1 1"
FT   REPEAT          167..192
FT                   /note="PbH1 2"
FT   REPEAT          193..214
FT                   /note="PbH1 3"
FT   REPEAT          215..235
FT                   /note="PbH1 4"
FT   REPEAT          244..265
FT                   /note="PbH1 5"
FT   REPEAT          273..295
FT                   /note="PbH1 6"
FT   REPEAT          307..352
FT                   /note="PbH1 7"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        209..225
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        359..368
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  38109 MW;  8D42D1E8C43D38BA CRC64;
     MRSVELLSLA ALGSLVAAAP APSRVSDLTK RSSTCTFTAA SQATESASGC SEIVLDNIEV
     PAGETLDLSD VDDGTTIVFE GTTTFGYKEW SGPLIRFGGK DITVKQNSGA VIDGEGSRWW
     DGEGTNGGKT KPKFMYAHSL EDSTITGLSI KNTPVQAISV QATNLYLIDI TIDNSDGDDN
     GGHNTDGFDI SESTGVYIRG ATVKNQDDCI AINSGENIEF SGGTCSGGHG LSIGSVGGRD
     DNTVKNVTIT DSTVTDSANG VRIKTVYDAT GSVSEVTYSN IKLSGITDYG IVIEQDYENG
     SPTGTPTTGV PITDLTIDGV TGTVESDAVE VYILCGDGSC SDWTWEGVDI TGGETSSKCE
     NVPSGASC