PGLRA_ASPFU
ID PGLRA_ASPFU Reviewed; 368 AA.
AC Q4WQT2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=AFUA_4G13920;
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; AAHF01000005; EAL89402.1; -; Genomic_DNA.
DR RefSeq; XP_751440.1; XM_746347.1.
DR AlphaFoldDB; Q4WQT2; -.
DR SMR; Q4WQT2; -.
DR STRING; 746128.CADAFUBP00006900; -.
DR EnsemblFungi; EAL89402; EAL89402; AFUA_4G13920.
DR GeneID; 3509371; -.
DR KEGG; afm:AFUA_4G13920; -.
DR VEuPathDB; FungiDB:Afu4g13920; -.
DR eggNOG; ENOG502QST2; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; Q4WQT2; -.
DR OMA; EGSRWWD; -.
DR OrthoDB; 601945at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
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_0000393637"
FT CHAIN 32..368
FT /note="Probable endopolygalacturonase A"
FT /id="PRO_0000393638"
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; 38110 MW; C0C05DA680961511 CRC64;
MRSVKLFGLA ALGSLGAAAP APSRVSDLTK RSSTCTFTAA SQATESASGC SEIVLDNIEV
PAGETLDLSD VDDGTTIVFE GTTTFGYKEW SGPLIRFGGK DITIKQNSGA VIDGEGSRWW
DGEGTNGGKT KPKFMYAHSL EDSTITGLSI KNTPVQAISV QATNLYLIDI TIDNSDGDDN
GGHNTDGFDI SESTGVYIRG ATVKNQDDCI AINSGENIEF SGGTCSGGHG LSIGSVGGRD
DNTVKNVTIT DSTVTDSANG VRIKTVYDAT GSVSQVTYSN IKLSGITDYG IVIEQDYENG
SPTGTPTTGV PITDLTIDGV TGTVESDAVE VYILCGDGSC SDWTWEGVDI TGGEKSSKCE
NVPSGASC
