PGLRB_ASPFU
ID PGLRB_ASPFU Reviewed; 364 AA.
AC Q4WBE1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable endopolygalacturonase B;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase B;
DE AltName: Full=Polygalacturonase B;
DE Flags: Precursor;
GN Name=pgaB; Synonyms=pecB; ORFNames=AFUA_8G01970;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000014; EAL84971.1; -; Genomic_DNA.
DR RefSeq; XP_747009.1; XM_741916.1.
DR AlphaFoldDB; Q4WBE1; -.
DR SMR; Q4WBE1; -.
DR STRING; 746128.CADAFUBP00008239; -.
DR EnsemblFungi; EAL84971; EAL84971; AFUA_8G01970.
DR GeneID; 3504571; -.
DR KEGG; afm:AFUA_8G01970; -.
DR VEuPathDB; FungiDB:Afu8g01970; -.
DR eggNOG; ENOG502QTAW; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; Q4WBE1; -.
DR OMA; GSTIKFM; -.
DR OrthoDB; 601945at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
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; 6.
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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..29
FT /evidence="ECO:0000255"
FT /id="PRO_0000393648"
FT CHAIN 30..364
FT /note="Probable endopolygalacturonase B"
FT /id="PRO_0000393649"
FT REPEAT 159..188
FT /note="PbH1 1"
FT REPEAT 189..210
FT /note="PbH1 2"
FT REPEAT 211..231
FT /note="PbH1 3"
FT REPEAT 240..261
FT /note="PbH1 4"
FT REPEAT 269..291
FT /note="PbH1 5"
FT REPEAT 303..324
FT /note="PbH1 6"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..47
FT /evidence="ECO:0000250"
FT DISULFID 205..221
FT /evidence="ECO:0000250"
FT DISULFID 331..336
FT /evidence="ECO:0000250"
FT DISULFID 355..364
FT /evidence="ECO:0000250"
SQ SEQUENCE 364 AA; 37691 MW; 05635DA690820FBE CRC64;
MHFFQSSLVA ATMGAALVAA APAADLETRG SCTFTSTSAL KSGKASCSTI TLQNIAVPAG
ETLDLTGLKT GTTVVFDGTT TFGYKEWEGP LISASGTSIT IKQNPGAKID CDGARWWDGK
GGNGGKKKPK FFSAHKLNKS NITGLKVYNT PVHGFSIQSD HLTIKDVLLD NSAGTKLGHN
TDAFDVGSST YITIDGATVY NQDDCLAVNS GEHITFTNGY CNGGHGLSIG SVGGRSNNVV
NDVTISNSQV INSQNGARIK TVYGATGSVT GVKFQDISLK GITKYGIVVQ QDYENGKPTG
KPTNGVKVSD ITFEKVTGTV TSSATDIYIL CGSGSCTNWT WSGNSVTGGK KSSSCKNVPA
GASC
