PGLRX_ASPFC
ID PGLRX_ASPFC Reviewed; 432 AA.
AC B0YDE8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Probable exopolygalacturonase X;
DE Short=ExoPG;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase;
DE Flags: Precursor;
GN Name=pgaX; ORFNames=AFUB_095310;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP47682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS499602; EDP47682.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0YDE8; -.
DR SMR; B0YDE8; -.
DR PhylomeDB; B0YDE8; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
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; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..432
FT /note="Probable exopolygalacturonase X"
FT /id="PRO_0000393666"
FT REPEAT 231..252
FT /note="PbH1 1"
FT REPEAT 254..274
FT /note="PbH1 2"
FT REPEAT 285..306
FT /note="PbH1 3"
FT REPEAT 327..348
FT /note="PbH1 4"
FT REPEAT 362..394
FT /note="PbH1 5"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 247..264
FT /evidence="ECO:0000250"
FT DISULFID 392..398
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 47311 MW; 09F95B72D6015B72 CRC64;
MKFSYSFVQV VTLLLSLSPS VEGFTRSRND ACKPNHPFRP LPPSQPRTKT CHVVSNGHGK
DDSKNIMKAL HKCNNGGKVV FDANKVYTVG TALDMTFLKH IDLEVLGKIQ FTNDTDYWQA
NSFKHGFQNA TTFFQLGGED VNVYGGGTLD GNGQVWYDLY AEDALILRPI LFGVIGLKGG
TIGPLKLRYS PQWYQLVANS SDVIFDGIDI SGYSSSKNEA KNTDGWDTYR SDNIVIQNSV
INNGDDCVSF KPNSTNILVQ NLHCNGSHGI SVGSLGQYKG EVDIVQNVLV YNISMYNASD
GARIKVWPGV SSAMSEDLQG GGGLGSVKNV TYNQMYIENV DWAIEVTQCY GQKNLTLCNE
YPSNLTISDI HFKNFRGTTS GKRDPNVGTI VCSSPNVCSD IYAENIDVKS PKGTDNFVCT
NVDKSLLDVN CA
