PGXB_ASPFC
ID PGXB_ASPFC Reviewed; 453 AA.
AC B0YAA4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Probable exopolygalacturonase B;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase B;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase B;
DE Flags: Precursor;
GN Name=pgxB; ORFNames=AFUB_083960;
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=EDP48947.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS499600; EDP48947.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0YAA4; -.
DR SMR; B0YAA4; -.
DR PhylomeDB; B0YAA4; -.
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; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..453
FT /note="Probable exopolygalacturonase B"
FT /id="PRO_0000393675"
FT REPEAT 295..316
FT /note="PbH1 1"
FT REPEAT 327..348
FT /note="PbH1 2"
FT REPEAT 362..405
FT /note="PbH1 3"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
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 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 257..274
FT /evidence="ECO:0000250"
FT DISULFID 392..398
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 50030 MW; EE6E8C5A46BC5B71 CRC64;
MKFFALAALF ASTVNSIAVD GLIPGARVIP ANDVVALKKA GAYHQKHHHR RTVIIRSSSS
DEDDVSADFL WGIKRANHGG RLLLQNGKKY VIGKKLDLTF LKDIEVQLDG ELKFTNDVPY
WQANNFYYDF QKSISFWRWG GEDIKIFGSG VLNGNGQRWY NEFAGQEILD PNNKYYRPIL
FVTENATRVS VEGITQLNSP CWTNFFVRTK DISFDNVFIH AYSTNASALP KNTDGFDTLN
VDGLTVTNTR VDIGDDCLSP KPNTTNVFVK NLWCNGTHGA SMGSIGQYPG VLDIIENVWI
ENVTLLNGEN GARLKAWAGP DVGYGRINNV TYKNIHVENT DNPIVLDQCY FNINATQCAA
YPSRVNFTNI VFEDIYGTSS GKRGKVVADL TCSPNAVCSG IRLKNIHLTS PAGSPPVIVC
DGIQGDIGVE CQSSSNSTTK RSVDLARSLK YRA
