PGXC_ASPFC
ID PGXC_ASPFC Reviewed; 440 AA.
AC B0XYC4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Probable exopolygalacturonase C;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase C;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase C;
DE Flags: Precursor;
GN Name=pgxC; ORFNames=AFUB_040410;
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}.
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DR EMBL; DS499596; EDP52870.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XYC4; -.
DR SMR; B0XYC4; -.
DR EnsemblFungi; EDP52870; EDP52870; AFUB_040410.
DR VEuPathDB; FungiDB:AFUB_040410; -.
DR HOGENOM; CLU_016031_1_2_1; -.
DR PhylomeDB; B0XYC4; -.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..440
FT /note="Probable exopolygalacturonase C"
FT /id="PRO_0000393683"
FT REPEAT 188..210
FT /note="PbH1 1"
FT REPEAT 217..238
FT /note="PbH1 2"
FT REPEAT 240..261
FT /note="PbH1 3"
FT REPEAT 272..293
FT /note="PbH1 4"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 389..395
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 48017 MW; E8FFC8B8B17C10BC CRC64;
MLITNPALLG ILASLVPLAL GAPNQPIQAR SRKCVIPSSY ASSHGTADDS PAVASAFAQC
AENSVIVFQE GVDYNIFHPI KATNLSNVEI RVLGNLHLPQ DITAVQNIVK SGQSTWFTFQ
GPRVDWTGAD DIKNGWINSY GQAWWDANPA NSSSFPNRPH LMSYKTSQAS IKNFRSRKPI
AWNVKLQGDD ITVSHAIVDA TSTGGFPFNT DGFDVEGTNI SITDSVMFNG DDAIAVNTPS
HNIVFARNTI GYQSHGMSIG SLGKDPTDFA NITNLRFEDV TVIDALYAAR FKSWSGGRGL
VKNVVWKNIR TFNVTFPIFV TQSYSDQSAS RPGTIDPFSS VMMEDFTWSD FSGTINTYHP
GDGSCVTDPC WYNVGLPNLK HTEAIVLECN TESSCKNFRT EGIRLHPQSK DSPSVICMKA
TAELNPKLGF ECKNGTFVPH
