PGXC_NEOFI
ID PGXC_NEOFI Reviewed; 440 AA.
AC A1D7I1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=NFIA_068440;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027690; EAW21675.1; -; Genomic_DNA.
DR RefSeq; XP_001263572.1; XM_001263571.1.
DR AlphaFoldDB; A1D7I1; -.
DR SMR; A1D7I1; -.
DR STRING; 331117.A1D7I1; -.
DR EnsemblFungi; EAW21675; EAW21675; NFIA_068440.
DR GeneID; 4590218; -.
DR KEGG; nfi:NFIA_068440; -.
DR VEuPathDB; FungiDB:NFIA_068440; -.
DR eggNOG; ENOG502SI66; Eukaryota.
DR HOGENOM; CLU_016031_1_2_1; -.
DR OMA; RNITWKN; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000006702; 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; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..440
FT /note="Probable exopolygalacturonase C"
FT /id="PRO_0000393689"
FT REPEAT 217..238
FT /note="PbH1 1"
FT REPEAT 240..261
FT /note="PbH1 2"
FT REPEAT 272..293
FT /note="PbH1 3"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 350
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; 47924 MW; 7049248F2FE45546 CRC64;
MLITNPALLG ILASLAPLAL GAPNQSTQAR SRKCVIPSSY TSSQGTADDS PAVAGAFAQC
AENSVIIFQE GVDYNIFHPI KATNLSNVEI RVLGNLHLPQ DITAVQNIVK SGQNTWFTFQ
GPRVDWTGAD DINNGWINSY GQAWWDANPA NSSSFPNRPH LMSYKTSQAS IKNFRSRKPI
AWNVKLHGDD ITVTHAIVDA KSTGGFPFNT DGFDVEGTNI SITDSVMYNG DDAIAVNTPS
HNIVFARNTI GYQSHGMSIG SLGKDPTDFA NITNLRFEDV TVIDALYAAR FKSWSGGKGL
VKNVVWKNIR VFNVTFPIFV TQSYSDQSAS RSGTIDPSSS VMMEDFTWSN FSGSINTYHP
GDGSCVTNPC WYNAGLPNLK HTEAIVLECN TESSCKNFRT EGIRLYPQSK DSPSVICMKA
TAELNPKLGF ECKNGTFVPQ
