PGXC_ASPNC
ID PGXC_ASPNC Reviewed; 440 AA.
AC A2QEW2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 58.
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=An02g12450;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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=CAK44512.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM270034; CAK44512.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; A2QEW2; -.
DR SMR; A2QEW2; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; CAK44512; CAK44512; An02g12450.
DR Proteomes; UP000006706; Chromosome 4R.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..440
FT /note="Probable exopolygalacturonase C"
FT /id="PRO_5000219659"
FT REPEAT 215..236
FT /note="PbH1 1"
FT REPEAT 238..259
FT /note="PbH1 2"
FT REPEAT 265..288
FT /note="PbH1 3"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 387..393
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 47855 MW; 7A4F38E19D6B8BE3 CRC64;
MSVFKASFLF LLSSSLVHGV PHSSRASRSQ QCVVPSKYQA SNGMADDSVA VSQAFAQCAT
DSVIIFEEGV NYNIFQPITA TNLSNVEIRM HGNLHLPQNI TAVQNIVSDG TSTWFTLEGP
KVDWIGPEDV NNGWIDSYGQ PWWDANPAGS SGIDNRPHLM SFKSSQATMK YFRSRKPIAW
NVKLHGQDIT VSHAIIDATS TGSFPFNTDG FDVEGTNIQI TDSIMYNGDD AIAVGADSHD
TLFTRNTIGY QTHGMSIGSL GKDPTDFANI SNIRFDDVTV VDGLYAARFK SWSGGTGLVK
NVTWNNIRVF NVTFPIFVTQ SYSDQGASRS GTVNASSAVM MEDFTWSDFA GSINTYQPGD
GSCVSDPCWY NVGLPNLKHT EALIIECHTA QSCKNFVTDN IQLYPQVLEP ASVICMNATA
ALNPDLGFTC KNGTYSPLSN
