PGLRX_ASPNC
ID PGLRX_ASPNC Reviewed; 435 AA.
AC A2R060;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=An12g07500;
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}.
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DR EMBL; AM270279; CAK46374.1; -; Genomic_DNA.
DR RefSeq; XP_001395799.1; XM_001395762.1.
DR AlphaFoldDB; A2R060; -.
DR SMR; A2R060; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2R060; -.
DR EnsemblFungi; CAK46374; CAK46374; An12g07500.
DR GeneID; 4986099; -.
DR KEGG; ang:ANI_1_2108104; -.
DR VEuPathDB; FungiDB:An12g07500; -.
DR HOGENOM; CLU_016031_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
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.
DR PROSITE; PS00502; POLYGALACTURONASE; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..435
FT /note="Probable exopolygalacturonase X"
FT /id="PRO_5000220780"
FT REPEAT 199..229
FT /note="PbH1 1"
FT REPEAT 230..251
FT /note="PbH1 2"
FT REPEAT 253..273
FT /note="PbH1 3"
FT REPEAT 326..347
FT /note="PbH1 4"
FT REPEAT 361..409
FT /note="PbH1 5"
FT REGION 31..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..263
FT /evidence="ECO:0000250"
FT DISULFID 391..397
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 47294 MW; D886C1F42A0EB190 CRC64;
MRLTHVLSHT LGLLALGATA EAFSRSREAA CSPKKPFRPL PTSSSRDKTC HVRSHGDGSD
DSDYILSALH QCNHGGKVVF DEDKEYIIGT ALNMTFLKNI DLEVLGTILF TNDTDYWQAN
SFKQGFQNAT TFFQLGGEDV NMYGGGTING NGQVWYDLYA EDDLILRPIL MGIIGLNGGT
IGPLKLRYSP QYYHFVANSS NVLFDGIDIS GYSKSDNEAK NTDGWDTYRS NNIVIQNSVI
NNGDDCVSFK PNSTNILVQN LHCNGSHGIS VGSLGQYKDE VDIVENVYVY NISMFNASDM
ARIKVWPGTP SALSADLQGG GGSGSVKNIT YDTALIDNVD WAIEITQCYG QKNTTLCNEY
PSSLTISDVH IKNFRGTTSG SEDPYVGTIV CSSPDTCSDI YTSNINVTSP DGTNDFVCDN
VDESLLSVNC TATSD
