PGXA_ASPNC
ID PGXA_ASPNC Reviewed; 434 AA.
AC A2QW66;
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 A;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase A;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase A;
DE Flags: Precursor;
GN Name=pgxA; ORFNames=An11g04040;
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; AM270232; CAK48389.1; -; Genomic_DNA.
DR RefSeq; XP_001394399.1; XM_001394362.1.
DR AlphaFoldDB; A2QW66; -.
DR SMR; A2QW66; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QW66; -.
DR EnsemblFungi; CAK48389; CAK48389; An11g04040.
DR GeneID; 4984635; -.
DR KEGG; ang:ANI_1_1910094; -.
DR VEuPathDB; FungiDB:An11g04040; -.
DR HOGENOM; CLU_016031_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:AspGD.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:AspGD.
DR GO; GO:0016052; P:carbohydrate catabolic process; IDA:AspGD.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..434
FT /note="Probable exopolygalacturonase A"
FT /id="PRO_5000220581"
FT REPEAT 232..253
FT /note="PbH1 1"
FT REPEAT 255..275
FT /note="PbH1 2"
FT ACT_SITE 246
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
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 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 248..265
FT /evidence="ECO:0000250"
FT DISULFID 392..398
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 46966 MW; AAAEBE617EE910BC CRC64;
MKLPILVTLF ITLPALCVSS KTPSAPTISA YPKSPGNFKP ASGRQNSTSN VCEVKPNQTD
AAPGILAAAH TCNNGGTVFL PPGDFVVATA LDLTFLNNID FAIWGNITFK KDIDLWTTQA
FQYTFQTASL FWRFGGNNVN IYGDGKGVID GAGQYWWSAM AEDSSVMRPC LLGTDGLHHA
TISGLTMLNS PNWFNLIANS TDILISNMTM LVESEISDAP AKNTDGWDIY RSSNIVIQDS
RIVNTDDCVS FKPNSTQIVI QNLDCTGSHG ISVGSLGQYQ GETDIVEDLY IYNISMTDAS
DVARIKVWPG VPADTSGSTS GGGLGRVRNV TYEHMQSENN DHIISVSQCY ESKNQTMCDS
YPSKLVIEDV LFKDFKGTTS KKYDPEIGEL TCSSPDVCHN ITVQDINVTP PSGDSPTFTC
NNMGNSNLED ITCA
