ID   PGXA_ASPNG              Reviewed;         434 AA.
AC   Q27UB2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=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;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CBS 513.88;
RX   PubMed=16822232; DOI=10.1042/bj20060703;
RA   Martens-Uzunova E.S., Zandleven J.S., Benen J.A., Awad H., Kools H.J.,
RA   Beldman G., Voragen A.G., Van den Berg J.A., Schaap P.J.;
RT   "A new group of exo-acting family 28 glycoside hydrolases of Aspergillus
RT   niger that are involved in pectin degradation.";
RL   Biochem. J. 400:43-52(2006).
CC   -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC       polygalacturonic acid and oligogalacturonates.
CC       {ECO:0000269|PubMed:16822232}.
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; DQ374423; ABD61563.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q27UB2; -.
DR   SMR; Q27UB2; -.
DR   STRING; 5061.CADANGAP00008581; -.
DR   CLAE; PGX28A_ASPNG; -.
DR   VEuPathDB; FungiDB:An11g04040; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1178374; -.
DR   VEuPathDB; FungiDB:ATCC64974_90170; -.
DR   VEuPathDB; FungiDB:M747DRAFT_322702; -.
DR   eggNOG; ENOG502QPPR; Eukaryota.
DR   BioCyc; MetaCyc:MON-20556; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..434
FT                   /note="Exopolygalacturonase A"
FT                   /id="PRO_0000393674"
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