ID   PGLR2_ASPNA             Reviewed;         362 AA.
AC   P26214; G3XYE5;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Endopolygalacturonase II;
DE            Short=EPG-II;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 2;
DE   AltName: Full=Polygalacturonase II;
DE            Short=PG-II;
DE   AltName: Full=Polygalacturonase X2;
DE   Flags: Precursor;
GN   Name=pgaII; Synonyms=pg2; ORFNames=ASPNIDRAFT_182156;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-40 AND
RP   151-161.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RX   PubMed=2226842; DOI=10.1016/0014-5793(90)81066-w;
RA   Bussink H.J.D., Kester H.C.M., Visser J.;
RT   "Molecular cloning, nucleotide sequence and expression of the gene encoding
RT   prepro-polygalacturonase II of Aspergillus niger.";
RL   FEBS Lett. 273:127-130(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [3]
RP   GLYCOSYLATION AT ASN-240, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RX   PubMed=9276972;
RX   DOI=10.1002/(sici)1097-0231(199708)11:12<1257::aid-rcm19>3.0.co;2-x;
RA   Yang Y., Bergmann C., Benen J., Orlando R.;
RT   "Identification of the glycosylation site and glycan structures of
RT   recombinant endopolygalacturonase II by mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 11:1257-1262(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), AND MUTAGENESIS OF ASP-180;
RP   ASP-201; ASP-202; HIS-223; ARG-256 AND LYS-258.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RX   PubMed=10521427; DOI=10.1074/jbc.274.43.30474;
RA   van Santen Y., Benen J.A.E., Schroeter K.-H., Kalk K.H., Armand S.,
RA   Visser J., Dijkstra B.W.;
RT   "1.68-A crystal structure of endopolygalacturonase II from Aspergillus
RT   niger and identification of active site residues by site-directed
RT   mutagenesis.";
RL   J. Biol. Chem. 274:30474-30480(1999).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC       Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC       the smooth region of the plant cell wall.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC         galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; X58893; CAA41694.1; -; Genomic_DNA.
DR   EMBL; ACJE01000008; EHA24775.1; -; Genomic_DNA.
DR   PIR; S12895; S12895.
DR   RefSeq; XP_001397067.1; XM_001397030.1.
DR   PDB; 1CZF; X-ray; 1.68 A; A/B=1-362.
DR   PDBsum; 1CZF; -.
DR   AlphaFoldDB; P26214; -.
DR   SMR; P26214; -.
DR   STRING; 380704.P26214; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28II_ASPNG; -.
DR   GlyConnect; 126; 7 N-Linked glycans.
DR   GlyCosmos; P26214; 1 site, 12 glycans.
DR   GeneID; 4988138; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1143631; -.
DR   BRENDA; 3.2.1.15; 518.
DR   SABIO-RK; P26214; -.
DR   EvolutionaryTrace; P26214; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR31884; POLYGALACTURONASE; 1.
DR   PANTHER; PTHR31884:SF1; POLYGALACTURONASE; 1.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..27
FT                   /evidence="ECO:0000269|PubMed:2226842"
FT                   /id="PRO_0000024770"
FT   CHAIN           28..362
FT                   /note="Endopolygalacturonase II"
FT                   /id="PRO_0000024771"
FT   REPEAT          156..186
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          209..229
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          238..259
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          267..289
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          301..322
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:10521427"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000305|PubMed:10521427"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10521427,
FT                   ECO:0000269|PubMed:9276972"
FT                   /id="CAR_000232"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000269|PubMed:10521427,
FT                   ECO:0007744|PDB:1CZF"
FT   DISULFID        203..219
FT                   /evidence="ECO:0000269|PubMed:10521427,
FT                   ECO:0007744|PDB:1CZF"
FT   DISULFID        329..334
FT                   /evidence="ECO:0000269|PubMed:10521427,
FT                   ECO:0007744|PDB:1CZF"
FT   DISULFID        353..362
FT                   /evidence="ECO:0000269|PubMed:10521427,
FT                   ECO:0007744|PDB:1CZF"
FT   MUTAGEN         180
FT                   /note="D->E,N: Reduces activity by 99.9%. No effect on Km
FT                   for substrate."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   MUTAGEN         201
FT                   /note="D->E,N: Reduces activity by 99.9%. No effect on Km
FT                   for substrate."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   MUTAGEN         202
FT                   /note="D->E: Reduces activity by 99.4%. No effect on Km for
FT                   substrate."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   MUTAGEN         202
FT                   /note="D->N: Reduces activity by 99.9%. No effect on Km for
FT                   substrate."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   MUTAGEN         223
FT                   /note="H->A: Reduces activity by 99.5%. No effect on Km for
FT                   substrate."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   MUTAGEN         256
FT                   /note="R->N: Reduces activity by 86%. Reduces Km for
FT                   substrate 10-fold."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   MUTAGEN         258
FT                   /note="K->N: Reduces activity by 99.2%. Reduces Km for
FT                   substrate 10-fold."
FT                   /evidence="ECO:0000269|PubMed:10521427"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   HELIX           35..41
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          46..52
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          71..80
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          157..163
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   HELIX           169..172
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          203..216
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          218..222
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          237..260
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          265..292
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          302..318
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          322..328
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   TURN            331..333
FT                   /evidence="ECO:0007829|PDB:1CZF"
FT   STRAND          334..348
FT                   /evidence="ECO:0007829|PDB:1CZF"
SQ   SEQUENCE   362 AA;  37684 MW;  952A79F612BC8000 CRC64;
     MHSFASLLAY GLVAGATFAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL NNIEVPAGTT
     LDLTGLTSGT KVIFEGTTTF QYEEWAGPLI SMSGEHITVT GASGHLINCD GARWWDGKGT
     SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM AFSVQANDIT FTDVTINNAD GDTQGGHNTD
     AFDVGNSVGV NIIKPWVHNQ DDCLAVNSGE NIWFTGGTCI GGHGLSIGSV GDRSNNVVKN
     VTIEHSTVSN SENAVRIKTI SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP
     TNGVTIQDVK LESVTGSVDS GATEIYLLCG SGSCSDWTWD DVKVTGGKKS TACKNFPSVA
     SC
//