PGLR2_ASPNA
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 03-AUG-2022, entry version 122.
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 / NRRL
RC 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 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 EnsemblFungi; EHA24775; EHA24775; ASPNIDRAFT_182156.
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; -; 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 Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 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; Reference proteome;
KW Repeat; Secreted; 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
