PGLR1_ASPNG
ID PGLR1_ASPNG Reviewed; 368 AA.
AC P26213;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Endopolygalacturonase I;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase 1;
DE AltName: Full=Polygalacturonase I;
DE Short=PG-I;
DE Flags: Precursor;
GN Name=pgaI; Synonyms=pg1, pga1;
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 PROTEIN SEQUENCE OF 32-43; 107-117
RP AND 205-221.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=1934135; DOI=10.1007/bf00318519;
RA Bussink H.J.D., Brouwer K., de Graaff L.H., Kester H.C.M., Visser J.;
RT "Identification and characterization of a second polygalacturonase gene of
RT Aspergillus niger.";
RL Curr. Genet. 20:301-307(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-368, AND GLYCOSYLATION AT
RP SER-44; SER-46 AND ASN-246.
RX PubMed=14623112; DOI=10.1016/s0014-5793(03)01221-3;
RA van Pouderoyen G., Snijder H.J., Benen J.A.E., Dijkstra B.W.;
RT "Structural insights into the processivity of endopolygalacturonase I from
RT Aspergillus niger.";
RL FEBS Lett. 554:462-466(2003).
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; X58892; CAA41693.1; -; Genomic_DNA.
DR PIR; S17980; S17980.
DR PDB; 1NHC; X-ray; 1.70 A; A/B/C/D/E/F=33-368.
DR PDBsum; 1NHC; -.
DR AlphaFoldDB; P26213; -.
DR SMR; P26213; -.
DR STRING; 5061.CADANGAP00001113; -.
DR Allergome; 8269; Asp n Pectinase.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGA28I_ASPNG; -.
DR iPTMnet; P26213; -.
DR VEuPathDB; FungiDB:An01g11520; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1149968; -.
DR VEuPathDB; FungiDB:ATCC64974_14230; -.
DR VEuPathDB; FungiDB:M747DRAFT_286011; -.
DR eggNOG; ENOG502QST2; Eukaryota.
DR BRENDA; 3.2.1.15; 518.
DR EvolutionaryTrace; P26213; -.
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; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..31
FT /evidence="ECO:0000255"
FT /id="PRO_0000024768"
FT CHAIN 32..368
FT /note="Endopolygalacturonase I"
FT /id="PRO_0000024769"
FT REPEAT 140..161
FT /note="PbH1 1"
FT REPEAT 162..192
FT /note="PbH1 2"
FT REPEAT 193..214
FT /note="PbH1 3"
FT REPEAT 244..265
FT /note="PbH1 4"
FT REPEAT 273..295
FT /note="PbH1 5"
FT REPEAT 307..352
FT /note="PbH1 6"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 229
FT /evidence="ECO:0000305"
FT CARBOHYD 44
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:14623112"
FT CARBOHYD 46
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:14623112"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:14623112"
FT DISULFID 35..50
FT DISULFID 209..225
FT DISULFID 335..340
FT DISULFID 359..368
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1NHC"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1NHC"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1NHC"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1NHC"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 135..147
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1NHC"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 202..222
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 224..240
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 243..256
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 272..298
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 312..324
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:1NHC"
FT STRAND 340..354
FT /evidence="ECO:0007829|PDB:1NHC"
SQ SEQUENCE 368 AA; 38108 MW; CD9B46A9A99B5102 CRC64;
MHSYQLLGLA AVGSLVSAAP APSRVSEFAK KASTCTFTSA SEASESISSC SDVVLSSIEV
PAGETLDLSD AADGSTITFE GTTSFGYKEW KGPLIRFGGK DLTVTMADGA VIDGDGSRWW
DSKGTNGGKT KPKFMYIHDV EDSTFKGINI KNTPVQAISV QATNVHLNDF TIDNSDGDDN
GGHNTDGFDI SESTGVYISG ATVKNQDDCI AINSGESISF TGGTCSGGHG LSIGSVGGRD
DNTVKNVTIS DSTVSNSANG VRIKTIYKET GDVSEITYSN IQLSGITDYG IVIEQDYENG
SPTGTPSTGI PITDVTVDGV TGTLEDDATQ VYILCGDGSC SDWTWSGVDL SGGKTSDKCE
NVPSGASC
