PGLR1_ASPAC
ID PGLR1_ASPAC Reviewed; 378 AA.
AC O74213;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=KSM 510;
RA Kauppinen S., Andersen L.N., Christgau S., Dalboege H., Kofod L.V.;
RT "Molecular and biochemical characterization of three functionally different
RT polygalacturonases from the filamentous fungus Aspergillus aculeatus.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schnorr K.M., Kauppinen S.;
RT "Molecular and biochemical characterization of three polygalacturonases
RT from the filamentous fungus Aspergillus aculeatus.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-378, GLYCOSYLATION AT THR-44;
RP SER-46; SER-48; SER-52; SER-53; SER-55; SER-57; SER-62; THR-63; SER-73 AND
RP ASN-258, DISULFIDE BONDS, AND ACTIVE SITE.
RX PubMed=11518536; DOI=10.1006/jmbi.2001.4919;
RA Cho S.W., Lee S., Shin W.;
RT "The X-ray structure of Aspergillus aculeatus polygalacturonase and a
RT modeled structure of the polygalacturonase-octagalacturonate complex.";
RL J. Mol. Biol. 311:863-878(2001).
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; AF054893; AAC23565.1; -; mRNA.
DR EMBL; AJ581480; CAE46193.1; -; mRNA.
DR PDB; 1IA5; X-ray; 2.00 A; A=40-378.
DR PDB; 1IB4; X-ray; 2.00 A; A/B=40-378.
DR PDBsum; 1IA5; -.
DR PDBsum; 1IB4; -.
DR AlphaFoldDB; O74213; -.
DR SMR; O74213; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR iPTMnet; O74213; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_53360; -.
DR EvolutionaryTrace; O74213; -.
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;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..39
FT /evidence="ECO:0000255"
FT /id="PRO_0000024762"
FT CHAIN 40..378
FT /note="Endopolygalacturonase I"
FT /id="PRO_0000024763"
FT REPEAT 174..204
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 205..226
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 227..247
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 256..277
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 285..307
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11518536"
FT ACT_SITE 241
FT /evidence="ECO:0000269|PubMed:11518536"
FT CARBOHYD 44
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 46
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 48
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 52
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 53
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 55
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 57
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 62
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 63
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 73
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT DISULFID 43..61
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT DISULFID 221..237
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT DISULFID 345..350
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT DISULFID 369..378
FT /evidence="ECO:0000269|PubMed:11518536,
FT ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1IA5"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1IA5"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:1IA5"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1IA5"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1IA5"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1IA5"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1IA5"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 255..268
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 284..309
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 322..334
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:1IA5"
FT STRAND 350..364
FT /evidence="ECO:0007829|PDB:1IA5"
SQ SEQUENCE 378 AA; 38528 MW; DC5B9B6E1D2059C8 CRC64;
MHLNTTLLVS LALGAASVLA SPAPPAITAP PTAEEIAKRA TTCTFSGSNG ASSASKSKTS
CSTIVLSNVA VPSGTTLDLT KLNDGTHVIF SGETTFGYKE WSGPLISVSG SDLTITGASG
HSINGDGSRW WDGEGGNGGK TKPKFFAAHS LTNSVISGLK IVNSPVQVFS VAGSDYLTLK
DITIDNSDGD DNGGHNTDAF DIGTSTYVTI SGATVYNQDD CVAVNSGENI YFSGGYCSGG
HGLSIGSVGG RSDNTVKNVT FVDSTIINSD NGVRIKTNID TTGSVSDVTY KDITLTSIAK
YGIVVQQNYG DTSSTPTTGV PITDFVLDNV HGSVVSSGTN ILISCGSGSC SDWTWTDVSV
SGGKTSSKCT NVPSGASC
