PGLRX_ASPFN
ID PGLRX_ASPFN Reviewed; 433 AA.
AC B8NG16;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Probable exopolygalacturonase X;
DE Short=ExoPG;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase;
DE Flags: Precursor;
GN Name=pgaX; ORFNames=AFLA_131770;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates. {ECO:0000250}.
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; EQ963478; EED50415.1; -; Genomic_DNA.
DR RefSeq; XP_002379191.1; XM_002379150.1.
DR AlphaFoldDB; B8NG16; -.
DR SMR; B8NG16; -.
DR STRING; 5059.CADAFLAP00007056; -.
DR EnsemblFungi; EED50415; EED50415; AFLA_131770.
DR VEuPathDB; FungiDB:AFLA_131770; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR HOGENOM; CLU_016031_1_0_1; -.
DR OMA; YSPQWYT; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
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; 4.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..433
FT /note="Probable exopolygalacturonase X"
FT /id="PRO_0000393667"
FT REPEAT 229..250
FT /note="PbH1 1"
FT REPEAT 252..272
FT /note="PbH1 2"
FT REPEAT 325..346
FT /note="PbH1 3"
FT REPEAT 360..403
FT /note="PbH1 4"
FT REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..262
FT /evidence="ECO:0000250"
FT DISULFID 390..396
FT /evidence="ECO:0000250"
SQ SEQUENCE 433 AA; 46813 MW; 95BFAB6F69225469 CRC64;
MKLTQATTLL LSLGLSLPVE GFSLSRTNAV GPKPPFRPLP ASTPRNKTCQ VQSNGDGTDD
APYILAALKQ CNNGGKVVFA EDKEYTIGTA LDMTFLKHVD LEILGKITFT PDTDYWQENS
FKHTFQNATT FFNLGGTDVN VYGGGELNGN GQVWYDLYAE DALILRPILV GIIGLHGGTI
GPLKLRYSPQ WYQLVANSSD VLFDGIDISG YSSSENEAKN TDGWDTYRSS NIVIQNSVIN
NGDDCVSFKP NSTEILVQNL HCNGSHGISV GSLGQYQGEV DIVQNVLVYN ISMYNASDMA
RIKVWPGISS AMSEDLQGGG GLGSVQNITY DKMYIENVDW AIEVTQCYGQ KNQTLCNENP
SNLTISDVYF NDLTGVTSGK NDPNVGTIIC SSPDVCSGIH ATNIDVKSPD GDSGFVCTNV
DEEFLDVECA SSS
