PGXC_ASPFN
ID PGXC_ASPFN Reviewed; 437 AA.
AC B8MZZ6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Probable exopolygalacturonase C;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase C;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase C;
DE Flags: Precursor;
GN Name=pgxC; ORFNames=AFLA_086360;
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; EQ963472; EED57938.1; -; Genomic_DNA.
DR RefSeq; XP_002373550.1; XM_002373509.1.
DR AlphaFoldDB; B8MZZ6; -.
DR SMR; B8MZZ6; -.
DR STRING; 332952.B8MZZ6; -.
DR EnsemblFungi; EED57938; EED57938; AFLA_086360.
DR VEuPathDB; FungiDB:AFLA_086360; -.
DR eggNOG; ENOG502SI66; Eukaryota.
DR HOGENOM; CLU_016031_1_2_1; -.
DR OMA; RNITWKN; -.
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; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; SSF51126; 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..437
FT /note="Probable exopolygalacturonase C"
FT /id="PRO_0000393684"
FT REPEAT 215..236
FT /note="PbH1 1"
FT REPEAT 238..259
FT /note="PbH1 2"
FT REPEAT 270..291
FT /note="PbH1 3"
FT REPEAT 299..320
FT /note="PbH1 4"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 386..392
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 47626 MW; FC9600F1F9DEE7CB CRC64;
MLITKTAFLA FLLSSVPLAH GAGGNSSSPD ARGRRCVVRS SNGTADDSPE VSRVFAQCAT
NSVIVFQEGV DYNIFQPIKA TNLSNVEIQM HGNLHLPQNI SAVRDIVNAG TSTWFTLEGP
RVDWTGPEDV NNGWIKSYGQ AWWDANPPNG TGISGRPHLM SYKTSQATIK YFRSGKPIAW
NMKLHGEDIA VSHAIVDASS TGSFPFNTDA FDVQGTNIRI SDSIMYNGDD AIAVGSDSHN
IVFERNTIGY QSHGMSIGSL GKDASAFANI TNLRFEDVTV IDALYAARFK SWTGGQGLVK
NVTWKNIRVY NVTFPIFVTQ SYYDQSVSRD GVDTESSVMM EDFTWEDFSG SINSYQPGDG
SCATDPCWYN AGLPNLKHTE ALVIECNTDK SCKNFVTKNI QLYPQVLEPA SVICMKATAE
LNPNLGFNCS NGTFTSA
