PGXC_ASPOR
ID PGXC_ASPOR Reviewed; 437 AA.
AC Q2UQ40;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=AO090005001400;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007151; BAE56325.1; -; Genomic_DNA.
DR RefSeq; XP_001818327.1; XM_001818275.1.
DR AlphaFoldDB; Q2UQ40; -.
DR SMR; Q2UQ40; -.
DR STRING; 510516.Q2UQ40; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; BAE56325; BAE56325; AO090005001400.
DR GeneID; 5990272; -.
DR KEGG; aor:AO090005001400; -.
DR VEuPathDB; FungiDB:AO090005001400; -.
DR HOGENOM; CLU_016031_1_2_1; -.
DR OMA; RNITWKN; -.
DR Proteomes; UP000006564; Chromosome 1.
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; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..437
FT /note="Probable exopolygalacturonase C"
FT /id="PRO_0000393687"
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
