PGXC_ASPTN
ID PGXC_ASPTN Reviewed; 432 AA.
AC Q0CXI3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=ATEG_01601;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476595; EAU38358.1; -; Genomic_DNA.
DR RefSeq; XP_001208966.1; XM_001208966.1.
DR AlphaFoldDB; Q0CXI3; -.
DR SMR; Q0CXI3; -.
DR STRING; 341663.Q0CXI3; -.
DR EnsemblFungi; EAU38358; EAU38358; ATEG_01601.
DR GeneID; 4316238; -.
DR VEuPathDB; FungiDB:ATEG_01601; -.
DR eggNOG; ENOG502SI66; Eukaryota.
DR HOGENOM; CLU_016031_1_2_1; -.
DR OMA; RFKSWIG; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000007963; 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; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..432
FT /note="Probable exopolygalacturonase C"
FT /id="PRO_0000393688"
FT REPEAT 206..227
FT /note="PbH1 1"
FT REPEAT 229..250
FT /note="PbH1 2"
FT REPEAT 261..282
FT /note="PbH1 3"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 377..383
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 47632 MW; D979D6F4D99782E9 CRC64;
MPISKGIFLS LLSTLPLALA GHRSHRCVVP SSNGTRDDSP AIAKVFAQCA TDSIIVFQEG
VDYNVFQPIK AENLSNVEIR MHGNLHLPQN ISAVQEIVKA GNSYWFTLEG PRVDWTGSED
INHGWINSYG QAWWDANPPN GTGIENRPHL LSYTTSDATI KYMRSRKPIA HNCRLHGDDI
TVTHAIVDAY STGGFPFNTD GFDVAGTNIR ISDSVMYNGD DAIAVGSGSH DIVFERNTIG
YQSHGMSIGS LGKDPTDFAN ITNLRFEDVT VIDALYAARF KSWTGGQGLV KNVTWKNIRV
FNVTFPIFVT QSYWDQGANR GDVDESSSVM MEDFTWSDFT GSINTYQPGD GSCASDPCWY
NAGLPNLQHT EAIILECNTA TSCKNFVTEN IQLYPQSMDA PHLICMNATA ELNPRLGFDC
RNGMYTALSE RH
