PGXC_ASPNG
ID PGXC_ASPNG Reviewed; 440 AA.
AC Q27UB0; Q2EQQ3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=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;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CBS 513.88;
RX PubMed=16822232; DOI=10.1042/bj20060703;
RA Martens-Uzunova E.S., Zandleven J.S., Benen J.A., Awad H., Kools H.J.,
RA Beldman G., Voragen A.G., Van den Berg J.A., Schaap P.J.;
RT "A new group of exo-acting family 28 glycoside hydrolases of Aspergillus
RT niger that are involved in pectin degradation.";
RL Biochem. J. 400:43-52(2006).
CC -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates. {ECO:0000250,
CC ECO:0000269|PubMed:16822232}.
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; DQ369752; ABD14402.1; -; mRNA.
DR EMBL; DQ374425; ABD61565.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27UB0; -.
DR SMR; Q27UB0; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGX28C_ASPNG; -.
DR VEuPathDB; FungiDB:An02g12450; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1107081; -.
DR VEuPathDB; FungiDB:ATCC64974_52820; -.
DR VEuPathDB; FungiDB:M747DRAFT_275664; -.
DR BioCyc; MetaCyc:MON-20554; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..440
FT /note="Exopolygalacturonase C"
FT /id="PRO_0000393686"
FT REPEAT 215..236
FT /note="PbH1 1"
FT REPEAT 238..259
FT /note="PbH1 2"
FT REPEAT 265..288
FT /note="PbH1 3"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /evidence="ECO:0000250"
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 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 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 387..393
FT /evidence="ECO:0000250"
FT CONFLICT 44
FT /note="M -> T (in Ref. 1; ABD14402)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> A (in Ref. 1; ABD14402)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="T -> I (in Ref. 1; ABD14402)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="A -> T (in Ref. 1; ABD14402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 47855 MW; 7A4F38E19D6B8BE3 CRC64;
MSVFKASFLF LLSSSLVHGV PHSSRASRSQ QCVVPSKYQA SNGMADDSVA VSQAFAQCAT
DSVIIFEEGV NYNIFQPITA TNLSNVEIRM HGNLHLPQNI TAVQNIVSDG TSTWFTLEGP
KVDWIGPEDV NNGWIDSYGQ PWWDANPAGS SGIDNRPHLM SFKSSQATMK YFRSRKPIAW
NVKLHGQDIT VSHAIIDATS TGSFPFNTDG FDVEGTNIQI TDSIMYNGDD AIAVGADSHD
TLFTRNTIGY QTHGMSIGSL GKDPTDFANI SNIRFDDVTV VDGLYAARFK SWSGGTGLVK
NVTWNNIRVF NVTFPIFVTQ SYSDQGASRS GTVNASSAVM MEDFTWSDFA GSINTYQPGD
GSCVSDPCWY NVGLPNLKHT EALIIECHTA QSCKNFVTDN IQLYPQVLEP ASVICMNATA
ALNPDLGFTC KNGTYSPLSN
