RGXA_ASPNG
ID RGXA_ASPNG Reviewed; 438 AA.
AC Q2EQQ2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Putative galacturan 1,4-alpha-galacturonidase A;
DE EC=3.2.1.67;
DE AltName: Full=Exopolygalacturonase A;
DE AltName: Full=Exorhamnogalacturonase A;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase A;
DE Flags: Precursor;
GN Name=rgxA;
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].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
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 -!- 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; DQ369753; ABD14403.1; -; mRNA.
DR AlphaFoldDB; Q2EQQ2; -.
DR SMR; Q2EQQ2; -.
DR STRING; 5061.CADANGAP00001404; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR VEuPathDB; FungiDB:An01g14650; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1171920; -.
DR VEuPathDB; FungiDB:ATCC64974_11730; -.
DR VEuPathDB; FungiDB:M747DRAFT_354149; -.
DR eggNOG; ENOG502QWT4; Eukaryota.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
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; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..438
FT /note="Putative galacturan 1,4-alpha-galacturonidase A"
FT /id="PRO_0000395079"
FT REPEAT 186..222
FT /note="PbH1 1"
FT REPEAT 223..244
FT /note="PbH1 2"
FT REPEAT 246..266
FT /note="PbH1 3"
FT REPEAT 277..303
FT /note="PbH1 4"
FT REPEAT 323..344
FT /note="PbH1 5"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
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 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 397..403
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 47897 MW; D27923376E88ED6D CRC64;
MRMPSAISIG VFAGLSLAAS AVPSLRKNGT TCTVIPLGNG QDDVPNILSA VDECGQTSGG
RVVLPAPYTY RINQRMTTHL TDSRLEIGGT LLFSDDIDYW VNNSYRVDFQ NQSSAWRITG
HDYVVDGGPH RGGVDGNGQL WYTWAKGGSN VFGRPMPVHV FESTRATLRN LAIRQPQFWA
VLVDSSSHIN LDNFYVNATN HDSSVSPEGE WVQNTDGIDT YRSDHITITN WVYQGGDDAV
AFKGNSTNIH VENVTVYGGP GIAFGSLGQY PDRTDIVENV TVRNVRVQPS FQRAMNSGVY
FKSWIGVNYG VPPNGGGGGH GYVRNVSVEN LRLKDVQLPV YIDTCLSYLF SENITQYCDT
STYEFEDLHF RNISGNGLAT VTDYPGKNIS FAVALLCSEK APCTDLTFQD ISITLPGNYT
GKHVLCENAE VEGLPCNS
