RGXA_ASPNC
ID RGXA_ASPNC Reviewed; 438 AA.
AC A2QBB4; Q27UA9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 63.
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; ORFNames=An01g14650;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 -!- INDUCTION: By rhamnose. {ECO:0000269|PubMed:16822232}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK44162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ374426; ABD61566.1; -; Genomic_DNA.
DR EMBL; AM269993; CAK44162.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001389853.2; XM_001389816.2.
DR AlphaFoldDB; A2QBB4; -.
DR SMR; A2QBB4; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QBB4; -.
DR EnsemblFungi; CAK44162; CAK44162; An01g14650.
DR GeneID; 4977826; -.
DR KEGG; ang:ANI_1_1976014; -.
DR VEuPathDB; FungiDB:An01g14650; -.
DR Proteomes; UP000006706; Chromosome 2R.
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;
KW Reference proteome; Repeat; 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_5000219494"
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; 47770 MW; F3D5C89388F1CDBC CRC64;
MRMPSAISIG VIAGLSVAAS AVPSLQKNGT TCTVIPLGNG QDDVPNILSA VDECGQTSGG
RVVLPAPYTY RINQRMTTHL TDSRLEIGGT LLFSDDIDYW VNNSYRVDFQ NQSSAWRITG
HDYVVDGGPR QGGVDGNGQL WYTWAKGGSN VFGRPMPVHV FESTRATLRN LAIRQPQFWA
VLVDSSSHIN LDNFYVNATN HDSSVSPEGE WVQNTDGIDT YRSDHITVTN WVYQGGDDAV
AFKGNSTNIH VENVTVYGGP GIAFGSLGQY PDRTDIVENV TVRNVRVQPS FQRAMNSGVY
FKSWIGVNYG VPPNGGGGGH GYVRNVSVEN LRLKDVQLPV YIDTCLSYLF SENITQYCDT
STYEFEDLHF RNISGNGLAT VTDYPGKNIS FAVALLCSEK APCTDLTFQD ISITLPGNYT
GKHVLCENAE AEGLPCNS
