RGXC_ASPNC
ID RGXC_ASPNC Reviewed; 423 AA.
AC A2RAY7; Q27UA7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Putative galacturan 1,4-alpha-galacturonidase C;
DE EC=3.2.1.67;
DE AltName: Full=Exopolygalacturonase C;
DE AltName: Full=Exorhamnogalacturonase C;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase C;
DE Flags: Precursor;
GN Name=rgxC; ORFNames=An18g04810;
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, galacturonic acid, polygalacturonic acid and
CC sugar beet pectin. {ECO:0000269|PubMed:16822232}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; DQ374428; ABD61568.1; -; Genomic_DNA.
DR EMBL; AM270408; CAK43283.1; -; Genomic_DNA.
DR RefSeq; XP_001398939.1; XM_001398902.1.
DR AlphaFoldDB; A2RAY7; -.
DR SMR; A2RAY7; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2RAY7; -.
DR EnsemblFungi; CAK43283; CAK43283; An18g04810.
DR GeneID; 4990047; -.
DR KEGG; ang:ANI_1_1372164; -.
DR VEuPathDB; FungiDB:An18g04810; -.
DR HOGENOM; CLU_016031_1_1_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
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:0000272; P:polysaccharide catabolic process; 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 Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..423
FT /note="Putative galacturan 1,4-alpha-galacturonidase C"
FT /id="PRO_5000221344"
FT REPEAT 215..236
FT /note="PbH1 1"
FT REPEAT 238..258
FT /note="PbH1 2"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
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 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 231..248
FT /evidence="ECO:0000250"
FT DISULFID 379..385
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 45904 MW; 1AD372EC2DC16AA5 CRC64;
MQLRASVLLS FLGLASVGHA GNVENNHNVC TVRANGGHQD DVPNIMAAFK ECGNGGTIIF
PEDQSYWIAT RLHPTLKDVA IEWRGKWTFS DNLTYWRNNS YPIAFQNHHA GFIISGDNIT
INGYGTGGID GNGNTWYTAE KGDTQPGRPM PFVFWNVSEV IVDSFYVKDP PLWSVNIMNG
TNMRFNNIYC NATAVDAPWG DNWVQNTDGF DTMDATNIQL TNFVYQGGDD CIAIKPRSYN
IDIQNVTCRG GNGIAIGSLG QYLEDSSVAN IRVDKVNIIR YNEDMHNSAY LKTWVGALVP
QSSYESAGVP RGDGWGSIRN VLFSNFNVQG ASAGPSISQD SGDNGSYAGT SKMSISNVAF
VNFTGWVDTE KSVVSTVSCS EVHPCYNIDY DNVVLYPGKN ATTAGTGSCK YTADGGVHGL
SGC
