RHGE_ASPNC
ID RHGE_ASPNC Reviewed; 448 AA.
AC A2QXE8; Q1ZZM1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Probable rhamnogalacturonase E;
DE Short=RGase E;
DE Short=RHG E;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=rhgE; ORFNames=An11g08700;
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].
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: Pectinolytic enzymes consist of four classes of enzymes:
CC pectine lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-
CC alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions
CC of pectins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK46056.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAK46056.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ417226; ABD67158.1; -; Genomic_DNA.
DR EMBL; AM270245; CAK46056.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2QXE8; -.
DR SMR; A2QXE8; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; CAK46056; CAK46056; An11g08700.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..448
FT /note="Probable rhamnogalacturonase E"
FT /id="PRO_5000220640"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 296
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..69
FT /evidence="ECO:0000250"
FT DISULFID 223..240
FT /evidence="ECO:0000250"
FT DISULFID 346..352
FT /evidence="ECO:0000250"
FT DISULFID 374..382
FT /evidence="ECO:0000250"
FT CONFLICT 215
FT /note="L -> LV (in Ref. 1; ABD67158)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="G -> GS (in Ref. 1; ABD67158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 47628 MW; 5BBAB90167E28246 CRC64;
MTWSTSFLVA TSLLSIINSV HAQLTGSVGP LTSVIDKAAV KTCNVCDYGA SSDNTTGVGQ
PIIDAFTDCG SGGLIHVPEG DYLLKDWVSS ENGSAWSIQL DGVLHWDSSP SAQSYIFAIT
GGSDSELSSS NATGAIQGSG YLYHRHNTYT SPRMLYISGV SDWTVHDLVL VNSPMPHFVI
DGGYNGEAYN MAICGGDHGG LDGIDLYGGN IWIHLMVTNK DECVTSKTNS HNFLIENIYC
NPSGGCAIGS LGSSVNVTNI LYRNVYTWDS NQMMMIKTNG GLGNVSNIVF ENFIGHGNVN
SLDLDSYWSS MNAIDGVGIY YHNITIYNWT GTAIDGETRP PIRVICPEDM PCTEITLVQI
DLLVEEGRYD EYYCAIACGG YCLDSATSTL TTYTTTTYGN SASTGYEAPT MADDLATAFG
TTASIPTPTT PASFFPGVAP VSAVAGSS
