RHGD_ASPNC
ID RHGD_ASPNC Reviewed; 443 AA.
AC A2QWT2; Q27UA5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Putative rhamnogalacturonase D;
DE Short=RGase D;
DE Short=RHG D;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=rhgD; ORFNames=An11g06320;
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 -!- CAUTION: Lacks the conserved His residue in position 290 essential for
CC rhamnogalacturonase activity. Its enzyme activity is therefore unsure.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ374430; ABD61570.1; -; Genomic_DNA.
DR EMBL; AM270241; CAK96934.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QWT2; -.
DR SMR; A2QWT2; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QWT2; -.
DR EnsemblFungi; CAK96934; CAK96934; An11g06320.
DR VEuPathDB; FungiDB:An11g06320; -.
DR HOGENOM; CLU_016031_7_2_1; -.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..443
FT /note="Putative rhamnogalacturonase D"
FT /id="PRO_0000394956"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..63
FT /evidence="ECO:0000250"
FT DISULFID 217..234
FT /evidence="ECO:0000250"
FT DISULFID 338..344
FT /evidence="ECO:0000250"
FT DISULFID 366..375
FT /evidence="ECO:0000250"
SQ SEQUENCE 443 AA; 47724 MW; CD2CF8C23CB35F5E CRC64;
MLVTSLIALL PAIAAAQVSG TVGPRTSASA KAAEKVCNVL DYGASANSTI DIGPPLKEAF
QDCQTGGLVY IPEGDYLLSS WVSLVYGSGW ALQLDGIIYR DKNVTDGGNM IFIEHTSDIE
IFSNNSAGAI QGYGYLFHEQ DEYGPRILRL NNVTDFSVHD LILVDSPAYF LNLVESYNGE
VYNMVIRGAS MGGLDGIDIS GANYWIHDVE VTNGDECVTV KSPSANVRVE NVFCNHSGGC
AMGSLGTDTN ISNIEFENIY TYNSTQMYMI KSNGGNGTVT NCSFKNFIGY SNAYMLDLDT
YWGDESDGDG IKYENIGFEN WKGTSSNGIQ RSPIRILCPD ANPCTNITLT AVELWTDTGD
YVKQECSSAY GEGECLRQQN GTLASYSFTT TITSVPVTAY SPTTTMPGLI STSMDTTTSI
PIPTIPTSFF PGASAYSTLM ANM
