RHGA_ASPNC
ID RHGA_ASPNC Reviewed; 446 AA.
AC A2QYE5;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Probable rhamnogalacturonase A;
DE Short=RGase A;
DE Short=RHG A;
DE EC=3.2.1.171;
DE Flags: Precursor;
GN Name=rhgA; ORFNames=An12g00950;
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 [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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic
CC bond in the rhamnogalacturonan I backbone with initial inversion of
CC anomeric configuration releasing oligosaccharides with beta-D-GalA at
CC the reducing end.; EC=3.2.1.171;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AM270260; CAK41025.1; -; Genomic_DNA.
DR RefSeq; XP_001395184.1; XM_001395147.1.
DR AlphaFoldDB; A2QYE5; -.
DR SMR; A2QYE5; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QYE5; -.
DR EnsemblFungi; CAK41025; CAK41025; An12g00950.
DR GeneID; 4985445; -.
DR KEGG; ang:ANI_1_1364104; -.
DR VEuPathDB; FungiDB:An12g00950; -.
DR HOGENOM; CLU_016031_7_2_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0046576; F:rhamnogalacturonan alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase activity; IDA:AspGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..446
FT /note="Probable rhamnogalacturonase A"
FT /id="PRO_5000220678"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
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 236
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 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..65
FT /evidence="ECO:0000250"
FT DISULFID 218..235
FT /evidence="ECO:0000250"
FT DISULFID 341..347
FT /evidence="ECO:0000250"
FT DISULFID 369..378
FT /evidence="ECO:0000250"
SQ SEQUENCE 446 AA; 46957 MW; 25638A8D74BC4E18 CRC64;
MPALPILALA LAPLLVNGQL SGSVGPLTSA HSKAATKTCN VLDYGAVADN STDIGSALSE
AWDACSDGGL IYIPPGDYAM DTWVSLSGGK ATAIILDGTI YRTGTDGGNM ILVENSSDFE
LYSNSSSGAV QGFGYVYHRE GDLDGPRILR LQDVSNFAVH DIILVDAPAF HFVMDDCSDG
EVYNMAIRGG NSGGLDGIDV WGSNIWVHDV EVTNKDECVT VKSPANNILV ESIYCNWSGG
CAMGSLGADT DITDILYRNV YTWSSNQMYM IKSNGGSGTV NNTVLENFIG HGNAYSLDVD
SYWSSMTAVD GDGVQLSNIT FKNWKGTEAD GAERGPIKVV CSDTAPCTDI TIEDFAMWTE
SGDEQTYTCE SAYGDGFCLE DSDSTTSYTT TQTVTTAPSG YSATTMAADL TTDFGTTASI
PIPTIPTSFY PGLTAISPLA SAATTA
