RHGC_ASPNC
ID RHGC_ASPNC Reviewed; 459 AA.
AC A2QLQ5; Q27UA6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Probable rhamnogalacturonase C;
DE Short=RGase C;
DE Short=RHG C;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=rhgC; ORFNames=An06g02070;
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}.
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DR EMBL; DQ374429; ABD61569.1; -; Genomic_DNA.
DR EMBL; AM270115; CAK48050.1; -; Genomic_DNA.
DR RefSeq; XP_001391028.1; XM_001390991.1.
DR AlphaFoldDB; A2QLQ5; -.
DR SMR; A2QLQ5; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QLQ5; -.
DR EnsemblFungi; CAK48050; CAK48050; An06g02070.
DR GeneID; 4981206; -.
DR KEGG; ang:ANI_1_554054; -.
DR VEuPathDB; FungiDB:An06g02070; -.
DR HOGENOM; CLU_016031_7_2_1; -.
DR Proteomes; UP000006706; Chromosome 8ER.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..459
FT /note="Probable rhamnogalacturonase C"
FT /id="PRO_0000394954"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
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 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
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 337..343
FT /evidence="ECO:0000250"
FT DISULFID 365..374
FT /evidence="ECO:0000250"
SQ SEQUENCE 459 AA; 49814 MW; 292D4B8D98B001EE CRC64;
MRASILPLTL FLATLAGAQL SGPVGPLVDY STKARNQTCN IIDYGAVADG KTDISQALLD
AWGNCSVGGL VYIPPGNYSL AEDIELKHGQ SSAIQLDGVV MRGHRGSYQM ILIRDCNDFE
FFSGNSRGAI QGFGYEYLQN DTYGERLLRI QEVNNFSVHG FALIDSPSYY IVFDTVTSGE
VYNILIRGVT SVGATDAIDV WGENMWFHDI EVSNGDECVT VKSPAHNYLI ENIYCNLSGG
TAIGSLGTGT NISDIHYRNL YMNQADACFL KSNNGDGIVK NIIWENVIVH GGPYPLAIDE
AWGDDRGSVG VQVSNLTFRN WHGESVSASR PVIRLQCDSD VPCYDITIEN VNLWANDSNY
VVWQCENAYG DGACLSSAEG TKDLETFTSK QTITATPSYA APTMAADFTF NLPSTSPFTI
PPMPTSFYPG ATPISTLLHL HGAGGLPSAS PISHHRRHQ
