RHGB_ASPNC
ID RHGB_ASPNC Reviewed; 558 AA.
AC A2R3G4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Probable rhamnogalacturonase B;
DE Short=RGase B;
DE Short=RHG B;
DE EC=3.2.1.171;
DE Flags: Precursor;
GN Name=rhgB; ORFNames=An14g04200;
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; AM270321; CAK48512.1; -; Genomic_DNA.
DR RefSeq; XP_001401044.1; XM_001401007.2.
DR AlphaFoldDB; A2R3G4; -.
DR SMR; A2R3G4; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2R3G4; -.
DR EnsemblFungi; CAK48512; CAK48512; An14g04200.
DR GeneID; 4987277; -.
DR KEGG; ang:ANI_1_604124; -.
DR VEuPathDB; FungiDB:An14g04200; -.
DR HOGENOM; CLU_016031_7_2_1; -.
DR Proteomes; UP000006706; Chromosome 1R.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..558
FT /note="Probable rhamnogalacturonase B"
FT /id="PRO_5000220953"
FT REGION 503..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..68
FT /evidence="ECO:0000250"
FT DISULFID 221..238
FT /evidence="ECO:0000250"
FT DISULFID 344..350
FT /evidence="ECO:0000250"
FT DISULFID 372..381
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 57933 MW; 3A349505F6E3C305 CRC64;
MLLDKLSVLS FLGLAPIFAA AQLSGSVGPL TSASTKAATK TCNVLDYGAK ADKSTDLGAP
LASAFADCKS GGLVYVPSGD YALSTWARLS GGEAWALQID GIIYRTGTDG GNMIYIEHSS
DFELFSSTSE GAMQGLGYEF HADDNWSGPR LLRLYEVTDF SVHDFILVDS PSFHFSLDTC
TNGEIYNMAI RGGNHGGLDG IDVWSNNIWV HDVEVTNKDE CVTVKSPSKN ILIESIYCNW
SGGCGMGSFG SDTNVSDITY RNIYTWSSNN MMLIKSNGGS GFVENVLLEN FIGHGNAYSL
DIDSYWASMS AVDGDGVQLS NITVKNWKGT EAYGAERGPV KVVCADGAPC YDITIEDFAM
WTEEGDSQWY SCESAYGSGY CLQDSDDHVS YSVTTSTVSS APSGYSATSM AADLTTDFGS
TVSIPIPTIP TSFYPGATPY SALMANSAST AAASSIASHA TVHSSSASVA ASVPSAVAPS
ESIPAATSAV VSSAAAIAPS PAVGAQEGST TSAPSFAAPS GAGNSPQGPT GASGFGEKGQ
QGEQGEQGEQ GEQGVCYV
