RGXB_ASPNC
ID RGXB_ASPNC Reviewed; 429 AA.
AC A2QG68; Q27UA8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Alpha-L-rhamnosidase rgxB;
DE EC=3.2.1.40;
DE AltName: Full=Exopolygalacturonase B;
DE AltName: Full=Exorhamnogalacturonase B;
DE AltName: Full=Pnp-rhamnohydrolase;
DE Flags: Precursor;
GN Name=rgxB; ORFNames=An03g02080;
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], FUNCTION, AND INDUCTION.
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: Alpha-L-rhamnosidase which is able to degrade p-nitrophenyl-
CC alpha-L-rhamnopyranoside (pnp_Rha). The natural substrate of this
CC enzyme has not been identified yet. {ECO:0000269|PubMed:16822232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC in alpha-L-rhamnosides.; EC=3.2.1.40;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: By rhamnose and sugar beet pectin.
CC {ECO:0000269|PubMed:16822232}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD61567.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAK38178.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ374427; ABD61567.1; ALT_INIT; Genomic_DNA.
DR EMBL; AM270048; CAK38178.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001390107.2; XM_001390070.2.
DR AlphaFoldDB; A2QG68; -.
DR SMR; A2QG68; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; RHA28B_ASPNG; -.
DR PaxDb; A2QG68; -.
DR EnsemblFungi; CAK38178; CAK38178; An03g02080.
DR GeneID; 4980196; -.
DR KEGG; ang:ANI_1_1122034; -.
DR BioCyc; MetaCyc:MON-18216; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..429
FT /note="Alpha-L-rhamnosidase rgxB"
FT /id="PRO_5000219749"
FT REPEAT 217..238
FT /note="PbH1 1"
FT REPEAT 240..260
FT /note="PbH1 2"
FT REPEAT 271..292
FT /note="PbH1 3"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
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 97
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 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
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 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 374..380
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 45770 MW; E3A3484DD58F6BB3 CRC64;
MAPIALKILL FTSLIVPSIS LSDQARNGHA RTICEVKPGG SSEIDDVPAI VDALTTCGSG
GRVIFSNNTY HINSVMNTTW LDDVEIDLQG TLLWSTNISY WLNHSLPVGY QNQSTAWILG
GKDIVFEGHG YGTFNGSGQT WYRYVGSTSN YPRRPNQLTV SGAMGAVFKG LRFVQSQMWT
MSIIHTSNSW FDSIYVNNLY DDGGSAQNTD GANTIYSKNI TLTNWEVVNG DDSISTKANS
TDITIANCTF TSGLGIAIGS IGQYNGAFET VERLKISNIT YEKTTHAVYF KTWTGDQVGY
PPNGGGGGLG YASDIVATNL KTNNLKGAPF TISQCTTFSG ASGNCTNSKF QIRDLVFTDI
SGTTDSSDVA SFQCSAVAPC EDITIENVSL RIAGNTTHAE EYLCGNVDGT VGFNCTGDVC
VGSSATGGC
