RGLB_ASPOR
ID RGLB_ASPOR Reviewed; 238 AA.
AC Q2UDJ8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Probable rhamnogalacturonate lyase B;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglB; ORFNames=AO090012000147;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC pectin lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone
CC of pectin (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000305}.
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DR EMBL; AP007161; BAE60367.1; -; Genomic_DNA.
DR RefSeq; XP_003189969.1; XM_003189921.1.
DR AlphaFoldDB; Q2UDJ8; -.
DR EnsemblFungi; BAE60367; BAE60367; AO090012000147.
DR GeneID; 10099929; -.
DR KEGG; aor:AO090012000147; -.
DR HOGENOM; CLU_085593_0_0_1; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Lyase; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..238
FT /note="Probable rhamnogalacturonate lyase B"
FT /id="PRO_0000394376"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 238 AA; 26531 MW; 638E23F7A68040C7 CRC64;
MRLRTSLGVA SACASVASAA LKVTEDNSTI TLANDRLTST FAKDKGRVSE LFLDGQDLLG
PISGNTGVGP YLDCYCIPSG FYTAGSTDPR LEVVQGTDST GTKYAGVILN DTYTPTGQQF
QQYWFLRDGE TGLHTFSRLA YYNETTPFLR NLQEFRTLFR PNTELWTHLT SSEAQTAPLP
SKEAIANEVV VQDATWRFNN TPNDAYYTQF SEYFTKYTFS NCMGLFKTYW YAASANLQ