ID   RHGB_ASPOR              Reviewed;         532 AA.
AC   Q2TWN8;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=AO090010000484;
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       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; AP007175; BAE66335.1; -; Genomic_DNA.
DR   RefSeq; XP_001827468.1; XM_001827416.1.
DR   AlphaFoldDB; Q2TWN8; -.
DR   SMR; Q2TWN8; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; BAE66335; BAE66335; AO090010000484.
DR   GeneID; 5999602; -.
DR   KEGG; aor:AO090010000484; -.
DR   VEuPathDB; FungiDB:AO090010000484; -.
DR   HOGENOM; CLU_016031_7_2_1; -.
DR   OMA; PNCQPNI; -.
DR   Proteomes; UP000006564; Chromosome 8.
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; ISS:UniProtKB.
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..532
FT                   /note="Probable rhamnogalacturonase B"
FT                   /id="PRO_0000394389"
FT   REGION          466..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..500
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        239
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        374..383
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  56503 MW;  C2C4B98299C26FCD CRC64;
     MRINTLSLFS LVSLVPTLAL ASLSGSVGPL TSASTKAATK TCNVLDYGAK ADKTTDLGPP
     LASAFADCKS GGLVYVPSGD YALSTWAKLS GGKAWALQID GTIYRTGTDG GNMIFIEHSS
     DFELFSSTSS GAMQGLGYEY HKDNKWSGPR LLRLYDVTDF SVHDFILVDA PAFHFSLDTC
     TNGEVYNMAI RGGNHGGLDG VDVWSTNVWI HDIEVTNKDE CVTVKSPSKN ILVENIYCNW
     SGGCGMGSLG KDTDISDITY RNIYTWNSNN MMFIKSNGGS GSATNLLFEN FIGHGNAYSF
     DIDSYWASMS SQGGNGVELS NITLRNWKGT EENGASRGPI KIVCPDGAPC YDITIEDFAM
     WTEDSSRQRQ WYSCRNAYGT GFCLKSGSNH VAYEATTTTV SSAPSGYSAA TMAADLKTDF
     GITASIPIPT IPTSFYPGAT PYSALMANKG STAKVRAVVA PSKPTTVAAA TSTPAEQQTS
     TSTPAPAVEQ PSQQSPGQSA GEVGGCPFGN GRSVPTGPPR AGHRHHQRHG HH