ID   RHGA_ASPOR              Reviewed;         467 AA.
AC   Q2U293;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Probable rhamnogalacturonase A;
DE            Short=RGase A;
DE            Short=RHG A;
DE            EC=3.2.1.171;
DE   Flags: Precursor;
GN   Name=rhgA; ORFNames=AO090038000552;
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; AP007169; BAE64322.1; -; Genomic_DNA.
DR   RefSeq; XP_001825455.1; XM_001825403.1.
DR   AlphaFoldDB; Q2U293; -.
DR   SMR; Q2U293; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; BAE64322; BAE64322; AO090038000552.
DR   GeneID; 5997550; -.
DR   KEGG; aor:AO090038000552; -.
DR   VEuPathDB; FungiDB:AO090038000552; -.
DR   HOGENOM; CLU_016031_7_2_1; -.
DR   OMA; KSNQMYM; -.
DR   Proteomes; UP000006564; Chromosome 6.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..467
FT                   /note="Probable rhamnogalacturonase A"
FT                   /id="PRO_0000394384"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        292
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..348
FT                   /evidence="ECO:0000250"
FT   DISULFID        370..379
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  49455 MW;  E592B56DD69EFC5F CRC64;
     MHSLSLISLA LLSPLLVNAQ LSGHVGPLTS SSSKASTKTC NVQDYGAKAD KETDIGSAIE
     KAWDDCAEGG VVYIPSGDYA MFSRLKLSGG KASAIQLDGI IYRTGSDGGN LFMIEHSSDF
     EFFSSTSQGA IQGLGYEFHK DGSLNGPRLL RFYDVTDFSV HDVALVDSPA FHLSLDTCKN
     AEIYNMAIRG GDSGGLDGVD IWSENVWVHD VEVTNKDECV TVKSPAKNIL VENIYCNWSG
     GCAMGSLGAD TNISDVVYRN VYTWKSNQMY MIKSNGGSGS VSNLVLENFI GHGNAYSLDI
     DGEWSSMSTV SGDGVQLNNI TVRNWKGTEE DGAARGPIKV VCAEKAPCTD ITIDDFALWT
     ESGDEQTYSC ENGFGSGFCL QDGDGTSSYS TVITETAAPT GYEASSMSND LSTAFGTDAS
     IPIPTIPTSF FPGATPYSAL AGAASGNAAK ATSSATASRF RHRRGSH