ID   RHGE_ASPOR              Reviewed;         432 AA.
AC   Q2U7A4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable rhamnogalacturonase E;
DE            Short=RGase E;
DE            Short=RHG E;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=rhgE; ORFNames=AO090124000009;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AP007165; BAE62561.1; -; Genomic_DNA.
DR   RefSeq; XP_001823694.1; XM_001823642.1.
DR   AlphaFoldDB; Q2U7A4; -.
DR   SMR; Q2U7A4; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; BAE62561; BAE62561; AO090124000009.
DR   GeneID; 5995765; -.
DR   KEGG; aor:AO090124000009; -.
DR   VEuPathDB; FungiDB:AO090124000009; -.
DR   HOGENOM; CLU_016031_7_2_1; -.
DR   OMA; MFHFVID; -.
DR   Proteomes; UP000006564; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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..432
FT                   /note="Probable rhamnogalacturonase E"
FT                   /id="PRO_0000394959"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        329..335
FT                   /evidence="ECO:0000250"
FT   DISULFID        357..366
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  45955 MW;  F682B28BC0C62A92 CRC64;
     MQSKTFSVLS SCLLLIATVQ GQLSGSVGPS TSISDKKAVK TCNVLDYGAT NDNKTDVGQP
     IMNAFEDCGS GGVIYIPEGD YLIQEWVSLR NGTAFAIQLD GVIYRNGTTT SQGYMFGISG
     GSDFELYSST SKGAIQGSGY LYHMNGEFTA PRLLHISDVS HWSVHDIALV DAPMFHFVID
     DASNGEVYNM AIRGGNSGGL DGIDVSGDNI WIHDVMVTNK DECVTVKTGS HNFQIENIYC
     NWSGGCAMDS LGSGTNVSNI VYRNIYTWNS NQMYMIKSNG GDGEVSNLLF ENFIGHGNAY
     SLDLDSEWSS MDTVDGDDGE SRPPIRVICP EAIPCTDITI EDVDLWTEEG DSETYVCKNA
     FGSGACLKSD SSSTATYATT TTVTSAPSGY SATTMAADLT SAFGTDASIP IPTIPTSFYP
     GATPYSALAG SS