RHGC_ASPOR
ID RHGC_ASPOR Reviewed; 447 AA.
AC Q2UFD2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Probable rhamnogalacturonase C;
DE Short=RGase C;
DE Short=RHG C;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=rhgC; ORFNames=AO090026000252;
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; AP007159; BAE59733.1; -; Genomic_DNA.
DR RefSeq; XP_001821735.1; XM_001821683.1.
DR AlphaFoldDB; Q2UFD2; -.
DR SMR; Q2UFD2; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; BAE59733; BAE59733; AO090026000252.
DR GeneID; 5993763; -.
DR KEGG; aor:AO090026000252; -.
DR VEuPathDB; FungiDB:AO090026000252; -.
DR HOGENOM; CLU_016031_7_2_1; -.
DR OMA; TNGDECV; -.
DR Proteomes; UP000006564; Chromosome 3.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..447
FT /note="Probable rhamnogalacturonase C"
FT /id="PRO_0000394955"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 316
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 338..344
FT /evidence="ECO:0000250"
FT DISULFID 366..375
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 48280 MW; 1334C710A43A6B55 CRC64;
MQVKLFYTLA LWAPILVSAQ LSGSVGPLVD FKTKAKNKTC DITDYGAVAD GKTDVGPAIL
DAWGNCSTGG LIYVPPGTYS LATDLELKHG ESTAFQLDGV LARGHEGSYQ LILVRNCHDC
EFFSGNSQGA VQGYGYEYLQ DGNYGERLFR FQDVSDFSVH GFAAIDSPAY YLVFDTVSNG
EIYNLLVRGI ADLGMTDAFD IWGQNVWVHD IEVTNGDECV TVKSPASDFL IENIYCNLSG
GTAIGSLGTG TNISNIHYRN LYMNQADACY LKTHNGDGIV KNIVWENVIV HRGPYPLAVN
EAWGKDVGST GVQVQNLTFR NWYGENTANS RPAIRIECDE DVPCYDITLD NVNLWTEDGD
YVEWSCANAY GSGACLQEAK DTGDLATYTT AVTVTATPSY SATHMPGDFT TNPPSTAPFT
IPPMPTSFYP GATPISTLLS LSGAGGL
