RGXA_ASPOR
ID RGXA_ASPOR Reviewed; 437 AA.
AC Q2UP32;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Putative galacturan 1,4-alpha-galacturonidase A;
DE EC=3.2.1.67;
DE AltName: Full=Exopolygalacturonase A;
DE AltName: Full=Exorhamnogalacturonase A;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase A;
DE Flags: Precursor;
GN Name=rgxA; ORFNames=AO090001000133;
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: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AP007154; BAE56683.1; -; Genomic_DNA.
DR RefSeq; XP_001818685.1; XM_001818633.1.
DR AlphaFoldDB; Q2UP32; -.
DR SMR; Q2UP32; -.
DR STRING; 510516.Q2UP32; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; BAE56683; BAE56683; AO090001000133.
DR GeneID; 5990656; -.
DR KEGG; aor:AO090001000133; -.
DR VEuPathDB; FungiDB:AO090001000133; -.
DR HOGENOM; CLU_016031_1_1_1; -.
DR OMA; HIHHINC; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 4.
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; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..437
FT /note="Putative galacturan 1,4-alpha-galacturonidase A"
FT /id="PRO_0000395080"
FT REPEAT 222..243
FT /note="PbH1 1"
FT REPEAT 245..265
FT /note="PbH1 2"
FT REPEAT 276..302
FT /note="PbH1 3"
FT REPEAT 322..343
FT /note="PbH1 4"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
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 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
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 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 396..402
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 48055 MW; 6286E8AE10304E53 CRC64;
MKLSGSSALL LLGFGLLGHA SPLVHVQGKN CTVKPLGHGQ DDVPNILHAV EKCGQTPGGR
ISLPAPYTYR INQRMTTHLE SSTLEVGGML LFSDDITYWV NNSYRIDFQN QSTAWRITGH
DYVVDGGPER GGIDGNGQLW YTWAKGGSNV FGRPMPLHVL NSTRAVLRNI AIRQPQFWAV
LVESSSHVEL DNFYVNATNS DPNATEDTVW IQNTDGIDTY RSDHVTITNW VYEGGDDAVA
FKPNSTNIHV ENVTVYGGPG IAFGSLGQYP DRYDIVENIT VKNANFQPSS QRAMNSGIYF
KSWIGVNFGV PPNGGGNGHG YVRNVTVEDI TFKDVQLPIY IDTCLSYLFD QNVTQYCDTS
TFRFDDLHFR NISGNGLATP TNYTGRNITF AVSMICSKEA PCTDITFEDV DIKLPESYSG
KSVLCENAGV QGLECNS
