PGXB_ASPOR
ID PGXB_ASPOR Reviewed; 435 AA.
AC Q2TW03;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Probable exopolygalacturonase B;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase B;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase B;
DE Flags: Precursor;
GN Name=pgxB; ORFNames=AO090010000753;
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; AP007175; BAE66570.1; -; Genomic_DNA.
DR RefSeq; XP_001827703.2; XM_001827651.2.
DR AlphaFoldDB; Q2TW03; -.
DR SMR; Q2TW03; -.
DR STRING; 510516.Q2TW03; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PRIDE; Q2TW03; -.
DR VEuPathDB; FungiDB:AO090010000753; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase 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 Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..435
FT /note="Probable exopolygalacturonase B"
FT /id="PRO_0000393679"
FT REPEAT 208..239
FT /note="PbH1 1"
FT REPEAT 240..261
FT /note="PbH1 2"
FT REPEAT 262..283
FT /note="PbH1 3"
FT REPEAT 294..315
FT /note="PbH1 4"
FT REPEAT 326..347
FT /note="PbH1 5"
FT REPEAT 366..388
FT /note="PbH1 6"
FT ACT_SITE 254
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256..273
FT /evidence="ECO:0000250"
FT DISULFID 391..397
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48386 MW; C4D45E2D9050B524 CRC64;
MKFFLATLFA SAVSSIAVDR LIPGAQIIPE SDTRALLRVG GHHDKYHDRR TITIRPSRND
TDDVSRDFLW GIKHANHGGR LLLKKGEKYV IGRKLDLTFL DDIEVQLDGE LKFTDDVSYW
QENNFYYDFQ KSITFWRWGG KDIKIFGTGL LNGNGQRWYN EFAGQEILDP DNEYYRPILF
LTENATRISV EGITQLNSPC WTNFFIQSKD VSFDDVYIHA FSTNKSALPK NSDGFDSLNV
DGLTVTNTRV DVGDDCFSPK PNTTNIFVQN LLCNNTHGVS MGSIGQYPGV MDIIEHAYIE
NVTLLNGQNG ARLKAWAGQD VGYGRINNIT YKNIRIENTD APVVLDQCYF DIEAAECAQY
PSQVNVTNIL FENISGTSSG KNGKVVADLV CSPNAVCSDI QLKNINLTSP AGSPPEIICE
GVQGDIGVEC QASAD
