PGXB_ASPTN
ID PGXB_ASPTN Reviewed; 435 AA.
AC Q0C7H7;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=ATEG_10357;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476610; EAU29354.1; -; Genomic_DNA.
DR RefSeq; XP_001218705.1; XM_001218704.1.
DR AlphaFoldDB; Q0C7H7; -.
DR SMR; Q0C7H7; -.
DR STRING; 341663.Q0C7H7; -.
DR EnsemblFungi; EAU29354; EAU29354; ATEG_10357.
DR GeneID; 4354598; -.
DR VEuPathDB; FungiDB:ATEG_10357; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR HOGENOM; CLU_016031_1_0_1; -.
DR OMA; DQCYFNV; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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_0000393680"
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 368
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; 47930 MW; EBCD890BD1789445 CRC64;
MKFFTAALFA SAVSAFAVDS IIPGARVIPA TDTLELQHVG AHHHKHPNRR TVTIRSSRND
TDDVSKDFLW GISRANHGGR LLLQKGKKYV IGKKLDLSFL NNIEVQLDGE LKFTDDVPYW
QKNNFYYSFQ KSISFWRWGG QDIKIFGSGV LNGNGQRWYN EFAGQEILDP DNTFYRPILF
VTENATRVSV EGITQLNSPC WTNFFVGSND VSFDNVYIEA FSTNASALPK NTDGFDSYNV
KGLSVTNTRV NVGDDCFSPK PNTTDIFVQN LWCNGTHGVS MGSIGQYPGV MDIIEHAYIE
NVTLLNGQNG ARLKAWAGEN VGYGRINNIT YKNIRIENTD KPVVLDQCYF NVDTATCAEY
PSSVNITNIT FENVYGTSSG KEGKVVADLV CSPNAVCSDI HLADIDLTSP AGSPPVIICE
GIQGDIGVEC QSSTS
