PGXB_NEOFI
ID PGXB_NEOFI Reviewed; 453 AA.
AC A1DAX2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=NFIA_096340;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027694; EAW20012.1; -; Genomic_DNA.
DR RefSeq; XP_001261909.1; XM_001261908.1.
DR AlphaFoldDB; A1DAX2; -.
DR SMR; A1DAX2; -.
DR STRING; 36630.CADNFIAP00009133; -.
DR EnsemblFungi; EAW20012; EAW20012; NFIA_096340.
DR GeneID; 4588479; -.
DR KEGG; nfi:NFIA_096340; -.
DR VEuPathDB; FungiDB:NFIA_096340; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR HOGENOM; CLU_016031_1_0_1; -.
DR OMA; VIENLWM; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000006702; 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..453
FT /note="Probable exopolygalacturonase B"
FT /id="PRO_0000393682"
FT REPEAT 295..316
FT /note="PbH1 1"
FT REPEAT 327..348
FT /note="PbH1 2"
FT REPEAT 362..405
FT /note="PbH1 3"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 257..274
FT /evidence="ECO:0000250"
FT DISULFID 392..398
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 50095 MW; 093A0633FDC324F4 CRC64;
MKFLALAALF ASTVSSIAVD GLIPGARVIP ANDVVALKKV GAHHQKHPHR RTVIIRPSFN
DEDDVSADFL WGIKWANRGG RLLLQKGKKY VIGKKLDLTF LKDIEVQLDG ELKFTNDVPY
WQANNFYYDF QKSISFWRWG GEDIKIFGSG VLNGNGQRWY NEFAGQEILD PNNKYYRPIL
FVTENATRVS VEGITQLNSP CWTNFFVRTK DISFNNVFIH AYSTNASALP KNTDGFDTLN
VDGLTVTNTR VDIGDDCLSP KPNTTNVFVQ NLWCNGTHGT SMGSIGQYPG VLDIIENVWI
ENVTLLNGEN GARLKAWAGP NVGYGRINNV TYKNIHVENT DNPIVLDQCY FNINATQCAA
YPSRVNFTNI VFENIYGTSS GKHGKVVADL TCSPNAVCSG IRLKNIHLTS PAGSPPVIVC
DGIQGDIGVE CQSSTNLTTK RSIGLARNLK YKA
