PGLRX_NEOFI
ID PGLRX_NEOFI Reviewed; 432 AA.
AC A1DLC1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Probable exopolygalacturonase X;
DE Short=ExoPG;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase;
DE Flags: Precursor;
GN Name=pgaX; ORFNames=NFIA_049320;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW15592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027698; EAW15592.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001257489.1; XM_001257488.1.
DR AlphaFoldDB; A1DLC1; -.
DR SMR; A1DLC1; -.
DR STRING; 36630.CADNFIAP00004091; -.
DR GeneID; 4584003; -.
DR KEGG; nfi:NFIA_049320; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
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; 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; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..432
FT /note="Probable exopolygalacturonase X"
FT /id="PRO_0000393671"
FT REPEAT 231..252
FT /note="PbH1 1"
FT REPEAT 254..274
FT /note="PbH1 2"
FT REPEAT 285..306
FT /note="PbH1 3"
FT REPEAT 327..348
FT /note="PbH1 4"
FT REPEAT 362..394
FT /note="PbH1 5"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
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 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 247..264
FT /evidence="ECO:0000250"
FT DISULFID 392..398
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 47344 MW; 17305302FD3EA7DF CRC64;
MKFSYSFVQV VSLLLSLSPS VEGFTRSRND ACKPNHPFRP LPPSQPRTKT CHVVSNGHGK
DDSKNIMQAL HKCNNGGKVV FDANKVYTVG TALDMTFLKH IDLEVLGKIQ FTNDTDYWQA
HSFKHGFQNA TTFFQLGGQD VNVYGGGTFD GNGQVWYDLY AEDALILRPI LFGIIGLKGG
TIGPLKLRYS PQWYQLVANS SDVIFDGIDI SGYSSSKNEA KNTDGWDTYR SDNIVIQNSV
INNGDDCVSF KPNSTNIIVQ NLHCNGSHGI SVGSLGQYKG EVDIVQNVLV YNISMYNASD
GARIKVWPGV SSAMSEDLQG GGGLGSVKNI TYNQMYIENV DWAIEVTQCY GQKNLTLCNE
HPSNLTISDI HFKNFRGTTS GKRDPDVGTI VCSSPNVCSD IHAENINVKS PKGTDEFVCT
NVDKSLLDVN CA
