(data stored in ACNUC7421 zone)

SWISSPROT: PGLRX_ASPFU

ID   PGLRX_ASPFU             Reviewed;         432 AA.
AC   Q4WCZ8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   11-DEC-2019, entry version 73.
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=AFUA_6G02980;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL85740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AAHF01000012; EAL85740.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_747778.1; XM_742685.1.
DR   SMR; Q4WCZ8; -.
DR   STRING; 746128.CADAFUBP00009263; -.
DR   GeneID; 3505169; -.
DR   KEGG; afm:AFUA_6G02980; -.
DR   EuPathDB; FungiDB:Afu6g02980; -.
DR   HOGENOM; HOG000217379; -.
DR   InParanoid; Q4WCZ8; -.
DR   KO; K01213; -.
DR   OrthoDB; 1028572at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; 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;
DR   PRODOM; Q4WCZ8.
DR   SWISS-2DPAGE; Q4WCZ8.
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_0000393668"
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;  47311 MW;  09F95B72D6015B72 CRC64;
     MKFSYSFVQV VTLLLSLSPS VEGFTRSRND ACKPNHPFRP LPPSQPRTKT CHVVSNGHGK
     DDSKNIMKAL HKCNNGGKVV FDANKVYTVG TALDMTFLKH IDLEVLGKIQ FTNDTDYWQA
     NSFKHGFQNA TTFFQLGGED VNVYGGGTLD GNGQVWYDLY AEDALILRPI LFGVIGLKGG
     TIGPLKLRYS PQWYQLVANS SDVIFDGIDI SGYSSSKNEA KNTDGWDTYR SDNIVIQNSV
     INNGDDCVSF KPNSTNILVQ NLHCNGSHGI SVGSLGQYKG EVDIVQNVLV YNISMYNASD
     GARIKVWPGV SSAMSEDLQG GGGLGSVKNV TYNQMYIENV DWAIEVTQCY GQKNLTLCNE
     YPSNLTISDI HFKNFRGTTS GKRDPNVGTI VCSSPNVCSD IYAENIDVKS PKGTDNFVCT
     NVDKSLLDVN CA
//

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