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PGXB_ASPFU
ID   PGXB_ASPFU              Reviewed;         453 AA.
AC   Q4WBK6;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   25-MAY-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=AFUA_8G02630;
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;
OC   Aspergillus subgen. Fumigati.
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=EAL84906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000014; EAL84906.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_746944.1; XM_741851.1.
DR   AlphaFoldDB; Q4WBK6; -.
DR   SMR; Q4WBK6; -.
DR   STRING; 746128.CADAFUBP00008173; -.
DR   GeneID; 3504371; -.
DR   KEGG; afm:AFUA_8G02630; -.
DR   VEuPathDB; FungiDB:Afu8g02630; -.
DR   eggNOG; ENOG502QPPR; Eukaryota.
DR   HOGENOM; CLU_016031_1_0_1; -.
DR   InParanoid; Q4WBK6; -.
DR   OrthoDB; 1028572at2759; -.
DR   Proteomes; UP000002530; 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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..453
FT                   /note="Probable exopolygalacturonase B"
FT                   /id="PRO_0000393677"
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;  50058 MW;  EE6E8C5A46A36671 CRC64;
     MKFFALAALF ASTVNSIAVD GLIPGARVIP ANDVVALKKA GAYHQKHHHR RTVIIRSSSS
     DEDDVSADFL WGIKRANHGG RLLLQNGKKY VIGKKLDLTF LKDIEVQLDG ELKFTNDVPY
     WQANNFYYDF QKSISFWRWG GEDIKIFGSG VLNGNGQRWY NEFAGQEILD PNNKYYRPIL
     FVTENATRVS VEGITQLNSP CWTNFFVRTK DISFDNVFIH AYSTNASALP KNTDGFDTLN
     VDGLTVTNTR VDIGDDCLSP KPNTTNVFVK NLWCNGTHGA SMGSIGQYPG VLDIIENVWI
     ENVTLLNGEN GARLKAWAGP DVGYGRINNV TYKNIHVENT DNPIVLDQCY FNINATQCAA
     YPSRVNFTNI VFEDIYGTSS GKRGKVVADL TCSPNAVCSG IRLKNIHLTS PAGSPPVIVC
     DGIQGDIGVE CQSSSNSTTR RSVDLARSLK YRA
 
 
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