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PGXB_ASPNG
ID   PGXB_ASPNG              Reviewed;         438 AA.
AC   Q27UB1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=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;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CBS 513.88;
RX   PubMed=16822232; DOI=10.1042/bj20060703;
RA   Martens-Uzunova E.S., Zandleven J.S., Benen J.A., Awad H., Kools H.J.,
RA   Beldman G., Voragen A.G., Van den Berg J.A., Schaap P.J.;
RT   "A new group of exo-acting family 28 glycoside hydrolases of Aspergillus
RT   niger that are involved in pectin degradation.";
RL   Biochem. J. 400:43-52(2006).
CC   -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC       polygalacturonic acid and oligogalacturonates.
CC       {ECO:0000269|PubMed:16822232}.
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; DQ374424; ABD61564.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q27UB1; -.
DR   SMR; Q27UB1; -.
DR   STRING; 5061.CADANGAP00003593; -.
DR   CLAE; PGX28B_ASPNG; -.
DR   VEuPathDB; FungiDB:An03g06740; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1186687; -.
DR   VEuPathDB; FungiDB:ATCC64974_76140; -.
DR   VEuPathDB; FungiDB:M747DRAFT_368542; -.
DR   eggNOG; ENOG502QPPR; Eukaryota.
DR   BioCyc; MetaCyc:MON-20555; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; Repeat; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..438
FT                   /note="Exopolygalacturonase B"
FT                   /id="PRO_0000393678"
FT   REPEAT          209..248
FT                   /note="PbH1 1"
FT   REPEAT          295..316
FT                   /note="PbH1 2"
FT   REPEAT          327..348
FT                   /note="PbH1 3"
FT   REPEAT          398..430
FT                   /note="PbH1 4"
FT   ACT_SITE        255
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
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   438 AA;  48383 MW;  C1BB7FECF39374D3 CRC64;
     MYLLPLTLFL TAAFGVSIPR SPLIPGAQIV PASSTADLRA IGAQHHKYPD RETVTIRASR
     NALDDVSSDF LWGLKQANHG GRLLLKQGET YVIGKKLDLT FLDNIEVQLE GEIQFTNNIT
     YWQANNFYYD FQKSITFWRW GGQDIKIFGS GVLNGNGQKW YDEFAGKQIL VYNTFYRPIL
     FLTDNATRIS VEGITQLNSP CWTNFFVRTN DVSFDNVYIH AFSTNASSDP ANTDGMDSLD
     VDGVSFTNMR IDVGDDCFSP KPNTTNIFVQ NMWCNNTHGV SMGSIGQYAG EMDIIENVYI
     ENVTLLNGQN GARLKAWAGQ DVGYGRINNV TYKNIQIQNT DAPIVLDQCY FDINATECAK
     YPSAVNITNI LFENIWGSSS GKDGKIVADL VCSPDAVCTN ITLSNVNLTS PKGTAEIVCD
     DIQGGIGVDC VSDESVTR
 
 
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