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PGLR_PENJA
ID   PGLR_PENJA              Reviewed;         371 AA.
AC   O42824;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 7719;
RA   Ishida Y., Kakibuchi K., Hirao Y., Izumori K.;
RT   "Cloning and characterization of a polygalacturonase-encoding gene from
RT   Penicillium janthinellum.";
RL   J. Ferment. Bioeng. 84:257-260(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC         galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; D79980; BAA24524.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42824; -.
DR   SMR; O42824; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
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; 7.
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; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..34
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024790"
FT   CHAIN           35..371
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024791"
FT   REPEAT          95..117
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          165..195
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          196..217
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          218..238
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          247..268
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          276..298
FT                   /note="PbH1 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          310..355
FT                   /note="PbH1 7"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        38..53
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        212..228
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        338..343
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        362..371
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   371 AA;  38327 MW;  9E3AD97A1BD2BED5 CRC64;
     MPSYLRNLVW ATLAAGLVSA APTPSRVSDL TKKSSSTCTF SSAASASASK SSCSTIVLSN
     IEVPAGKTLD LTDLKDGTKV IFEGTTTFGY KEWSGPLIKI SGSDITVEAA DGAVINADGS
     RWWDGEGTNG GKTKPKFFYA HSLDDSTISG LNIKNTPVQA FSIQSDNLII DGVTIDNSDG
     DENGGHNTDG FDISESTGVT IRNAVVKNQD DCIAINSGQN IYFTGGTCSG GHGLSIGSVG
     GRDDNTVKNV TITDSTVTDS ANGVRIKTVY DATGSVSDVT FSDITVSGIT DYGIVIEQDY
     ENGSPTGTPT SGVPITDLTV KGITGSVESD AVEVYILCGD DACSDWTWSG VDITSGQTSS
     KCENVPSGAS C
 
 
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