ID   PGLR1_PECCC             Reviewed;         402 AA.
AC   P18192; Q08933; Q47464;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Endo-polygalacturonase;
DE            EC=3.2.1.15;
DE   Flags: Precursor;
GN   Name=peh; Synonyms=peh-1, peh1;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=2215211; DOI=10.1111/j.1365-2958.1990.tb00675.x;
RA   Hinton J.C.D., Gill D.R., Lalo D., Plastow G.S., Salmond G.P.C.;
RT   "Sequence of the peh gene of Erwinia carotovora: homology between Erwinia
RT   and plant enzymes.";
RL   Mol. Microbiol. 4:1029-1036(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=71;
RX   PubMed=8074530; DOI=10.1128/aem.60.7.2545-2552.1994;
RA   Liu Y., Chatterjee A., Chatterjee A.K.;
RT   "Nucleotide sequence and expression of a novel pectate lyase gene (pel-3)
RT   and a closely linked endopolygalacturonase gene (peh-1) of Erwinia
RT   carotovora subsp. carotovora 71.";
RL   Appl. Environ. Microbiol. 60:2545-2552(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=71;
RX   PubMed=8407675; DOI=10.1111/j.1365-2672.1993.tb02760.x;
RA   Laing E., Pretorius I.S.;
RT   "A note on the primary structure and expression of an Erwinia carotovora
RT   polygalacturonase-encoding gene (peh1) in Escherichia coli and
RT   Saccharomyces cerevisiae.";
RL   J. Appl. Bacteriol. 75:149-158(1993).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; X52944; CAA37119.1; -; Genomic_DNA.
DR   EMBL; L32172; AAA57139.1; -; Genomic_DNA.
DR   EMBL; M83222; AAA03624.1; -; Unassigned_RNA.
DR   PIR; S11773; S11773.
DR   RefSeq; WP_039543807.1; NZ_VBUA01000013.1.
DR   AlphaFoldDB; P18192; -.
DR   SMR; P18192; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   PATRIC; fig|555.16.peg.2200; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
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; 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; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..402
FT                   /note="Endo-polygalacturonase"
FT                   /id="PRO_0000024758"
FT   ACT_SITE        249
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   VARIANT         37
FT                   /note="A -> T (in strain: 71)"
FT   VARIANT         297
FT                   /note="I -> V (in strain: 71)"
FT   VARIANT         399
FT                   /note="T -> N (in strain: 71)"
FT   CONFLICT        396
FT                   /note="K -> N (in Ref. 2; AAA57139)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  42634 MW;  2D37097DF1AE4916 CRC64;
     MEYQSGKRVL SLSLGLIGLF SASAFASDSR TVSEPKAPSS CTVLKADSST ATSTIQKALN
     NCGQGKAVKL SAGSSSVFLS GPLSLPSGVS LLIDKGVTLR AVNNAKSFEN APSSCGVVDT
     NGKGCDAFIT ATSTTNSGIY GPGTIDGQGG VKLQDKKVSW WDLAADAKVK KLKQNTPRLI
     QINKSKNFTL YNVSLINSPN FHVVFSDGDG FTAWKTTIKT PSTARNTDGI DPMSSKNITI
     AHSNISTGDD NVAIKAYKGR SETRNISILH NEFGTGHGMS IGSETMGVYN VTVDDLIMTG
     TTNGLRIKSD KSAAGVVNGV RYSNVVMKNV AKPIVIDTVY EKKEGSNVPD WSDITFKDIT
     SQTKGVVVLN GENAKKPIEV TMKNVKLTSD STWQIKNVTV KK