ID   PEHX_DICCH              Reviewed;         602 AA.
AC   P15922;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Exo-poly-alpha-D-galacturonosidase;
DE            Short=Exo-PG;
DE            EC=3.2.1.82 {ECO:0000269|PubMed:2168372};
DE   Flags: Precursor;
GN   Name=pehX;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-40, SUBCELLULAR
RP   LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=EC16;
RX   PubMed=2168372; DOI=10.1128/jb.172.9.4988-4995.1990;
RA   He S.Y., Collmer A.;
RT   "Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of
RT   the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia
RT   chrysanthemi EC16.";
RL   J. Bacteriol. 172:4988-4995(1990).
RN   [2]
RP   DOMAIN FIBRONECTIN TYPE-III.
RX   PubMed=1409594; DOI=10.1073/pnas.89.19.8990;
RA   Bork P., Doolittle R.F.;
RT   "Proposed acquisition of an animal protein domain by bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8990-8994(1992).
CC   -!- FUNCTION: Contributes significantly to bacterial utilization of
CC       polygalacturonate and the induction of pectate lyase in the presence of
CC       extracellular pectic polymers. {ECO:0000269|PubMed:2168372}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC         galacturonosyl](n-2) + alpha-D-galacturonosyl-(1->4)-D-galacturonate;
CC         Xref=Rhea:RHEA:56232, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14734,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:140523, ChEBI:CHEBI:141004;
CC         EC=3.2.1.82; Evidence={ECO:0000269|PubMed:2168372};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2168372}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; M31308; AAA24842.1; -; Genomic_DNA.
DR   PIR; A36715; A36715.
DR   RefSeq; WP_039999104.1; NZ_JAFCAF010000013.1.
DR   AlphaFoldDB; P15922; -.
DR   SMR; P15922; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   BioCyc; MetaCyc:MON-15662; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033917; F:exo-poly-alpha-galacturonosidase 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   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.160.20.10; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:2168372"
FT   CHAIN           28..602
FT                   /note="Exo-poly-alpha-D-galacturonosidase"
FT                   /id="PRO_0000024824"
FT   DOMAIN          32..149
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   ACT_SITE        395
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
SQ   SEQUENCE   602 AA;  64444 MW;  C7F44689C343B34B CRC64;
     MKVITFSRRS ALASIVATCL MSTPALAATA QAPQKLQIPT LSYDDHSVML VWDTPEDTSN
     ITDYQIYQNG QLIGLASQNN DKNSPAKPYI SAFYKSDAAN FHHRIVLQNA KVDGLKAGTD
     YQFTVRTVYA DGTTSNDSNT VTTTTTAVPK VINITQYGAK GDGTTLNTSA IQKAIDACPT
     GCRIDVPAGV FKTGALWLKS DMTLNLLQGA TLLGSDNAAD YPDAYKIYSY VSQVRPASLL
     NAIDKNSSAV GTFKNIRIVG KGIIDGNGWK RSADAKDELG NTLPQYVKSD NSKVSKDGIL
     AKNQVAAAVA TGMDTKTAYS QRRSSLVTLR GVQNAYIADV TIRNPANHGI MFLESENVVE
     NSVIHQTFNA NNGDGVEFGN SQNIMVFNSV FDTGDDSINF AAGMGQDAQK QEPSQNAWLF
     NNFFRHGHGA VVLGSHTGAG IVDVLAENNV ITQNDVGLRA KSAPAIGGGA HGIVFRNSAM
     KNLAKQAVIV TLSYADNNGT IDYTPAKVPA RFYDFTVKNV TVQDSTGSNP AIEITGDSSK
     DIWHSQFIFS NMKLSGVSPT SISDLSDSQF NNLTFSNLRS GSSPWKFGTV KNVTVDGKTV
     TP