ID   PLYX_DICCH              Reviewed;         749 AA.
AC   P22751;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   04-NOV-2026, entry version 87.
DE   RecName: Full=Pectate disaccharide-lyase {ECO:0000305};
DE            EC=4.2.2.9 {ECO:0000269|PubMed:2254266};
DE   AltName: Full=Exopolygalacturonate lyase {ECO:0000303|PubMed:2254266};
DE            Short=ExoPL {ECO:0000303|PubMed:2254266};
DE   Flags: Precursor;
GN   Name=pelX {ECO:0000303|PubMed:2254266};
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-46, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND DISRUPTION PHENOTYPE.
RC   STRAIN=EC16;
RX   PubMed=2254266; DOI=10.1128/jb.172.12.6950-6958.1990;
RA   Brooks A.D., Yang He S., Gold S., Keen N.T., Collmer A., Hutcheson S.W.;
RT   "Molecular cloning of the structural gene for exopolygalacturonate lyase
RT   from Erwinia chrysanthemi EC16 and characterization of the enzyme
RT   product.";
RL   J. Bacteriol. 172:6950-6958(1990).
CC   -!- FUNCTION: Exo-cleaving lyase that catalyzes the digestion of pectate.
CC       Contributes to pectate catabolism but not to bacterial virulence. In
CC       vitro can also use citrus pectin and highly methyl-esterified Link
CC       pectin as substrates. {ECO:0000269|PubMed:2254266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl](n) = 4-(4-deoxy-alpha-D-
CC         galact-4-enuronosyl)-D-galacturonate + [(1->4)-alpha-D-
CC         galacturonosyl](n-2); Xref=Rhea:RHEA:57104, Rhea:RHEA-COMP:14570,
CC         Rhea:RHEA-COMP:14734, ChEBI:CHEBI:60189, ChEBI:CHEBI:140523;
CC         EC=4.2.2.9; Evidence={ECO:0000269|PubMed:2254266};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000305|PubMed:2254266};
CC   -!- ACTIVITY REGULATION: Activity on pectate is nearly completely inhibited
CC       by ethyleneglycol-bis-(P-aminoethyl ether) N,N'-tetraacetic acid
CC       (EGTA), EDTA or nitrilotriacetic acid. Activity is specifically
CC       restored by the addition of Ca(2+). {ECO:0000269|PubMed:2254266}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:2254266};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C1A7}.
CC   -!- DISRUPTION PHENOTYPE: Mutant exhibits reduced growth on pectate, but
CC       retains pathogenicity on chrysanthemum. {ECO:0000269|PubMed:2254266}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC       {ECO:0000305}.
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DR   EMBL; M62739; AAA24850.1; -; Genomic_DNA.
DR   PIR; A37839; A37839.
DR   AlphaFoldDB; P22751; -.
DR   SMR; P22751; -.
DR   CAZy; PL9; Polysaccharide Lyase Family 9.
DR   OMA; AAPGNYF; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0047489; F:pectate disaccharide-lyase activity; EXP:UniProtKB.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR053868; Pel9A-like_beta_helix.
DR   InterPro; IPR058863; PelX-like_Ig.
DR   InterPro; IPR058953; PelX-like_N.
DR   InterPro; IPR052052; Polysaccharide_Lyase_9.
DR   PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR   PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR   Pfam; PF22842; Pel9A-like_beta_helix; 1.
DR   Pfam; PF25850; PelX_Ig; 1.
DR   Pfam; PF25849; PelX_N; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Lyase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:2254266"
FT   CHAIN           27..749
FT                   /note="Pectate disaccharide-lyase"
FT                   /id="PRO_0000024935"
FT   ACT_SITE        595
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT   BINDING         538
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT   BINDING         562
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT   BINDING         563
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT   BINDING         566
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1A7"
SQ   SEQUENCE   749 AA;  82240 MW;  449BB25C23F2A9B5 CRC64;
     MKYAASGLLS VALNSLLLLG SNQRFATQDV APVWRGIAFG QSTDVNFATN VLPEKVGVND
     VTINGKKLTV NDKADLSAPI TIESRGGKIA NTHDGLTFFY TQLPANVNFT LQSDVTVEQF
     GPESDAKPNA QEGAGLLVRD ILGVPRQEPL KEGYEEFPAA SNMVMNAIMT QDKKSKTEVK
     MQLISRNGVT QPWGNTNAEI TRTSYQEKIN LEQTPTFRLK LERTNDGFIT AYAPKGSDQW
     VSKTVKGADL VTHQDKDHYY VGFFASRNAK ITISNASLTT SPANTKPSAP FKAETTAPLL
     QVASSSLSTS DTYPVQARVN YNGTVEVFQN GKSLGKPQRV RAGDDFSLTT RLTQQKSDFK
     LVYIPSEGED KTAKETSFSV EKITLADARN LYVSPEGKAG NDGSKNAPLD IKTAINALPG
     GGTLWLMDGD YSATVIPVSA TQRKGMKTLM PVGKKAVFHG LQLNASYWKV KGIEITEKSF
     RIEGSHNQIE RLLAHHCDNT GIQVSSSDNV GRPLWASHNL ILNSESHSNQ HPSKKDADGF
     AVKMRVGEGN VIRGAFSHDN VDDGFDLFNK IEDGPNGAVM IENSISLNNT SNGFKLGGEG
     QPVAHQVKNS IAIGNHMDGF SDNFNPGALQ VSNNIALDNV RFNFIFRPSP YYGYEKQGIF
     KNNVSLRTQP GKYDDAVVGR LDASNYFIRI IERSTVRVRK SRRRITNPSR CQRSSAGMKK
     AACNWVIFCR RSNRHKTQRH RNRYPSTPA
//