PLYX_DICCH
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 03-AUG-2022, entry version 75.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 PRIDE; P22751; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047489; F:pectate disaccharide-lyase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF13229; Beta_helix; 1.
DR SUPFAM; SSF51126; SSF51126; 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