ID   PELD_PECCA              Reviewed;         314 AA.
AC   P24112;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Pectin lyase;
DE            EC=4.2.2.10;
GN   Name=pnl;
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Er;
RX   PubMed=2018526; DOI=10.1016/0006-291x(91)90927-y;
RA   Ohnishi H., Nishida T., Yoshida A., Kamio Y., Izaki K.;
RT   "Nucleotide sequence of pnl gene from Erwinia carotovora Er.";
RL   Biochem. Biophys. Res. Commun. 176:321-327(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-18.
RC   STRAIN=Er;
RX   PubMed=2185758; DOI=10.1016/0006-291x(90)92392-d;
RA   Nishida T., Suzuki T., Ito K., Kamio Y., Izaki K.;
RT   "Cloning and expression of pectin lyase gene from Erwinia carotovora in
RT   Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 168:801-808(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX   PubMed=7764549; DOI=10.1271/bbb.58.432;
RA   Ohnishi H., Nikaidou N., Kamio Y., Izaki K.;
RT   "Analysis of promoter region of the pectin lyase gene from Erwinia
RT   carotovora Er.";
RL   Biosci. Biotechnol. Biochem. 58:432-433(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC   -!- INDUCTION: By DNA-damaging agents such as nalidixic acid, mitomycin C
CC       or UV light.
CC   -!- MISCELLANEOUS: In most stains, pnl production is accompanied by cell
CC       lysis and production of a bacteriocin.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; M65057; AAA24857.1; -; Genomic_DNA.
DR   PIR; JH0389; JH0389.
DR   AlphaFoldDB; P24112; -.
DR   SMR; P24112; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0047490; F:pectin lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase.
FT   CHAIN           1..314
FT                   /note="Pectin lyase"
FT                   /id="PRO_0000212995"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   314 AA;  33709 MW;  D94769EA15DB4DE1 CRC64;
     MAYPTTNLTG LIGFAKAAKV TGGTGGKVVT VNSLADFKSA VSGSAKTIVV LGSSLKTSAL
     TKVVFGSNKT IVGSFGGANV LTNIHLRAES NSSNVIFQNL VFKHDVAIKD NDDIQLYLNY
     GKGYWVDHCS WPGHTWSDND GSLDKLIYIG EKADYITISN CLFSNHKYGC IFGHPADDNN
     SAYNGYPRLT ICHNYYENIQ VRAPGLMRYG YFHVFNNYVN KFQLAFTVAQ NANVISERNV
     FGSGAEKKGM VDDKGNGSTF TDNGSSPAAV ASKSPAAKWT ASSNYSYSLM TTAAAQSWVV
     SNAGAQNSAL KFPS