PLYA_DICCH
ID PLYA_DICCH Reviewed; 393 AA.
AC P0C1A2; P29155;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Pectate lyase A;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN Name=pelA;
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].
RC STRAIN=EC16;
RX PubMed=3042750; DOI=10.1128/jb.170.8.3468-3478.1988;
RA Tamaki S.J., Gold S., Robeson M., Manulis S., Keen N.T.;
RT "Structure and organization of the pel genes from Erwinia chrysanthemi
RT EC16.";
RL J. Bacteriol. 170:3468-3478(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-393.
RX PubMed=12037303; DOI=10.1107/s0907444902005851;
RA Thomas L.M., Doan C.N., Oliver R.L., Yoder M.D.;
RT "Structure of pectate lyase A: comparison to other isoforms.";
RL Acta Crystallogr. D 58:1008-1015(2002).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLADES
CC subfamily. {ECO:0000305}.
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DR EMBL; M14509; AAA24843.1; -; Genomic_DNA.
DR PIR; B31091; WZWC6A.
DR PDB; 1JRG; X-ray; 2.10 A; A/B=33-393.
DR PDB; 1JTA; X-ray; 1.80 A; A=33-393.
DR PDB; 1OOC; X-ray; 2.94 A; A/B=33-393.
DR PDB; 1PE9; X-ray; 1.60 A; A/B=33-393.
DR PDBsum; 1JRG; -.
DR PDBsum; 1JTA; -.
DR PDBsum; 1OOC; -.
DR PDBsum; 1PE9; -.
DR AlphaFoldDB; P0C1A2; -.
DR SMR; P0C1A2; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR BRENDA; 4.2.2.2; 2141.
DR UniPathway; UPA00545; UER00824.
DR EvolutionaryTrace; P0C1A2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Calcium; Disulfide bond; Lyase; Metal-binding; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..393
FT /note="Pectate lyase A"
FT /id="PRO_0000024852"
FT ACT_SITE 273
FT /evidence="ECO:0000255"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 330..358
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1PE9"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1PE9"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1PE9"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1PE9"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1OOC"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1OOC"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:1PE9"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1PE9"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1JRG"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:1PE9"
SQ SEQUENCE 393 AA; 42080 MW; 20025C904FD7B345 CRC64;
MMNKASGRSF TRSSKYLLAT LIAGMMASGV SAAELVSDKA LESAPTVGWA SQNGFTTGGA
AATSDNIYIV TNISEFTSAL SAGAEAKIIQ IKGTIDISGG TPYTDFADQK ARSQINIPAN
TTVIGLGTDA KFINGSLIID GTDGTNNVII RNVYIQTPID VEPHYEKGDG WNAEWDAMNI
TNGAHHVWID HVTISDGNFT DDMYTTKDGE TYVQHDGALD IKRGSDYVTI SNSLIDQHDK
TMLIGHNDTN SAQDKGKLHV TLFNNVFNRV TERAPRVRYG SIHSFNNVFK GDAKDPVYRY
QYSFGIGTSG SVLSEGNSFT IANLSASKAC KVVKKFNGSI FSDNGSVLNG SAVDLSGCGF
SAYTSKIPYI YDVQPMTTEL AQSITDNAGS GKL
