PGLR2_PECPM
ID PGLR2_PECPM Reviewed; 402 AA.
AC P26509; K4FKA4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Endo-polygalacturonase;
DE EC=3.2.1.15 {ECO:0000269|PubMed:2215212};
DE Flags: Precursor;
GN Name=pehA; OrderedLocusNames=W5S_3318;
OS Pectobacterium parmentieri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=1905730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=SCC3193;
RX PubMed=2215212; DOI=10.1111/j.1365-2958.1990.tb00676.x;
RA Saarilahti H.T., Heino P., Pakkanen R., Kalkkinen N., Palva I., Palva E.T.;
RT "Structural analysis of the pehA gene and characterization of its protein
RT product, endopolygalacturonase, of Erwinia carotovora subspecies
RT carotovora.";
RL Mol. Microbiol. 4:1037-1044(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCC3193;
RX PubMed=23045508; DOI=10.1128/jb.00681-12;
RA Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P.,
RA Paulin L., Pirhonen M., Palva T., Holm L.;
RT "Genome sequence of Pectobacterium sp. strain SCC3193.";
RL J. Bacteriol. 194:6004-6004(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=9733763; DOI=10.1074/jbc.273.38.24660;
RA Pickersgill R., Smith D., Worboys K., Jenkins J.;
RT "Crystal structure of polygalacturonase from Erwinia carotovora ssp.
RT carotovora.";
RL J. Biol. Chem. 273:24660-24664(1998).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC {ECO:0000269|PubMed:2215212}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC Evidence={ECO:0000269|PubMed:2215212};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9733763}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2215212}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; X51701; CAA35998.1; -; Genomic_DNA.
DR EMBL; CP003415; AFI91392.1; -; Genomic_DNA.
DR PIR; S11772; S11772.
DR RefSeq; WP_014700877.1; NZ_QESW01000026.1.
DR PDB; 1BHE; X-ray; 1.90 A; A=27-402.
DR PDBsum; 1BHE; -.
DR AlphaFoldDB; P26509; -.
DR SMR; P26509; -.
DR STRING; 1905730.W5S_3318; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblBacteria; AFI91392; AFI91392; W5S_3318.
DR KEGG; pec:W5S_3318; -.
DR PATRIC; fig|1166016.3.peg.3378; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_016031_0_0_6; -.
DR OMA; EKRQFGE; -.
DR OrthoDB; 593041at2; -.
DR EvolutionaryTrace; P26509; -.
DR Proteomes; UP000008044; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..402
FT /note="Endo-polygalacturonase"
FT /id="PRO_0000024759"
FT ACT_SITE 249
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 277
FT /evidence="ECO:0000305"
FT DISULFID 41..62
FT DISULFID 115..125
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1BHE"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1BHE"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1BHE"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 263..273
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 279..300
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:1BHE"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 316..329
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 350..361
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:1BHE"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:1BHE"
SQ SEQUENCE 402 AA; 42853 MW; C1902D8C5388B6B5 CRC64;
MEYQSGKRVL SLSLGLIGLF SASAWASDSR TVSEPKTPSS CTTLKADSST ATSTIQKALN
NCDQGKAVRL SAGSTSVFLS GPLSLPSGVS LLIDKGVTLR AVNNAKSFEN APSSCGVVDK
NGKGCDAFIT AVSTTNSGIY GPGTIDGQGG VKLQDKKVSW WELAADAKVK KLKQNTPRLI
QINKSKNFTL YNVSLINSPN FHVVFSDGDG FTAWKTTIKT PSTARNTDGI DPMSSKNITI
AYSNIATGDD NVAIKAYKGR AETRNISILH NDFGTGHGMS IGSETMGVYN VTVDDLKMNG
TTNGLRIKSD KSAAGVVNGV RYSNVVMKNV AKPIVIDTVY EKKEGSNVPD WSDITFKDVT
SETKGVVVLN GENAKKPIEV TMKNVKLTSD STWQIKNVNV KK
