PMEA_DICD3
ID PMEA_DICD3 Reviewed; 366 AA.
AC P0C1A9; E0SAZ5; P07863;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Pectinesterase A;
DE Short=PE A;
DE EC=3.1.1.11 {ECO:0000269|PubMed:8370537};
DE AltName: Full=Pectin methylesterase A;
DE Short=PME {ECO:0000303|PubMed:8370537};
DE Flags: Precursor;
GN Name=pemA {ECO:0000303|PubMed:21217001};
GN Synonyms=pem {ECO:0000303|PubMed:8370537}; OrderedLocusNames=Dda3937_03374;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-34, FUNCTION,
RP CATALYTIC ACTIVITY, PROBABLE PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=3937;
RX PubMed=8370537; DOI=10.1016/0378-1119(93)90664-o;
RA Laurent F., Kotoujansky A., Labesse G., Bertheau Y.;
RT "Characterization and overexpression of the pem gene encoding pectin
RT methylesterase of Erwinia chrysanthemi strain 3937.";
RL Gene 131:17-25(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=3937;
RX PubMed=8830237; DOI=10.1046/j.1365-2958.1996.389922.x;
RA Shevchik V.E., Condemine G., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Characterization of pectin methylesterase B, an outer membrane lipoprotein
RT of Erwinia chrysanthemi 3937.";
RL Mol. Microbiol. 19:455-466(1996).
RN [4] {ECO:0007744|PDB:2NSP, ECO:0007744|PDB:2NST, ECO:0007744|PDB:2NT6, ECO:0007744|PDB:2NT9, ECO:0007744|PDB:2NTB, ECO:0007744|PDB:2NTP, ECO:0007744|PDB:2NTQ}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-366 IN COMPLEXES WITH
RP SUBSTRATES AND PRODUCT, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, REACTION
RP MECHANISM, PROBABLE PATHWAY, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF
RP GLN-153; GLN-177; ASP-178; VAL-198; ASP-199; ARG-267; TRP-269; THR-272 AND
RP MET-306.
RC STRAIN=3937;
RX PubMed=17717531; DOI=10.1038/sj.emboj.7601816;
RA Fries M., Ihrig J., Brocklehurst K., Shevchik V.E., Pickersgill R.W.;
RT "Molecular basis of the activity of the phytopathogen pectin
RT methylesterase.";
RL EMBO J. 26:3879-3887(2007).
CC -!- FUNCTION: Catalyzes the first step in maceration and soft-rotting of
CC plant tissue. {ECO:0000305|PubMed:17717531,
CC ECO:0000305|PubMed:8370537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC Evidence={ECO:0000269|PubMed:17717531, ECO:0000269|PubMed:8370537};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000305|PubMed:17717531,
CC ECO:0000305|PubMed:8370537}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17717531,
CC ECO:0000269|PubMed:8370537}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8370537}. Note=Upon
CC overexpression also accumulates in the periplasm.
CC {ECO:0000269|PubMed:8370537}.
CC -!- DISRUPTION PHENOTYPE: Decreased growth on methylated oligogalacturides;
CC double pemA-pemB deletions grow very poorly on methylated
CC oligogalacturides. {ECO:0000269|PubMed:8830237}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; L07644; AAA24852.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM99554.1; -; Genomic_DNA.
DR PIR; JN0799; JN0799.
DR RefSeq; WP_013318985.1; NC_014500.1.
DR PDB; 2NSP; X-ray; 1.70 A; A/B=25-366.
DR PDB; 2NST; X-ray; 1.70 A; A/B=25-366.
DR PDB; 2NT6; X-ray; 1.70 A; A/B=25-366.
DR PDB; 2NT9; X-ray; 1.90 A; A/B=25-366.
DR PDB; 2NTB; X-ray; 1.80 A; A/B=25-366.
DR PDB; 2NTP; X-ray; 1.70 A; A/B=25-366.
DR PDB; 2NTQ; X-ray; 1.80 A; A/B=25-366.
DR PDBsum; 2NSP; -.
DR PDBsum; 2NST; -.
DR PDBsum; 2NT6; -.
DR PDBsum; 2NT9; -.
DR PDBsum; 2NTB; -.
DR PDBsum; 2NTP; -.
DR PDBsum; 2NTQ; -.
DR AlphaFoldDB; P0C1A9; -.
DR SMR; P0C1A9; -.
DR STRING; 198628.Dda3937_03374; -.
DR EnsemblBacteria; ADM99554; ADM99554; Dda3937_03374.
DR GeneID; 9734805; -.
DR KEGG; ddd:Dda3937_03374; -.
DR PATRIC; fig|198628.6.peg.3312; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_012243_3_1_6; -.
DR OMA; NRVAWCR; -.
DR OrthoDB; 1095798at2; -.
DR BioCyc; DDAD198628:DDA3937_RS15630-MON; -.
DR BioCyc; MetaCyc:MON-15656; -.
DR UniPathway; UPA00545; UER00823.
DR EvolutionaryTrace; P0C1A9; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0005615; C:extracellular space; IDA:ASAP.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IDA:ASAP.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl esterase; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8370537"
FT CHAIN 25..366
FT /note="Pectinesterase A"
FT /id="PRO_0000233033"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:17717531"
FT ACT_SITE 199
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17717531"
FT SITE 177
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:17717531"
FT DISULFID 192..212
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 153
FT /note="Q->A: Strong decrease in affinity for substrate."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 177
FT /note="Q->A: Strong decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 178
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 198
FT /note="V->A: Strong decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 199
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 267
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 269
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 272
FT /note="T->A: Decreases affinity for substrate."
FT /evidence="ECO:0000269|PubMed:17717531"
FT MUTAGEN 306
FT /note="M->A: Strong decrease in catalytic activity.
FT Decreases affinity for substrate."
FT /evidence="ECO:0000269|PubMed:17717531"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2NSP"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 193..211
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2NSP"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:2NSP"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:2NSP"
SQ SEQUENCE 366 AA; 39373 MW; C67C1A4D2C04735F CRC64;
MLKTISGTLA LSLIIAASVH QAQAATTYNA VVSKSSSDGK TFKTIADAIA SAPAGSTPFV
ILIKNGVYNE RLTITRNNLH LKGESRNGAV IAAATAAGTL KSDGSKWGTA GSSTITISAK
DFSAQSLTIR NDFDFPANQA KSDSDSSKIK DTQAVALYVT KSGDRAYFKD VSLVGYQDTL
YVSGGRSFFS DCRISGTVDF IFGDGTALFN NCDLVSRYRA DVKSGNVSGY LTAPSTNINQ
KYGLVITNSR VIRESDSVPA KSYGLGRPWH PTTTFSDGRY ADPNAIGQTV FLNTSMDNHI
YGWDKMSGKD KNGNTIWFNP EDSRFFEYKS YGAGATVSKD RRQLTDAQAA EYTQSKVLGD
WTPTLP
