PMEA_DICCH
ID PMEA_DICCH Reviewed; 366 AA.
AC P0C1A8; P07863;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Pectinesterase A;
DE Short=PE A;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase A;
DE Flags: Precursor;
GN Name=pemA; Synonyms=pem;
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=B374;
RX PubMed=2837615; DOI=10.1111/j.1365-2958.1988.tb00026.x;
RA Plastow G.S.;
RT "Molecular cloning and nucleotide sequence of the pectin methyl esterase
RT gene of Erwinia chrysanthemi B374.";
RL Mol. Microbiol. 2:247-254(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 25-366.
RC STRAIN=B374;
RX PubMed=11162105; DOI=10.1006/jmbi.2000.4324;
RA Jenkins J., Mayans O., Smith D., Worboys K., Pickersgill R.W.;
RT "Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase
RT reveals a novel esterase active site.";
RL J. Mol. Biol. 305:951-960(2001).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; Y00549; CAA68628.1; -; Genomic_DNA.
DR PIR; S03770; S03770.
DR PDB; 1QJV; X-ray; 2.37 A; A/B=25-366.
DR PDBsum; 1QJV; -.
DR AlphaFoldDB; P0C1A8; -.
DR SMR; P0C1A8; -.
DR BRENDA; 3.1.1.11; 2141.
DR SABIO-RK; P0C1A8; -.
DR UniPathway; UPA00545; UER00823.
DR EvolutionaryTrace; P0C1A8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
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 Disulfide bond; Hydrolase; Secreted; Signal.
FT SIGNAL 1..24
FT CHAIN 25..366
FT /note="Pectinesterase A"
FT /id="PRO_0000023498"
FT ACT_SITE 178
FT /note="Proton donor"
FT ACT_SITE 199
FT /note="Nucleophile"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 177
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 192..212
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1QJV"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 193..211
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:1QJV"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1QJV"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:1QJV"
SQ SEQUENCE 366 AA; 39319 MW; DA7DD9A45290660B CRC64;
MLKTISGTLA LSLIIAASVH QAQAATTYNA VVSKSSSDGK TFKTIADAIA SAPAGSTPFV
ILIKNGVYNE RLTITRNNLL 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 YGAGAAVSKD RRQLTDAQAA EYTQSKVLGD
WTPTLP
