UniProtKB - P0C1A9 (PMEA_DICD3)

BLAST

>sp|P0C1A9|PMEA_DICD3 Pectinesterase A OS=Dickeya dadantii (strain 3937) OX=198628 GN=pemA PE=1 SV=1
MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFV
ILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAK
DFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTL
YVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQ
KYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHI
YGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGD
WTPTLP

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History
Entry version 65 (20 Jun 2018)
Sequence version 1 (18 Apr 2006)
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Protein

Pectinesterase A

Gene

pemA

Organism

Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in maceration and soft-rotting of plant tissue.

Catalytic activityⁱ

Pectin + n H₂O = n methanol + pectate.

Pathwayⁱ: pectin degradation

This protein is involved in step 1 of the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:

This subpathway is part of the pathway pectin degradation, which is itself part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin, the pathway pectin degradation and in Glycan metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	109	Substrate	1
Binding siteⁱ	153	Substrate	1
Siteⁱ	177	Transition state stabilizer	1
Active siteⁱ	178	Proton donor	1
Active siteⁱ	199	Nucleophile	1
Binding siteⁱ	219	Substrate	1
Binding siteⁱ	226	Substrate	1
Binding siteⁱ	230	Substrate	1
Binding siteⁱ	267	Substrate	1
Binding siteⁱ	269	Substrate	1
Binding siteⁱ	272	Substrate; via amide nitrogen and carbonyl oxygen	1

GO - Molecular functionⁱ

aspartyl esterase activity Source: UniProtKB-KW
pectinesterase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell wall modification Source: InterPro
pectin catabolic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Aspartyl esterase, Hydrolase
Biological process	Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCycⁱ	DDAD198628:DDA3937_RS15630-MONOMER MetaCyc:MONOMER-15656
UniPathwayⁱ	UPA00545;UER00823

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Pectinesterase A (EC:3.1.1.11) Short name: PE A Alternative name(s): Pectin methylesterase A
Gene namesⁱ	Name:pemA Synonyms:pem Ordered Locus Names:Dda3937_03374
Organismⁱ	Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Taxonomic identifierⁱ	198628 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Pectobacteriaceae › Dickeya › Dickeya dadantii
Proteomesⁱ	UP000006859 Componentⁱ: Chromosome

Subcellular locationⁱ

Secreted

GO - Cellular componentⁱ

cell wall Source: InterPro
extracellular region Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	153	Q → A: Strong decrease in affinity for substrate. 1 Publication	1
Mutagenesisⁱ	177	Q → A: Strong decrease in catalytic activity. 1 Publication	1
Mutagenesisⁱ	178	D → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	198	V → A: Strong decrease in catalytic activity. 1 Publication	1
Mutagenesisⁱ	199	D → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	267	R → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	269	W → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	272	T → A: Decreases affinity for substrate. 1 Publication	1
Mutagenesisⁱ	306	M → A: Strong decrease in catalytic activity. Decreases affinity for substrate. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 24	By similarityAdd BLAST		24
ChainⁱPRO_0000233033	25 – 366	Pectinesterase AAdd BLAST		342

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	192 ↔ 212	1 Publication

Keywords - PTMⁱ

Disulfide bond

Interactionⁱ

Subunit structureⁱ

Monomer.

Protein-protein interaction databases

STRINGⁱ	198628.Dda3937_03374

STRINGⁱ

198628.Dda3937_03374

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	29 – 32	Combined sources	4
Beta strandⁱ	36 – 38	Combined sources	3
Beta strandⁱ	42 – 44	Combined sources	3
Helixⁱ	45 – 50	Combined sources	6
Beta strandⁱ	54 – 57	Combined sources	4
Beta strandⁱ	59 – 63	Combined sources	5
Beta strandⁱ	65 – 69	Combined sources	5
Beta strandⁱ	72 – 74	Combined sources	3
Beta strandⁱ	79 – 84	Combined sources	6
Turnⁱ	86 – 88	Combined sources	3
Beta strandⁱ	89 – 93	Combined sources	5
Helixⁱ	108 – 111	Combined sources	4
Beta strandⁱ	114 – 117	Combined sources	4
Beta strandⁱ	119 – 121	Combined sources	3
Beta strandⁱ	123 – 131	Combined sources	9
Helixⁱ	135 – 140	Combined sources	6
Beta strandⁱ	156 – 159	Combined sources	4
Beta strandⁱ	164 – 174	Combined sources	11
Beta strandⁱ	180 – 182	Combined sources	3
Beta strandⁱ	184 – 191	Combined sources	8
Beta strandⁱ	193 – 211	Combined sources	19
Beta strandⁱ	213 – 216	Combined sources	4
Beta strandⁱ	229 – 234	Combined sources	6
Beta strandⁱ	244 – 248	Combined sources	5
Beta strandⁱ	250 – 255	Combined sources	6
Beta strandⁱ	263 – 266	Combined sources	4
Beta strandⁱ	272 – 275	Combined sources	4
Beta strandⁱ	278 – 281	Combined sources	4
Beta strandⁱ	288 – 293	Combined sources	6
Beta strandⁱ	300 – 302	Combined sources	3
Beta strandⁱ	306 – 309	Combined sources	4
Beta strandⁱ	315 – 318	Combined sources	4
Helixⁱ	320 – 322	Combined sources	3
Beta strandⁱ	323 – 329	Combined sources	7
Helixⁱ	346 – 349	Combined sources	4
Helixⁱ	350 – 352	Combined sources	3
Helixⁱ	354 – 358	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P0C1A9
SMRⁱ	P0C1A9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P0C1A9

EvolutionaryTraceⁱ

P0C1A9

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the pectinesterase family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG4105NBR Bacteria COG4677 LUCA
HOGENOMⁱ	HOG000217409
KEGG Orthology (KO) More...KOⁱ	K01051
OMAⁱ	NRVAWCR
Database of Orthologous Groups More...OrthoDBⁱ	POG091H0DD6

Family and domain databases

Gene3Dⁱ	2.160.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR012334 Pectin_lyas_fold IPR011050 Pectin_lyase_fold/virulence IPR033131 Pectinesterase_Asp_AS IPR000070 Pectinesterase_cat
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01095 Pectinesterase, 1 hit
SUPFAMⁱ	SSF51126 SSF51126, 1 hit
PROSITEⁱ	View protein in PROSITE PS00503 PECTINESTERASE_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0C1A9-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MLKTISGTLA LSLIIAASVH QAQAATTYNA VVSKSSSDGK TFKTIADAIA 
        60         70         80         90        100
SAPAGSTPFV ILIKNGVYNE RLTITRNNLH LKGESRNGAV IAAATAAGTL 
       110        120        130        140        150
KSDGSKWGTA GSSTITISAK DFSAQSLTIR NDFDFPANQA KSDSDSSKIK 
       160        170        180        190        200
DTQAVALYVT KSGDRAYFKD VSLVGYQDTL YVSGGRSFFS DCRISGTVDF 
       210        220        230        240        250
IFGDGTALFN NCDLVSRYRA DVKSGNVSGY LTAPSTNINQ KYGLVITNSR 
       260        270        280        290        300
VIRESDSVPA KSYGLGRPWH PTTTFSDGRY ADPNAIGQTV FLNTSMDNHI 
       310        320        330        340        350
YGWDKMSGKD KNGNTIWFNP EDSRFFEYKS YGAGATVSKD RRQLTDAQAA 
       360 
EYTQSKVLGD WTPTLP

Length:366

Mass (Da):39,373

Last modified:April 18, 2006 - v1

Checksum:ⁱC67C1A4D2C04735F

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L07644 Genomic DNA Translation: AAA24852.1 CP002038 Genomic DNA Translation: ADM99554.1
PIRⁱ	JN0799
NCBI Reference Sequences More...RefSeqⁱ	WP_013318985.1, NC_014500.1

Genome annotation databases

EnsemblBacteriaⁱ	ADM99554; ADM99554; Dda3937_03374
GeneIDⁱ	9734805
KEGGⁱ	ddd:Dda3937_03374
PATRICⁱ	fig\|198628.6.peg.3312

Protein	Similar proteins		Species	Score	Length	Source
P0C1A9	Pectinesterase A	)	DICCH		366	UniRef90_P0C1A9
Pectinesterase		Dickeya sp. DCE-01		368
Pectinesterase (Fragment)		DICDA		366
Pectinesterase		Dickeya fangzhongdai		366
Pectinesterase		DICC1		366
+19

Protein	Similar proteins		Species	Score	Length	Source
P0C1A9	Pectinesterase A	)	DICCH		366	UniRef50_P0C1A9
Pectinesterase		Dickeya sp. DCE-01		368
Pectinesterase (Fragment)		DICDA		366
Pectinesterase		Dickeya solani RNS 08.23.3.1.A		366
Pectinesterase		Dickeya fangzhongdai		366
+186

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L07644 Genomic DNA Translation: AAA24852.1 CP002038 Genomic DNA Translation: ADM99554.1
PIRⁱ	JN0799
RefSeqⁱ	WP_013318985.1, NC_014500.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2NSP	X-ray	1.70	A/B	25-366	[»]
	2NST	X-ray	1.70	A/B	25-366	[»]
	2NT6	X-ray	1.70	A/B	25-366	[»]
	2NT9	X-ray	1.90	A/B	25-366	[»]
	2NTB	X-ray	1.80	A/B	25-366	[»]
	2NTP	X-ray	1.70	A/B	25-366	[»]
	2NTQ	X-ray	1.80	A/B	25-366	[»]
ProteinModelPortalⁱ	P0C1A9
SMRⁱ	P0C1A9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	198628.Dda3937_03374

STRINGⁱ

198628.Dda3937_03374

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ADM99554; ADM99554; Dda3937_03374
GeneIDⁱ	9734805
KEGGⁱ	ddd:Dda3937_03374
PATRICⁱ	fig\|198628.6.peg.3312

Phylogenomic databases

eggNOGⁱ	ENOG4105NBR Bacteria COG4677 LUCA
HOGENOMⁱ	HOG000217409
KOⁱ	K01051
OMAⁱ	NRVAWCR
OrthoDBⁱ	POG091H0DD6

Enzyme and pathway databases

UniPathwayⁱ	UPA00545;UER00823
BioCycⁱ	DDAD198628:DDA3937_RS15630-MONOMER MetaCyc:MONOMER-15656

Miscellaneous databases

EvolutionaryTraceⁱ	P0C1A9

EvolutionaryTraceⁱ

P0C1A9

Family and domain databases

Gene3Dⁱ	2.160.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR012334 Pectin_lyas_fold IPR011050 Pectin_lyase_fold/virulence IPR033131 Pectinesterase_Asp_AS IPR000070 Pectinesterase_cat
Pfamⁱ	View protein in Pfam PF01095 Pectinesterase, 1 hit
SUPFAMⁱ	SSF51126 SSF51126, 1 hit
PROSITEⁱ	View protein in PROSITE PS00503 PECTINESTERASE_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PMEA_DICD3
Accessionⁱ	P0C1A9Primary (citable) accession number: P0C1A9 Secondary accession number(s): E0SAZ5, P07863
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
	Last sequence update:	April 18, 2006
	Last modified:	June 20, 2018
	This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0C1A9 (PMEA_DICD3)

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Pectinesterase A

pemA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: pectin degradation

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: pectin degradation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ