P17872 (PME_ASPTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase
Short name=PE
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase

Gene names

Name:

pme1

Organism

Aspergillus tubingensis

Taxonomic identifier

5068 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in maceration and soft-rotting of plant tissue.
Catalytic activity	Pectin + n H2O = n methanol + pectate.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular location	Secreted.
Sequence similarities	Belongs to the pectinesterase family.
Caution	Strain RH 5344 was previously said to be from A.niger.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell wall modification Inferred from electronic annotation. Source: InterPro pectin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cell wall Inferred from electronic annotation. Source: InterPro extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW pectinesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17
	Chain	18 – 331	314	Pectinesterase		PRO_0000023473
Sites
	Active site	161	1	Proton donor By similarity
	Active site	182	1	Nucleophile By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	247	1	Substrate By similarity
	Binding site	249	1	Substrate By similarity
	Site	160	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17872 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 25B52150884C797A	FASTA	331	35,715
	10 20 30 40 50 60 MVKSILASVL FAATALAASR MTAPSGAIVV AKSGGDYDTI SAAVDALSTT STETQTIFIE 70 80 90 100 110 120 EGSYDEQVYI PALSGKLIVY GQTEDTTTYT SNLVNITHAI ALADVDNDDE TATLRNYAEG 130 140 150 160 170 180 SAIYNLNIAN TCGQACHQAL AVSAYASEQG YYACQFTGYQ DTLLAETGYQ VYAGTYIEGA 190 200 210 220 230 240 VDFIFGQHAR AWFHECDIRV LEGPSSASIT ANGRSSESDD SYYVIHKSTV AAADGNDVSS 250 260 270 280 290 300 GTYYLGRPWS QYARVCFQKT SMTDVINHLG WTEWSTSTPN TENVTFVEYG NTGTGAEGPR 310 320 330 ANFSSELTEP ITISWLLGSD WEDWVDTSYI N

References

[1]	"Nucleotide and derived amino acid sequence of a pectinesterase cDNA isolated from Aspergillus niger strain RH 5344." Khanh N.Q., Albrecht H., Ruttkowski E., Loeffler F., Gottschalk M., Jany K.-D. Nucleic Acids Res. 18:4262-4262(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: RH 5344.
[2]	"Characterization and expression of a genomic pectin methyl esterase-encoding gene in Aspergillus niger." Khanh N.Q., Ruttkowski E., Leidinger K., Albrecht H., Gottschalk M. Gene 106:71-77(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52902 mRNA. Translation: CAA37084.1. X54145 Genomic DNA. Translation: CAA38084.1.
PIR	JT0589.
3D structure databases
ProteinModelPortal	P17872.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00545; UER00823.
Family and domain databases
Gene3D	2.160.20.10. 1 hit.
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. [Graphical view]
Pfam	PF01095. Pectinesterase. 1 hit. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME_ASPTU

Accession

Primary (citable) accession number: P17872

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program