Reviewed, UniProtKB/Swiss-Prot Q00645 (PELA_EMENI)

Names and origin

Protein names

Recommended name:
    Pectate lyase
    EC=4.2.2.2

Gene names

Name:	pelA
ORF Names:	AN0741

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the polysaccharide lyase 1 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pectate lyase 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 – 15	15	Potential
	Chain	16 – 326	311	Pectate lyase		PRO_0000024894
Sites
	Active site	219	1	Potential
	Metal binding	133	1	Calcium By similarity
	Metal binding	162	1	Calcium By similarity
	Metal binding	166	1	Calcium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q00645-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F6445A4A6D615D49	FASTA	326	34,580
	10 20 30 40 50 60 MRFTPLFLLA AVAIASPAPD LNARHELTRR QASESCPIGY CTQNGGTTGG AAGDTVTVTN 70 80 90 100 110 120 LADLTEAAES DGPLTIIVSG SISGSAKIRV ASDKTIFGES GSSITGIGFY IRRVSNVIMR 130 140 150 160 170 180 NLKISKVDAD NGDAIGIDAS SNVWVDHCDL SGDLSGGKDD LDGLVDISHG AEWITVSNTY 190 200 210 220 230 240 FHDHWKGSLI GHSDNNEDED LGHLHVTYAN NYWYNVYSRT PLIRFATVHI INNYWDSLID 250 260 270 280 290 300 TGVNCRMDAQ VLIQSSAFHN CPDRAIFFAD SDYTGYAVVD DVDLGGSSNS VPEGTLTPSS 310 320 LPYAAITALG SGQVASVIPG TAGQKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the Aspergillus nidulans pectate lyase pelA gene and evidence for binding of promoter regions to CREA, a regulator of carbon catabolite repression." Ho M.C., Whitehead M.P., Cleveland T.E., Dean R.A. Curr. Genet. 27:142-149(1995) [PubMed: 7788717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FGSC 4.
[2]	"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls." Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R. Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed: 16844780] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: FGSC A4 Glasgow.
[3]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U05592 Genomic DNA. Translation: AAA80568.1. DQ490468 mRNA. Translation: ABF50844.1. AACD01000012 Genomic DNA. Translation: EAA65383.1.
RefSeq	XP_658345.1.
3D structure databases
HSSP	HSSP built from PDB template 1JRG based on UniProtKB P29155.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Genome annotation databases
GeneID	2876513.
KEGG	ani:AN0741.2.
Enzyme and pathway databases
BRENDA	4.2.2.2. 3859.
Family and domain databases
InterPro	IPR002022. Amb_allergen. IPR012334. Pectin_lyas_fold. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF00544. Pec_lyase_C. 1 hit. [Graphical view]
SMART	SM00656. Amb_all. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PELA_EMENI

Accession

Primary (citable) accession number: Q00645
Secondary accession number(s): Q1HFV6, Q5BFD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	September 22, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)