Q9WYR4 (PTLY_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectate trisaccharide-lyase
EC=4.2.2.22

Alternative name(s):
Pectate lyase A
Short name=PelA

Gene names

Name:	pelA
Ordered Locus Names:	TM_0433

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	367 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	Cleaves unsaturated trigalacturonate from pectin. Activity is highest towards polygalacturonic acid, activity on methylated pectins decreases with an increasing degree of methylation. Ref.2
Catalytic activity	Eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate. Ref.2
Cofactor	Calcium. Ref.2
Enzyme regulation	Completely inactivated by EGTA. Ref.2
Subunit structure	Homotetramer. Ref.2
Subcellular location	Secreted › extracellular space Ref.2.
Sequence similarities	Belongs to the polysaccharide lyase 1 family. Contains 2 PbH1 repeats.
Biophysicochemical properties	Kinetic parameters: KM=0.6 mM for polygalacturonic acid Ref.2 pH dependence: Optimum pH is 9.0. Ref.2 Temperature dependence: Optimum temperature is 90 degrees Celsius. Half-life in the presence of 0.6 mM CaCl2 is 110 minutes at 95 degrees Celsius and 15 minutes at 100 degrees Celsius. Half-life in the absence of CaCl2 is 5 minutes at 90 degrees Celsius. Ref.2

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 367	340	Pectate trisaccharide-lyase		PRO_0000405016
Regions
	Repeat	151 – 173	23	PbH1 1
	Repeat	263 – 289	27	PbH1 2
Sites
	Active site	224	1	By similarity UniProtKB P39116
	Metal binding	144	1	Calcium By similarity UniProtKB P39116
	Metal binding	166	1	Calcium By similarity UniProtKB P39116
	Metal binding	170	1	Calcium By similarity UniProtKB P39116

Sequences

	Sequence		Length	Mass (Da)
	Q9WYR4 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: FDF57647B8476195	FASTA	367	40,607
	10 20 30 40 50 60 MLMRFSRVVS LVLLLVFTAV LTGAVKASLN DKPVGFASVP TADLPEGTVG GLGGEIVFVR 70 80 90 100 110 120 TAEELEKYTT AEGKYVIVVD GTIVFEPKRE IKVLSDKTIV GINDAKIVGG GLVIKDAQNV 130 140 150 160 170 180 IIRNIHFEGF YMEDDPRGKK YDFDYINVEN SHHIWIDHCT FVNGNDGAVD IKKYSNYITV 190 200 210 220 230 240 SWCKFVDHDK VSLVGSSDKE DPEQAGQAYK VTYHHNYFKN CIQRMPRIRF GMAHVFNNFY 250 260 270 280 290 300 SMGLRTGVSG NVFPIYGVAS AMGAKVHVEG NYFMGYGAVM AEAGIAFLPT RIMGPVEGYL 310 320 330 340 350 360 TLGEGDAKNE FYYCKEPEVR PVEEGKPALD PREYYDYTLD PVQDVPKIVV DGAGAGKLVF EELNTAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima." Kluskens L.D., van Alebeek G.J., Voragen A.G., de Vos W.M., van der Oost J. Biochem. J. 370:651-659(2003) [PubMed: 12443532] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35518.1.
PIR	D72376.
RefSeq	NP_228243.1. NC_000853.1.
3D structure databases
HSSP	HSSP built from PDB template 1JRG based on UniProtKB P29155.
ProteinModelPortal	Q9WYR4.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	897446.
GenomeReviews	Gene locus TM_0433 in contig AE000512_GR.
KEGG	tma:TM0433.
NMPDR	fig|243274.1.peg.427.
PATRIC	23935751. VBITheMar51294_0439.
TIGR	TM_0433.
Phylogenomic databases
HOGENOM	HBG465545.
OMA	NDGAVDI.
PhylomeDB	Q9WYR4.
ProtClustDB	CLSK872797.
Enzyme and pathway databases
BioCyc	TMAR243274:TM_0433-MONOMER.
BRENDA	4.2.2.2. 6331.
Family and domain databases
InterPro	IPR002022. Amb_allergen. IPR006626. PbH1. IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
KO	K01728.
Pfam	PF00544. Pec_lyase_C. 1 hit. [Graphical view]
SMART	SM00656. Amb_all. 1 hit. SM00710. PbH1. 2 hits. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PTLY_THEMA

Accession

Primary (citable) accession number: Q9WYR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program