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Protein

Pectate lyase A

Gene

pelA

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in maceration and soft-rotting of plant tissue.

Catalytic activityi

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.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Pathwayi: pectin degradation

This protein is involved in step 2 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:
  1. Pectinesterase (NM75_02575), Pectinesterase A (pemA), Pectinesterase (NM75_10885)
  2. Pectate lyase C (pelC), Pectate lyase D (pelD), Pectate lyase L (pelL), Pectate lyase E (pelE), Pectate lyase A (pelA), Pectate lyase B (pelB), Pectate lyase E (pelE)
  3. no protein annotated in this organism
  4. 5-dehydro-4-deoxy-D-glucuronate isomerase (NM75_18995), 5-dehydro-4-deoxy-D-glucuronate isomerase (NM75_20295)
  5. no protein annotated in this organism
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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi174CalciumBy similarity1
Metal bindingi176CalciumBy similarity1
Metal bindingi216CalciumBy similarity1
Metal bindingi220CalciumBy similarity1
Active sitei273Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.2.2. 2141.
UniPathwayiUPA00545; UER00824.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectate lyase A (EC:4.2.2.2)
Gene namesi
Name:pelA
OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifieri556 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000002485233 – 393Pectate lyase AAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi330 ↔ 358

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni38 – 41Combined sources4
Beta strandi46 – 48Combined sources3
Helixi49 – 51Combined sources3
Beta strandi52 – 54Combined sources3
Turni58 – 61Combined sources4
Helixi64 – 66Combined sources3
Beta strandi67 – 70Combined sources4
Helixi73 – 80Combined sources8
Turni81 – 84Combined sources4
Beta strandi87 – 91Combined sources5
Beta strandi93 – 96Combined sources4
Turni97 – 100Combined sources4
Helixi106 – 112Combined sources7
Beta strandi113 – 116Combined sources4
Beta strandi119 – 125Combined sources7
Beta strandi131 – 140Combined sources10
Helixi141 – 143Combined sources3
Beta strandi146 – 152Combined sources7
Beta strandi154 – 156Combined sources3
Beta strandi164 – 166Combined sources3
Turni167 – 169Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi177 – 181Combined sources5
Beta strandi185 – 191Combined sources7
Beta strandi193 – 195Combined sources3
Helixi201 – 203Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi210 – 212Combined sources3
Beta strandi218 – 221Combined sources4
Beta strandi226 – 232Combined sources7
Beta strandi234 – 240Combined sources7
Beta strandi242 – 245Combined sources4
Helixi251 – 254Combined sources4
Beta strandi259 – 264Combined sources6
Beta strandi266 – 272Combined sources7
Beta strandi274 – 279Combined sources6
Beta strandi281 – 286Combined sources6
Beta strandi288 – 292Combined sources5
Beta strandi296 – 298Combined sources3
Beta strandi303 – 306Combined sources4
Beta strandi311 – 316Combined sources6
Beta strandi318 – 322Combined sources5
Helixi326 – 332Combined sources7
Beta strandi333 – 337Combined sources5
Beta strandi340 – 345Combined sources6
Beta strandi356 – 359Combined sources4
Helixi378 – 387Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JRGX-ray2.10A/B33-393[»]
1JTAX-ray1.80A33-393[»]
1OOCX-ray2.94A/B33-393[»]
1PE9X-ray1.60A/B33-393[»]
ProteinModelPortaliP0C1A2.
SMRiP0C1A2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C1A2.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0C1A2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNKASGRSF TRSSKYLLAT LIAGMMASGV SAAELVSDKA LESAPTVGWA
60 70 80 90 100
SQNGFTTGGA AATSDNIYIV TNISEFTSAL SAGAEAKIIQ IKGTIDISGG
110 120 130 140 150
TPYTDFADQK ARSQINIPAN TTVIGLGTDA KFINGSLIID GTDGTNNVII
160 170 180 190 200
RNVYIQTPID VEPHYEKGDG WNAEWDAMNI TNGAHHVWID HVTISDGNFT
210 220 230 240 250
DDMYTTKDGE TYVQHDGALD IKRGSDYVTI SNSLIDQHDK TMLIGHNDTN
260 270 280 290 300
SAQDKGKLHV TLFNNVFNRV TERAPRVRYG SIHSFNNVFK GDAKDPVYRY
310 320 330 340 350
QYSFGIGTSG SVLSEGNSFT IANLSASKAC KVVKKFNGSI FSDNGSVLNG
360 370 380 390
SAVDLSGCGF SAYTSKIPYI YDVQPMTTEL AQSITDNAGS GKL
Length:393
Mass (Da):42,080
Last modified:April 18, 2006 - v1
Checksum:i20025C904FD7B345
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14509 Genomic DNA. Translation: AAA24843.1.
PIRiB31091. WZWC6A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14509 Genomic DNA. Translation: AAA24843.1.
PIRiB31091. WZWC6A.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JRGX-ray2.10A/B33-393[»]
1JTAX-ray1.80A33-393[»]
1OOCX-ray2.94A/B33-393[»]
1PE9X-ray1.60A/B33-393[»]
ProteinModelPortaliP0C1A2.
SMRiP0C1A2.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.
BRENDAi4.2.2.2. 2141.

Miscellaneous databases

EvolutionaryTraceiP0C1A2.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPLYA_DICCH
AccessioniPrimary (citable) accession number: P0C1A2
Secondary accession number(s): P29155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: November 2, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.