Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Endo-pectate lyase

Gene

pelI

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi173 – 1731Zinc 1Combined sources
Metal bindingi176 – 1761Zinc 2; via pros nitrogenCombined sources
Metal bindingi178 – 1781Zinc 2Combined sources
Metal bindingi191 – 1911CalciumCombined sources
Metal bindingi192 – 1921Calcium; via carbonyl oxygenCombined sources
Metal bindingi195 – 1951Zinc 1Combined sources
Binding sitei195 – 1951Galacturonate 1Combined sources
Metal bindingi213 – 2131CalciumCombined sources
Metal bindingi218 – 2181Calcium; via carbonyl oxygenCombined sources
Binding sitei227 – 2271Galacturonate 2Combined sources
Binding sitei256 – 2561Galacturonate 1Combined sources
Binding sitei258 – 2581Galacturonate 4Combined sources
Binding sitei317 – 3171Galacturonate 1Combined sources
Binding sitei322 – 3221Galacturonate 3Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

LyaseImported

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BRENDAi4.2.2.2. 2141.

Protein family/group databases

CAZyiPL3. Polysaccharide Lyase Family 3.

Names & Taxonomyi

Protein namesi
Submitted name:
Endo-pectate lyaseImported (EC:4.2.2.2Imported)
Gene namesi
Name:pelIImported
OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)Imported
Taxonomic identifieri556 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 344325Sequence analysisPRO_5004158860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi121 ↔ 134Combined sources
Disulfide bondi143 ↔ 193Combined sources
Disulfide bondi177 ↔ 182Combined sources
Disulfide bondi254 ↔ 257Combined sources
Disulfide bondi309 ↔ 334Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B4NX-ray1.45A/B1-344[»]
3B8YX-ray2.30A/B1-344[»]
3B90X-ray2.11A/B119-344[»]
ProteinModelPortaliO50325.
SMRiO50325. Positions 20-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO50325.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 318205Pectate_lyaseInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 2293Galacturonate 1 bindingCombined sources
Regioni249 – 2524Galacturonate 3 bindingCombined sources
Regioni255 – 2562Galacturonate 2 bindingCombined sources

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR004898. Pectate_lyase_cat.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF03211. Pectate_lyase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O50325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKYVIPLCA LTLAAPSFAA QTTLMLSQKS DVNYLGWSTD ESKVARQEVY
60 70 80 90 100
RGTTSNPDLR ERIAVLDAET RTFKDADTNS GLNYWYWVDV VSENQAQVVS
110 120 130 140 150
NAVTTAPNAG PLRAAKASSE CKPGATFENR TVDCGGVTIG TSCPNDSDKQ
160 170 180 190 200
KPLIILKNAT VKNLRISASG RADGIHCDSG NCTIENVIWE DICEDAATNN
210 220 230 240 250
GKTMTIVGGI AHNAKDGYGG KPDKVLQHNS KNSTTVVKGN FTLTGEHGKL
260 270 280 290 300
WRSCGDCSNN GGPRFLTVTS ATVNGTIDSI AGVNRNYGDV ATISGLKIKN
310 320 330 340
YKEGKPPVCE EFKGVVKGQG STEKYGEKWD TTNCKVSRSG VSKL
Length:344
Mass (Da):36,851
Last modified:June 1, 1998 - v1
Checksum:i2812B3652439FA76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13340 Genomic DNA. Translation: CAA73784.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13340 Genomic DNA. Translation: CAA73784.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B4NX-ray1.45A/B1-344[»]
3B8YX-ray2.30A/B1-344[»]
3B90X-ray2.11A/B119-344[»]
ProteinModelPortaliO50325.
SMRiO50325. Positions 20-344.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL3. Polysaccharide Lyase Family 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.2.2.2. 2141.

Miscellaneous databases

EvolutionaryTraceiO50325.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR004898. Pectate_lyase_cat.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF03211. Pectate_lyase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiO50325_DICCH
AccessioniPrimary (citable) accession number: O50325
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: March 16, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.