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

Diaminopimelate decarboxylase

Gene

lysA

Organism
Escherichia coli O26:H11 (strain 11368 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.UniRule annotation

Catalytic activityi

Meso-2,6-diaminoheptanedioate = L-lysine + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotationSAAS annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei227 – 2271Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei271 – 2711SubstrateUniRule annotation
Binding sitei307 – 3071SubstrateUniRule annotation
Binding sitei311 – 3111SubstrateUniRule annotation
Binding sitei343 – 3431SubstrateUniRule annotation
Binding sitei378 – 3781Pyridoxal phosphateUniRule annotation
Binding sitei378 – 3781SubstrateUniRule annotation

GO - Molecular functioni

  1. diaminopimelate decarboxylase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. lysine biosynthetic process via diaminopimelate Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciECOL573235:GCY7-4034-MONOMER.
UniPathwayiUPA00034; UER00027.

Names & Taxonomyi

Protein namesi
Recommended name:
Diaminopimelate decarboxylaseUniRule annotation (EC:4.1.1.20UniRule annotation)
Short name:
DAP decarboxylaseUniRule annotation
Short name:
DAPDCUniRule annotation
Gene namesi
Name:lysAUniRule annotationImported
Ordered Locus Names:ECO26_3911Imported
OrganismiEscherichia coli O26:H11 (strain 11368 / EHEC)Imported
Taxonomic identifieri573235 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001617: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi573235.ECO26_3911.

Structurei

3D structure databases

ProteinModelPortaliC8TG88.
SMRiC8TG88. Positions 2-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni268 – 2714Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0019.
HOGENOMiHOG000045070.
KOiK01586.
OrthoDBiEOG6Z9B18.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_02120. LysA.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01048. lysA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C8TG88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSLFSTDT DLTAENLLRL PAEFGCPVWV YDAQIIRRQI AALKQFDVVR
60 70 80 90 100
FAQKACSNIH ILRLMREQGV KVDSVSLGEI ERALAAGYNP QTHPDDIVFT
110 120 130 140 150
ADVIDQATLE RVSELQIPVN AGSVDMLDQL GQVSPGHRVW LRVNPGFGHG
160 170 180 190 200
HSQKTNTGGE NSKHGIWYTD LPAALDVIQR HHLQLVGIHM HIGSGVDYAH
210 220 230 240 250
LEQVCGAMVR QVIEFGQDLQ AISAGGGLSI PYQQGEEAVD TEHYYGLWNA
260 270 280 290 300
AREQIARHLG HPVKLEIEPG RFLVAQSGVL ITQVRSVKQM GSRHFVLVDA
310 320 330 340 350
GFNDLMRPAM YGSYHHISAL AADGRSLEHA PTVETVVAGP LCESGDVFTQ
360 370 380 390 400
QEGGNVETRA LPEVKAGDYL VLHDTGAYGA SMSSNYNSRP LLPEVLFDNG
410 420
QARLIRRRQT IEELLALELL
Length:420
Mass (Da):46,191
Last modified:November 3, 2009 - v1
Checksum:i000D02EE3F96FF3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010953 Genomic DNA. Translation: BAI27102.1.
RefSeqiYP_003230842.1. NC_013361.1.

Genome annotation databases

EnsemblBacteriaiBAI27102; BAI27102; ECO26_3911.
GeneIDi8481203.
KEGGieoj:ECO26_3911.
PATRICi18403575. VBIEscCol24965_4000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010953 Genomic DNA. Translation: BAI27102.1.
RefSeqiYP_003230842.1. NC_013361.1.

3D structure databases

ProteinModelPortaliC8TG88.
SMRiC8TG88. Positions 2-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi573235.ECO26_3911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI27102; BAI27102; ECO26_3911.
GeneIDi8481203.
KEGGieoj:ECO26_3911.
PATRICi18403575. VBIEscCol24965_4000.

Phylogenomic databases

eggNOGiCOG0019.
HOGENOMiHOG000045070.
KOiK01586.
OrthoDBiEOG6Z9B18.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00027.
BioCyciECOL573235:GCY7-4034-MONOMER.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_02120. LysA.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01048. lysA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
    Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
    Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 11368 / EHECImported.

Entry informationi

Entry nameiC8TG88_ECO26
AccessioniPrimary (citable) accession number: C8TG88
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: March 4, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.