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Protein

Diaminopimelate decarboxylase

Gene

lysA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-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 annotation

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes L-lysine from DL-2,6-diaminopimelate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Diaminopimelate decarboxylase (lysA)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from DL-2,6-diaminopimelate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei279Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei324SubstrateUniRule annotation1
Binding sitei361SubstrateUniRule annotation1
Binding sitei365SubstrateUniRule annotation1
Active sitei392Proton donorSequence analysis1
Binding sitei393SubstrateUniRule annotation1
Binding sitei421Pyridoxal phosphateUniRule annotation1
Binding sitei421SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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 annotation
Ordered Locus Names:sll0504
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001499361 – 469Diaminopimelate decarboxylaseAdd BLAST469

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei93N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ55484.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ55484. 2 interactors.

Structurei

3D structure databases

ProteinModelPortaliQ55484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni321 – 324Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000045071.
InParanoidiQ55484.
KOiK01586.
OMAiLKGNKFG.
PhylomeDBiQ55484.

Family and domain databases

CDDicd06828. PLPDE_III_DapDC. 1 hit.
Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_02120. LysA. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
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.

Q55484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSTEMPLPT TGSTLLKTPA SPSPNQNLLP LTAVINKNGE LEIGGCSVPA
60 70 80 90 100
LVEQFGSPLY ILDETTLRQA AQQYRQSFQA HYPGSSQVIY ASKAWSCLAV
110 120 130 140 150
VAIAAQEGLG FDVVSGGELF TTVSALKQLG WDEAEIAEKI YFHGNNKSVQ
160 170 180 190 200
ELQEAIAINC TIIVDNWLEL ETLTKLAADS GAPVKIMLRL TPGIECHTHE
210 220 230 240 250
YIKTGHLDSK FGFDPNQLEA VFTYIAQQPS LHCLGLHAHI GSQIFERQPH
260 270 280 290 300
KDLGEVLVQW FTKGLTYGLP LTELNIGGGL GICYTESDDP PSIEEWAQVA
310 320 330 340 350
AISVAKACDR QNIPYPKLIA EPGRSLVGSA CVTAYRVGGR KVVPNIRTYI
360 370 380 390 400
SVDGGMSDNP RPITYQSVYR VALANRMNDE ITETVTVAGK HCESGDILVK
410 420 430 440 450
DVALPAAEPG DIMVVAATGA YNHSMASNYN RLGRPAAVLV NQGQANLILQ
460
RETYTDLLRQ DCLPNRLLS
Length:469
Mass (Da):50,848
Last modified:November 1, 1996 - v1
Checksum:iB8179A8F18257DD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10831.1.
PIRiS75984.

Genome annotation databases

EnsemblBacteriaiBAA10831; BAA10831; BAA10831.
KEGGisyn:sll0504.
PATRICi23843274. VBISynSp132158_3175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10831.1.
PIRiS75984.

3D structure databases

ProteinModelPortaliQ55484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ55484. 2 interactors.

Proteomic databases

PRIDEiQ55484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10831; BAA10831; BAA10831.
KEGGisyn:sll0504.
PATRICi23843274. VBISynSp132158_3175.

Phylogenomic databases

HOGENOMiHOG000045071.
InParanoidiQ55484.
KOiK01586.
OMAiLKGNKFG.
PhylomeDBiQ55484.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00027.

Family and domain databases

CDDicd06828. PLPDE_III_DapDC. 1 hit.
Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_02120. LysA. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
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...

Entry informationi

Entry nameiDCDA_SYNY3
AccessioniPrimary (citable) accession number: Q55484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 113 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.