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Protein

Diaminopimelate decarboxylase

Gene

lysA

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei242 – 2421Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei317 – 3171SubstrateUniRule annotation
Binding sitei321 – 3211SubstrateUniRule annotation
Active sitei346 – 3461Proton donorSequence analysis
Binding sitei347 – 3471SubstrateUniRule annotation
Binding sitei375 – 3751Pyridoxal phosphateUniRule annotation
Binding sitei375 – 3751SubstrateUniRule annotation

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:ZMO1768
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Diaminopimelate decarboxylasePRO_0000149939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9Z661.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000045070.
KOiK01586.
OMAiLKGNKFG.
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.
IPR022644. De-COase2_N.
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.

Sequencei

Sequence statusi: Complete.

Q9Z661-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPFSLKNGT LCVEDIPLPE IAAQYGTPCY VYSHSYLTER ARRFTKALDG
60 70 80 90 100
AGKGKSLVAF AVKANPSQAI LASFAKEGLG ADVVSAGEIR RAVHAGIPPE
110 120 130 140 150
RIVFSGVGKT AEEMRYALEI GIGQFNIESV SEIEMLAEVA TSLGKKAAVA
160 170 180 190 200
LRINPDVDPH THAKIATGKA DTKFGIAAED ALSAYEKLAS YPSLKIQGIA
210 220 230 240 250
SHIGSQITDL APFEAAAERI YEIITALEKA GHAIETADLG GGLGVRYKDD
260 270 280 290 300
QPEPPSVEAY GEMIKRVTKG WNCRLIFEPG RSLIANAGVL LSKVIRIKES
310 320 330 340 350
KTARFVILDA AMNDLVRPTL YDAYHEIKAV TPSAQTYQAD IVGPVCETGD
360 370 380 390 400
IFARNRSISA VKADDLMAIM SAGAYGATMA SAYNSRPLVA EVMVSGNKSA
410 420
LIRKRQSVED LMRDEQKVEW L
Length:421
Mass (Da):45,249
Last modified:May 1, 1999 - v1
Checksum:i641732D7E14F32FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF102543 Genomic DNA. Translation: AAD19416.1.
AE008692 Genomic DNA. Translation: AAV90392.1.
RefSeqiWP_011241508.1. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV90392; AAV90392; ZMO1768.
KEGGizmo:ZMO1768.
PATRICi32568802. VBIZymMob102260_1676.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF102543 Genomic DNA. Translation: AAD19416.1.
AE008692 Genomic DNA. Translation: AAV90392.1.
RefSeqiWP_011241508.1. NC_006526.2.

3D structure databases

ProteinModelPortaliQ9Z661.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV90392; AAV90392; ZMO1768.
KEGGizmo:ZMO1768.
PATRICi32568802. VBIZymMob102260_1676.

Phylogenomic databases

HOGENOMiHOG000045070.
KOiK01586.
OMAiLKGNKFG.
OrthoDBiEOG6Z9B18.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00027.

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.
IPR022644. De-COase2_N.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Um H.W., Kang H.S.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.

Entry informationi

Entry nameiDCDA_ZYMMO
AccessioniPrimary (citable) accession number: Q9Z661
Secondary accession number(s): Q5NLL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: November 11, 2015
This is version 99 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

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.