Skip Header

Contribute Send feedback
Read comments (?) or add your own

D2A6Z4 (D2A6Z4_SHIF2) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Diaminopimelate decarboxylase HAMAP-Rule MF_02120
Short name=DAP decarboxylase HAMAP-Rule MF_02120
Short name=DAPDC HAMAP-Rule MF_02120
EC=4.1.1.20 HAMAP-Rule MF_02120
Gene names
Name:lysA HAMAP-Rule MF_02120 EMBL ADA75178.1
Ordered Locus Names:SFxv_3123 EMBL ADA75178.1
OrganismShigella flexneri serotype X (strain 2002017) [Complete proteome] [HAMAP] EMBL ADA75178.1
Taxonomic identifier591020 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella ›

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine By similarity. HAMAP-Rule MF_02120

Catalytic activity

Meso-2,6-diaminoheptanedioate = L-lysine + CO2. HAMAP-Rule MF_02120 RuleBase RU003738

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_02120 RuleBase RU003738 SAAS SAAS022644

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_02120 RuleBase RU003738

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_02120

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily. HAMAP-Rule MF_02120

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region268 – 2714Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2271Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2711Substrate By similarity HAMAP-Rule MF_02120
Binding site3071Substrate By similarity HAMAP-Rule MF_02120
Binding site3111Substrate By similarity HAMAP-Rule MF_02120
Binding site3431Substrate By similarity HAMAP-Rule MF_02120
Binding site3781Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3781Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue541N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
D2A6Z4 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: 5CF953BC40B338F9

FASTA42046,175
        10         20         30         40         50         60 
MPHSLFSTDT DLTAENLLRL PAEFGCPVWV YDAQIIRRQI AALKQFEVVR FAQKACSNIH 

        70         80         90        100        110        120 
ILRLMREQGV KVDSVSLGEI ERALAAGYNP QTHPDDIVFT ADVIDQATLE RVSELQIPVN 

       130        140        150        160        170        180 
AGSVDTLDQL GQVSPGHRVW LRVNPGFGHG HSQKTNTGGE NSKHGIWYTD LPAALDVIQR 

       190        200        210        220        230        240 
HHLQLVGIHM HIGSGVDYAH LEQVCGAMVR QVIEFGQDLQ AISAGGGLSI PYQQGEEAVD 

       250        260        270        280        290        300 
TEHYYGLWNA AREQIARHLG HPVKLEIEPG RFLVAQSGVL ITQVRSVKQM GSRHFVLVDA 

       310        320        330        340        350        360 
GFNDLMRPAM YGSYHHISAL AADGRSLEHA PTVETVVAGP LCESGDVFTQ QEGGNVETRA 

       370        380        390        400        410        420 
LPEVKAGDYL VLHDTGAYGA SMSSNYNSRP LLPEVLFDNG QARLIRRRQT IEELLALELL

« Hide

References

[1]"Emergence of a new multidrug resistance serotype X variant in an epidemic clone of Shigella flexneri."
Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z., Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X., Bai X. expand/collapse author list , Wang Y., Wang P., Xu Q., Xu J.
J. Clin. Microbiol. 48:419-426(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2002017 EMBL ADA75178.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001383 Genomic DNA. Translation: ADA75178.1.
RefSeqYP_005728471.1. NC_017328.1.

3D structure databases

ProteinModelPortalD2A6Z4.
SMRD2A6Z4. Positions 2-411.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADA75178; ADA75178; SFxv_3123.
GeneID12318355.
KEGGsfe:SFxv_3123.
PATRIC36748165. VBIShiFle60233_3380.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000045070.
KOK01586.

Enzyme and pathway databases

UniPathwayUPA00034; UER00027.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_02120. LysA.
InterProIPR009006. 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.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR01048. lysA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD2A6Z4_SHIF2
AccessionPrimary (citable) accession number: D2A6Z4
Entry history
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: May 1, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info