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F2LXX8 (F2LXX8_HIPMA) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Hipma_0266
OrganismHippea maritima (strain ATCC 700847 / DSM 10411 / MH2) [Complete proteome] [HAMAP] EMBL AEA33243.1
Taxonomic identifier760142 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfurellales › Desulfurellaceae › Hippea ›

Protein attributes

Sequence length412 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. RuleBase RU003738 HAMAP-Rule MF_02120

Cofactor

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

Pathway

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

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

Region272 – 2754Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2361Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2751Substrate By similarity HAMAP-Rule MF_02120
Binding site3111Substrate By similarity HAMAP-Rule MF_02120
Binding site3151Substrate By similarity HAMAP-Rule MF_02120
Binding site3421Substrate By similarity HAMAP-Rule MF_02120
Binding site3701Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3701Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue571N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
F2LXX8 [UniParc].

Last modified May 31, 2011. Version 1.
Checksum: 987512021BC680EC

FASTA41246,203
        10         20         30         40         50         60 
MFEYKNNELY AEGVRVKNIV DNVGSPVYVY SKGHFKAQFE KFNKAFSREH VIAFAIKSNS 

        70         80         90        100        110        120 
NLAVIKTFAS LGAGADIVSK GELFRAIKAG VDTSKIVFSG VAKRDDEIEY ALENDIMMIN 

       130        140        150        160        170        180 
VESEDELYNV NRVAEKLNKK ARIAFRVNPD VDPKTHPYIS TGLKKNKFGV PYEEAYDLYL 

       190        200        210        220        230        240 
KAKELKNIDV YGIQFHIGSQ LLDTTPIYDA SVRVADLMRR LTDKGVEFRV VDVGGGVGIV 

       250        260        270        280        290        300 
YDEKTDKEPD VNLYARQIEE AFRDFDVKLV LEPGRFLVGN GGILVSKVIY HKTNGQKNFL 

       310        320        330        340        350        360 
IIDAGMNDLL RPSLYKAYHK IAPMKKTGSK AIKCDIVGPI CETGDFFARD YEIEDVPNGN 

       370        380        390        400        410 
FIVVFSAGAY GFTMASNYNS RPRPAEVLVS GDSYRVVRER ESLEDLIKGE IL

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References

[1]"The complete genome of Hippea maritima DSM 10411."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L. expand/collapse author list , Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700847 / DSM 10411 / MH2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002606 Genomic DNA. Translation: AEA33243.1.
RefSeqYP_004339302.1. NC_015318.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA33243; AEA33243; Hipma_0266.
GeneID10391587.
KEGGhmr:Hipma_0266.
PATRIC54411179. VBIHipMar155866_0270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01586.

Enzyme and pathway databases

BioCycHMAR760142:GHVE-278-MONOMER.
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.
IPR022644. De-COase2_N.
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.
ProtoNetSearch...

Entry information

Entry nameF2LXX8_HIPMA
AccessionPrimary (citable) accession number: F2LXX8
Entry history
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: April 3, 2013
This is version 14 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