Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3MEQ0 (Q3MEQ0_ANAVT) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 64. 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

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:Ava_0912 EMBL ABA20536.1
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP] EMBL ABA20536.1
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Region317 – 3204Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2751Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site3201Substrate By similarity HAMAP-Rule MF_02120
Binding site3571Substrate By similarity HAMAP-Rule MF_02120
Binding site3611Substrate By similarity HAMAP-Rule MF_02120
Binding site3891Substrate By similarity HAMAP-Rule MF_02120
Binding site4171Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site4171Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue981N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
Q3MEQ0 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 0027FB30BE673B0B

FASTA46450,665
        10         20         30         40         50         60 
MVSTHPAGVQ DAGTQYLPQR RNTNTNISPN QELLPLTAKA NSQGNLEIGG CDVTTLVEQF 

        70         80         90        100        110        120 
GSPLYILDEE TLRTACQQYR DGFQKYYPGE SQVLYASKAW NCLAVCAIAG SEGLGIDVVS 

       130        140        150        160        170        180 
GGELYTALAA GVSPAKIYLH GNNKSREELI LAIESGVTIV ADNWYELRTL ASLTHTDQPV 

       190        200        210        220        230        240 
RIMLRLTPGI ECHTHEYIRT GHLDSKFGFD PNDLAEVFEF VSQQPNLNCV GLHAHIGSQI 

       250        260        270        280        290        300 
FERQPHRDLA AVMVQWLRDA NKYGLNVTEL NVGGGLGIKY VESDDPPSID EWVKAICEVV 

       310        320        330        340        350        360 
QSACAAENLP LPKLLSEPGR SLIATSCVTA YTVGSSKTIP EIRTYVSIDG GMSDNPRPIT 

       370        380        390        400        410        420 
YQSVYRAVIA NKLSVSHTET VTIAGKHCES GDILIKNAQL PKTEPGDILV VMATGAYNYS 

       430        440        450        460 
MASNYNRLPR PAAVVVANGE ANLILQRETY QDLIRQDCLP ERLK 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA20536.1.
RefSeqYP_321431.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3MEQ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_0912.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA20536; ABA20536; Ava_0912.
GeneID3681345.
KEGGava:Ava_0912.
PATRIC35422270. VBIAnaVar43351_1700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045071.
KOK01586.
OMAHCFNVES.
OrthoDBEOG6Z9B18.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-922-MONOMER.
UniPathwayUPA00034; UER00027.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 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.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR01048. lysA. 1 hit.
PROSITEPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ3MEQ0_ANAVT
AccessionPrimary (citable) accession number: Q3MEQ0
Entry history
Integrated into UniProtKB/TrEMBL: October 25, 2005
Last sequence update: October 25, 2005
Last modified: July 9, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)