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O27389 (DAPF_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine By similarity. HAMAP-Rule MF_00197

Catalytic activity

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. HAMAP-Rule MF_00197

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_00197

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197.

Sequence similarities

Belongs to the diaminopimelate epimerase family.

Sequence caution

The sequence AAB85812.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149888

Regions

Region9 – 102Substrate binding By similarity
Region76 – 783Substrate binding By similarity
Region216 – 2172Substrate binding By similarity
Region226 – 2272Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2251Proton donor/acceptor By similarity
Binding site121Substrate By similarity
Binding site481Substrate By similarity
Binding site671Substrate By similarity
Binding site1651Substrate By similarity
Binding site1981Substrate By similarity
Site1671Important for catalytic activity By similarity
Site2161Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 225 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
O27389 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 374300C9D7FBDDE7

FASTA28631,220
        10         20         30         40         50         60 
MILFSKMHGL GNDYVVIDES AQECIPEDKK PEFVREVCTR GFSVGADGVI FVQPASGEGD 

        70         80         90        100        110        120 
IRFRIFNADG SEAEMCGNGI RCFSKFVYDN AIVRKRRLEV ETLAGIKTVE LEVEDGAVVS 

       130        140        150        160        170        180 
SRVDMGTATF KTDQIPMDVE EYEFIDRFLP VEGEDIKLTA LSVGNPHAII FVDDAEGVDL 

       190        200        210        220        230        240 
DRLGPAIENH PLFPERINVH FVEVVSPSEI IMVTWERGAG PTMACGTGAT ASVIAGVKLE 

       250        260        270        280 
KLDDSVLVHL PGGELKIDVY QDGTELGAYM EGDAVMVFDG ILLRDP 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85812.1. Different initiation.
PIRD69044.
RefSeqNP_276451.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH1334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85812; AAB85812; MTH_1334.
GeneID1471051.
KEGGmth:MTH1334.

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMACFARFVL.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1336-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPF_METTH
AccessionPrimary (citable) accession number: O27389
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways