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A0B6C1 (DAPF_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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 namesRecommended name:
Diaminopimelate epimerase

Short name=DAP epimerase
EC=5.1.1.7
Gene names
Name:dapF
Ordered Locus Names:Mthe_0454
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length279 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete 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 – 279279Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011905

Regions

Region77 – 793Substrate binding By similarity
Region207 – 2082Substrate binding By similarity
Region218 – 2192Substrate binding By similarity

Sites

Active site771Proton donor/acceptor By similarity
Active site2171Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site501Substrate By similarity
Binding site681Substrate By similarity
Binding site1911Substrate By similarity
Site1611Important for catalytic activity By similarity
Site2071Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond77 ↔ 217 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A0B6C1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: F1CF018283554695

FASTA27930,386
        10         20         30         40         50         60 
MNQLEFVKLH GNGNDFILID ELNGERIPED EKSEASRILC HRNFGIGGDG VLFLVPSERA 

        70         80         90        100        110        120 
DIGMRLFQPD GSEAEMCGNG IRCLAKHAWE SGYVGERFSV ETLAGVIPIQ VRRDRKGFWA 

       130        140        150        160        170        180 
RVEMGIPRFE RSEIPADGEG TFLKVPLHGF EVSAVNTGVP HAVIFVENLD IPVEQIAPKI 

       190        200        210        220        230        240 
RHSSCFPEGA NVNFVRLGNH LEVRTFERGV EAETLSCGTG SVAAAAVARR LGLVGETVEV 

       250        260        270 
MTKGGPLRIS FAGEKAFMEG PAVTVCRGVV SDEILQTLQ 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK14245.1.
RefSeqYP_842885.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B6C1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349307.Mthe_0454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK14245; ABK14245; Mthe_0454.
GeneID4462611.
KEGGmtp:Mthe_0454.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycMMET349307:GHKI-462-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPF_METTP
AccessionPrimary (citable) accession number: A0B6C1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: February 19, 2014
This is version 48 of the entry and version 1 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