Q8YVD0 (DAPF2_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diaminopimelate epimerase 2
Short name=DAP epimerase 2
EC=5.1.1.7

Gene names

Name:	dapF2
Ordered Locus Names:	alr2048

Organism

Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Protein existence	Evidence 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 and an essential component of the bacterial peptidoglycan 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.
Sequence similarities	Belongs to the diaminopimelate epimerase family.
Sequence caution	The sequence BAB73747.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	diaminopimelate epimerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 279	279	Diaminopimelate epimerase 2 HAMAP-Rule MF_00197		PRO_0000149817
Regions
	Region	10 – 11	2	Substrate binding By similarity
	Region	75 – 77	3	Substrate binding By similarity
	Region	215 – 216	2	Substrate binding By similarity
	Region	225 – 226	2	Substrate binding By similarity
Sites
	Active site	75	1	Proton donor/acceptor By similarity
	Active site	224	1	Proton donor/acceptor By similarity
	Binding site	13	1	Substrate By similarity
	Binding site	47	1	Substrate By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Site	166	1	Important for catalytic activity By similarity
	Site	215	1	Important for catalytic activity By similarity
Amino acid modifications
	Disulfide bond	75 ↔ 224		HAMAP-Rule MF_00197

Sequences

	Sequence		Length	Mass (Da)
	Q8YVD0 [UniParc]. Last modified August 13, 2002. Version 2. Checksum: 6A669C3C7903B896	FASTA	279	30,233
	10 20 30 40 50 60 MAIEFTKYHG LGNDFILIDN RASKTPAITP EKAVEMCDRH FGIGADGVIF ALPGENGTDY 70 80 90 100 110 120 TMRIFNSDGS EPEMCGNGIR CLAAFLADLE GLSRNKDTYR IHTLAGVITP QLTPDGQIKV 130 140 150 160 170 180 DMGLPRLLAG EIPTTLGAAD GKVINQPLEV EGQTWEVTCV SMGNPHCITF VEDVAAIPLE 190 200 210 220 230 240 IIGPKFEHHP AFPQRTNTEF IQVVSRDYLK MRVWERGAGI TLACGTGACA SLVAAVLTGR 250 260 270 SDRLATVELP GGPLEIEWSE VDQRIYMTGP ADRVFTGKL

References

[1]

"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000019 Genomic DNA. Translation: BAB73747.1. Different initiation.
PIR	AB2062.
RefSeq	NP_486088.2. NC_003272.1.
3D structure databases
ProteinModelPortal	Q8YVD0.
ModBase	Search...
Protein-protein interaction databases
STRING	103690.alr2048.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB73747; BAB73747; BAB73747.
GeneID	1105643.
KEGG	ana:alr2048.
PATRIC	22774212. VBINosSp37423_2577.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0253.
HOGENOM	HOG000220466.
KO	K01778.
OMA	RFTKMQG.
ProtClustDB	PRK00450.
Enzyme and pathway databases
UniPathway	UPA00034; UER00025.
Family and domain databases
HAMAP	MF_00197. DAP_epimerase.
InterPro	IPR018510. DAP_epimerase_AS. IPR001653. DAP_epimerase_DapF. [Graphical view]
Pfam	PF01678. DAP_epimerase. 2 hits. [Graphical view]
TIGRFAMs	TIGR00652. DapF. 1 hit.
PROSITE	PS01326. DAP_EPIMERASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPF2_NOSS1

Accession

Primary (citable) accession number: Q8YVD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 2002
Last sequence update:	August 13, 2002
Last modified:	May 1, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program