##gff-version 3
P44859	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000149842;Note=Diaminopimelate epimerase	
P44859	UniProtKB	Active site	73	73	.	.	.	Note=Proton donor;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:16723397,ECO:0000305|PubMed:9843410,ECO:0000305|Ref.3,ECO:0007744|PDB:1BWZ,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397,PMID:9843410	
P44859	UniProtKB	Active site	217	217	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:16723397,ECO:0000305|PubMed:9843410,ECO:0000305|Ref.3,ECO:0007744|PDB:1BWZ,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397,PMID:9843410	
P44859	UniProtKB	Binding site	11	11	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	44	44	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	64	64	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	74	75	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	157	157	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	190	190	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	208	209	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Binding site	218	219	.	.	.	Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16723397,ECO:0007744|PDB:2GKE,ECO:0007744|PDB:2GKJ;Dbxref=PMID:16723397	
P44859	UniProtKB	Site	159	159	.	.	.	Note=Could be important to modulate the pK values of the two catalytic cysteine residues;Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:9843410,ECO:0007744|PDB:1BWZ;Dbxref=PMID:9843410	
P44859	UniProtKB	Site	208	208	.	.	.	Note=Could be important to modulate the pK values of the two catalytic cysteine residues;Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:9843410,ECO:0007744|PDB:1BWZ;Dbxref=PMID:9843410	
P44859	UniProtKB	Site	268	268	.	.	.	Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6K1	
P44859	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Inactive as epimerase%2C but it is able to rapidly catalyze the HF elimination via abstraction of the C-2 hydrogen of the D%2CL-3-fluoro-DAP analog and is essentially unable to catalyze the same elimination with the L%2CL-3-fluoro-DAP analog. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3	
P44859	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Enzymatically active%2C but it adopts a more open conformation. It is able to catalyze both epimerization of DAP and HF elimination of L%2CL-3-fluoro-DAP and D%2CL-3-fluoro-DAP. Able to slowly eliminate HF but does not catalyze epimerization%3B when associated with S-217. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17889830,ECO:0000269|Ref.3;Dbxref=PMID:17889830	
P44859	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Inactive as epimerase. It is able to rapidly catalyze the HF elimination via abstraction of the C-2 hydrogen of the L%2CL-3-fluoro-DAP analog and is essentially unable to catalyze the same elimination with the D%2CL-3-fluoro-DAP analog. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3	
P44859	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Enzymatically active%2C but it adopts a more open conformation. It is able to catalyze both epimerization of DAP and HF elimination of L%2CL-3-fluoro-DAP and D%2CL-3-fluoro-DAP. Able to slowly eliminate HF but does not catalyze epimerization%3B when associated with S-73. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17889830,ECO:0000269|Ref.3;Dbxref=PMID:17889830	
P44859	UniProtKB	Beta strand	2	8	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	11	17	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Helix	27	34	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	43	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	56	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Helix	74	86	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	93	98	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	103	108	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	114	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	137	142	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	147	163	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Turn	167	169	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Helix	172	180	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	190	198	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	201	208	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Turn	209	211	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Helix	218	230	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	236	242	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	245	251	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	258	262	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE	
P44859	UniProtKB	Beta strand	265	271	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GKE