SitesBLAST
Comparing CA265_RS23025 CA265_RS23025 diaminopimelate epimerase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
31% identity, 98% coverage: 3:257/260 of query aligns to 17:297/301 of 3ejxD
- active site: C89 (= C74), H180 (= H140), E235 (= E189), C244 (= C199), G247 (= G202)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N13), F29 (= F15), N80 (= N65), P86 (≠ G71), C89 (= C74), G90 (= G75), N91 (= N76), N178 (≠ S138), N217 (= N172), E235 (= E189), R236 (= R190), C244 (= C199), G245 (= G200), T246 (= T201)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
31% identity, 98% coverage: 3:257/260 of query aligns to 3:283/287 of 3ekmA
- active site: C75 (= C74), H166 (= H140), E221 (= E189), C230 (= C199), G233 (= G202)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N13), N66 (= N65), P72 (≠ G71), C75 (= C74), G76 (= G75), N77 (= N76), N164 (≠ S138), N203 (= N172), E221 (= E189), R222 (= R190), C230 (= C199), G231 (= G200), T232 (= T201)
Q8NP73 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
29% identity, 100% coverage: 1:260/260 of query aligns to 3:276/277 of Q8NP73
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
29% identity, 100% coverage: 1:260/260 of query aligns to 3:276/280 of 5m47A
- active site: C83 (= C74), H161 (= H140), E212 (= E189), C221 (= C199), G224 (= G202)
- binding 2,6-diaminopimelic acid: N15 (= N13), N74 (= N65), C83 (= C74), G84 (= G75), N85 (= N76), N159 (≠ S138), N194 (= N172), E212 (= E189), R213 (= R190), C221 (= C199), G222 (= G200), T223 (= T201)
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
28% identity, 98% coverage: 3:257/260 of query aligns to 1:270/274 of P0A6K1
- Y268 (≠ F255) Important for dimerization; mutation to A: Significantly less active than the wild-type dimer and unable to dimerize.
2gkjA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor dl-azidap (see paper)
27% identity, 98% coverage: 3:257/260 of query aligns to 1:270/274 of 2gkjA
- active site: C73 (= C74), H159 (= H140), E208 (= E189), C217 (= C199), G220 (= G202)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N13), Q44 (≠ G47), N64 (= N65), C73 (= C74), G74 (= G75), N75 (= N76), N157 (≠ S138), N190 (= N172), E208 (= E189), R209 (= R190), C217 (= C199), G218 (= G200), S219 (≠ T201)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
27% identity, 98% coverage: 3:257/260 of query aligns to 1:270/274 of 2gkeA
- active site: C73 (= C74), H159 (= H140), E208 (= E189), C217 (= C199), G220 (= G202)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N13), F13 (= F15), Q44 (≠ G47), N64 (= N65), V70 (≠ G71), C73 (= C74), G74 (= G75), N75 (= N76), N157 (≠ S138), N190 (= N172), E208 (= E189), R209 (= R190), C217 (= C199), G218 (= G200), S219 (≠ T201)
P44859 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see 2 papers)
27% identity, 98% coverage: 3:257/260 of query aligns to 1:270/274 of P44859
- N11 (= N13) binding
- Q44 (≠ G47) binding
- N64 (= N65) binding
- C73 (= C74) mutation to A: Inactive as epimerase, but it is able to rapidly catalyze the HF elimination via abstraction of the C-2 hydrogen of the D,L-3-fluoro-DAP analog and is essentially unable to catalyze the same elimination with the L,L-3-fluoro-DAP analog.; mutation to S: Enzymatically active, but it adopts a more open conformation. It is able to catalyze both epimerization of DAP and HF elimination of L,L-3-fluoro-DAP and D,L-3-fluoro-DAP. Able to slowly eliminate HF but does not catalyze epimerization; when associated with S-217.
- GN 74:75 (= GN 75:76) binding
- N157 (≠ S138) binding
- N190 (= N172) binding
- ER 208:209 (= ER 189:190) binding
- C217 (= C199) mutation to A: Inactive as epimerase. It is able to rapidly catalyze the HF elimination via abstraction of the C-2 hydrogen of the L,L-3-fluoro-DAP analog and is essentially unable to catalyze the same elimination with the D,L-3-fluoro-DAP analog.; mutation to S: Enzymatically active, but it adopts a more open conformation. It is able to catalyze both epimerization of DAP and HF elimination of L,L-3-fluoro-DAP and D,L-3-fluoro-DAP. Able to slowly eliminate HF but does not catalyze epimerization; when associated with S-73.
- GS 218:219 (≠ GT 200:201) binding
P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
27% identity, 98% coverage: 5:259/260 of query aligns to 3:280/289 of P9WP19
- C87 (= C74) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C199) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>CA265_RS23025 CA265_RS23025 diaminopimelate epimerase
MKINFFKYQGAGNDFILIDHTMSPLKNIDNQLVEQLCHRRFGIGADGLMFITKHEDYDFE
MHYFNADGKLGSMCGNGGRCIVAFAKQLGIIDRETNFLAVDGPHYARISENGEWVDLQMI
DVDTITKDGEAYILNTGSPHYVALQSDLKDFDVFTAGKNIRYNATYAEKGINVNFVEDKG
DHLFVRTYERGVEDETYACGTGVTAVAMAMAKHKNQTGHIKTAIKVLGGDIKIEFDYDGK
EFTNVFLCGPAKLVFEGEVE
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory