SitesBLAST
Comparing CCNA_03800 FitnessBrowser__Caulo:CCNA_03800 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)
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
38% identity, 96% coverage: 5:280/288 of query aligns to 3:270/274 of P0A6K1
- Y268 (= Y278) 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)
38% identity, 96% coverage: 5:280/288 of query aligns to 3:270/274 of 2gkjA
- active site: C73 (= C80), H159 (= H168), E208 (= E218), C217 (= C227), G220 (= G230)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N13), Q44 (= Q51), N64 (= N71), C73 (= C80), G74 (= G81), N75 (= N82), N157 (= N166), N190 (= N200), E208 (= E218), R209 (= R219), C217 (= C227), G218 (= G228), S219 (≠ T229)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
38% identity, 96% coverage: 5:280/288 of query aligns to 3:270/274 of 2gkeA
- active site: C73 (= C80), H159 (= H168), E208 (= E218), C217 (= C227), G220 (= G230)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N13), F13 (= F15), Q44 (= Q51), N64 (= N71), V70 (≠ A77), C73 (= C80), G74 (= G81), N75 (= N82), N157 (= N166), N190 (= N200), E208 (= E218), R209 (= R219), C217 (= C227), G218 (= G228), S219 (≠ T229)
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)
38% identity, 96% coverage: 5:280/288 of query aligns to 3:270/274 of P44859
- N11 (= N13) binding
- Q44 (= Q51) binding
- N64 (= N71) binding
- C73 (= C80) 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 81:82) binding
- N157 (= N166) binding
- N190 (= N200) binding
- ER 208:209 (= ER 218:219) binding
- C217 (= C227) 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 228:229) binding
3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
37% identity, 96% coverage: 5:280/288 of query aligns to 19:297/301 of 3ejxD
- active site: C89 (= C80), H180 (= H168), E235 (= E218), C244 (= C227), G247 (= G230)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N13), F29 (= F15), N80 (= N71), P86 (≠ A77), C89 (= C80), G90 (= G81), N91 (= N82), N178 (= N166), N217 (= N200), E235 (= E218), R236 (= R219), C244 (= C227), G245 (= G228), T246 (= T229)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
37% identity, 96% coverage: 5:280/288 of query aligns to 5:283/287 of 3ekmA
- active site: C75 (= C80), H166 (= H168), E221 (= E218), C230 (= C227), G233 (= G230)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N13), N66 (= N71), P72 (≠ A77), C75 (= C80), G76 (= G81), N77 (= N82), N164 (= N166), N203 (= N200), E221 (= E218), R222 (= R219), C230 (= C227), G231 (= G228), T232 (= T229)
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
30% identity, 78% coverage: 5:230/288 of query aligns to 7:224/280 of 5m47A
- active site: C83 (= C80), H161 (= H168), E212 (= E218), C221 (= C227), G224 (= G230)
- binding 2,6-diaminopimelic acid: N15 (= N13), N74 (= N71), C83 (= C80), G84 (= G81), N85 (= N82), N159 (= N166), N194 (= N200), E212 (= E218), R213 (= R219), C221 (= C227), G222 (= G228), T223 (= T229)
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)
30% identity, 78% coverage: 5:230/288 of query aligns to 7:224/277 of Q8NP73
P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
29% identity, 78% coverage: 5:230/288 of query aligns to 3:229/289 of P9WP19
- C87 (= C80) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C227) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>CCNA_03800 FitnessBrowser__Caulo:CCNA_03800
MSRTFLKMNGLGNDFVVIQTLTEAFDPTPEQIRAIAKRPGVDGKGGIGCDQVIAIDPPRA
EGASAYVRFWNSDGEVAGACGNGTRCVAWLLMQSAGKDAVAFDTVAGRLSGVAAGDKLVT
VDMGPPGLDWTQIPLAEEMNTERVELQVGPIDAPLVHTPVCVSMGNPHVVFFVDAPVTDD
FARGTGSLVEHHPLFPEGVNVGFAHIASRDHIRLKVWERGAGLTQACGTGACAAQVAAVR
RGLTDRKARVEFDTGSLTIEWRESDGHVIMTGPITMEYAGKLPELVAA
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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