SitesBLAST
Comparing Ga0059261_2394 FitnessBrowser__Korea:Ga0059261_2394 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)
33% identity, 75% coverage: 6:242/315 of query aligns to 17:260/301 of 3ejxD
- active site: C89 (= C79), H180 (= H168), E235 (= E217), C244 (= C226), G247 (≠ A229)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N16), F29 (= F18), N80 (= N70), P86 (= P76), C89 (= C79), G90 (≠ L80), N91 (= N81), N178 (= N166), N217 (= N200), E235 (= E217), R236 (= R218), C244 (= C226), G245 (= G227), T246 (= T228)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
33% identity, 75% coverage: 6:242/315 of query aligns to 3:246/287 of 3ekmA
- active site: C75 (= C79), H166 (= H168), E221 (= E217), C230 (= C226), G233 (≠ A229)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N16), N66 (= N70), P72 (= P76), C75 (= C79), G76 (≠ L80), N77 (= N81), N164 (= N166), N203 (= N200), E221 (= E217), R222 (= R218), C230 (= C226), G231 (= G227), T232 (= T228)
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
31% identity, 90% coverage: 6:287/315 of query aligns to 1:274/274 of P0A6K1
- Y268 (≠ W281) 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)
29% identity, 90% coverage: 6:287/315 of query aligns to 1:274/274 of 2gkjA
- active site: C73 (= C79), H159 (= H168), E208 (= E217), C217 (= C226), G220 (≠ A229)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N16), Q44 (≠ G51), N64 (= N70), C73 (= C79), G74 (≠ L80), N75 (= N81), N157 (= N166), N190 (= N200), E208 (= E217), R209 (= R218), C217 (= C226), G218 (= G227), S219 (≠ T228)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
29% identity, 90% coverage: 6:287/315 of query aligns to 1:274/274 of 2gkeA
- active site: C73 (= C79), H159 (= H168), E208 (= E217), C217 (= C226), G220 (≠ A229)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N16), F13 (= F18), Q44 (≠ G51), N64 (= N70), V70 (≠ P76), C73 (= C79), G74 (≠ L80), N75 (= N81), N157 (= N166), N190 (= N200), E208 (= E217), R209 (= R218), C217 (= C226), G218 (= G227), S219 (≠ T228)
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)
29% identity, 90% coverage: 6:287/315 of query aligns to 1:274/274 of P44859
- N11 (= N16) binding
- Q44 (≠ G51) binding
- N64 (= N70) binding
- C73 (= C79) 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 (≠ LN 80:81) binding
- N157 (= N166) binding
- N190 (= N200) binding
- ER 208:209 (= ER 217:218) binding
- C217 (= C226) 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 227:228) 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)
31% identity, 80% coverage: 6:258/315 of query aligns to 1:257/289 of P9WP19
- C87 (= C79) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C226) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
28% identity, 71% coverage: 4:228/315 of query aligns to 1:223/280 of 5m47A
- active site: C83 (= C79), H161 (= H168), E212 (= E217), C221 (= C226)
- binding 2,6-diaminopimelic acid: N15 (= N16), N74 (= N70), C83 (= C79), G84 (≠ L80), N85 (= N81), N159 (= N166), N194 (= N200), E212 (= E217), R213 (= R218), C221 (= C226), G222 (= G227), T223 (= T228)
Sites not aligning to the query:
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)
28% identity, 71% coverage: 4:228/315 of query aligns to 1:223/277 of Q8NP73
Query Sequence
>Ga0059261_2394 FitnessBrowser__Korea:Ga0059261_2394
MQAMRLTFTKCHGSGNDFVLLDARGSTLSDSEWGRIARSLCERDGPVGADGLLLLGEGSD
GAQFAQKVVNADGSIPETCLNGLRCTARAGFELLGIEAATVQLKTSDAQVARDADLAPGV
YTVRTTVGPASTDPQAAGVNLAAPVIDAPVPGLPNGRNFTAVAMPNPHLIAFVDTVDVAE
LTALGDWCEAGPDLLADRANVSFVALRPDGLFVQTYERGVGLTNACGTAMGAATHVAGLT
GRIPFGAWITVHNPGGRVKARAEGPAGGDAVTIAGNATFEWDGEIEIDPATGQTGALTVT
RRRDDETAAWAALRG
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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