SitesBLAST
Comparing 207333 FitnessBrowser__DvH:207333 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, 93% coverage: 10:270/282 of query aligns to 19:297/301 of 3ejxD
- active site: C89 (= C83), H180 (= H158), E235 (= E208), C244 (= C218), G247 (= G221)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N18), F29 (= F20), N80 (= N74), P86 (≠ A80), C89 (= C83), G90 (= G84), N91 (= N85), N178 (≠ V156), N217 (= N190), E235 (= E208), R236 (= R209), C244 (= C218), G245 (= G219), T246 (= T220)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
33% identity, 93% coverage: 10:270/282 of query aligns to 5:283/287 of 3ekmA
- active site: C75 (= C83), H166 (= H158), E221 (= E208), C230 (= C218), G233 (= G221)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N18), N66 (= N74), P72 (≠ A80), C75 (= C83), G76 (= G84), N77 (= N85), N164 (≠ V156), N203 (= N190), E221 (= E208), R222 (= R209), C230 (= C218), G231 (= G219), T232 (= T220)
2gkjA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor dl-azidap (see paper)
32% identity, 93% coverage: 8:270/282 of query aligns to 1:270/274 of 2gkjA
- active site: C73 (= C83), H159 (= H158), E208 (= E208), C217 (= C218), G220 (= G221)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N18), Q44 (≠ G53), N64 (= N74), C73 (= C83), G74 (= G84), N75 (= N85), N157 (≠ V156), N190 (= N190), E208 (= E208), R209 (= R209), C217 (= C218), G218 (= G219), S219 (≠ T220)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
32% identity, 93% coverage: 8:270/282 of query aligns to 1:270/274 of 2gkeA
- active site: C73 (= C83), H159 (= H158), E208 (= E208), C217 (= C218), G220 (= G221)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N18), F13 (= F20), Q44 (≠ G53), N64 (= N74), V70 (≠ A80), C73 (= C83), G74 (= G84), N75 (= N85), N157 (≠ V156), N190 (= N190), E208 (= E208), R209 (= R209), C217 (= C218), G218 (= G219), S219 (≠ T220)
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)
32% identity, 93% coverage: 8:270/282 of query aligns to 1:270/274 of P44859
- N11 (= N18) binding substrate
- Q44 (≠ G53) binding substrate
- N64 (= N74) binding substrate
- C73 (= C83) 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 84:85) binding substrate
- N157 (≠ V156) binding substrate
- N190 (= N190) binding substrate
- ER 208:209 (= ER 208:209) binding substrate
- C217 (= C218) 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 219:220) binding substrate
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
31% identity, 94% coverage: 10:273/282 of query aligns to 3:273/274 of P0A6K1
- Y268 (≠ F268) Important for dimerization; mutation to A: Significantly less active than the wild-type dimer and unable to dimerize.
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)
32% identity, 95% coverage: 7:273/282 of query aligns to 4:276/277 of Q8NP73
- N15 (= N18) binding substrate
- GN 84:85 (= GN 84:85) binding substrate
- N159 (≠ V156) binding substrate
- N194 (= N190) binding substrate
- ER 212:213 (= ER 208:209) binding substrate
- GT 222:223 (= GT 219:220) binding substrate
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
32% identity, 95% coverage: 7:273/282 of query aligns to 4:276/280 of 5m47A
- active site: C83 (= C83), H161 (= H158), E212 (= E208), C221 (= C218), G224 (= G221)
- binding 2,6-diaminopimelic acid: N15 (= N18), N74 (= N74), C83 (= C83), G84 (= G84), N85 (= N85), N159 (≠ V156), N194 (= N190), E212 (= E208), R213 (= R209), C221 (= C218), G222 (= G219), T223 (= T220)
P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
32% identity, 93% coverage: 10:272/282 of query aligns to 3:280/289 of P9WP19
- C87 (= C83) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C218) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>207333 FitnessBrowser__DvH:207333
MSGKKATVPFHKLHGCGNDFVFIDNRHLKLSVEAMPDWARSICRRAFGVGADGLVFLDTA
PQGHEADYIWHFYNADGSRAEMCGNASRCAAVLAVDLGFAGPRHAFGTDAGIVHAVADVE
AGYAKVELTRPRDLAAGTTLELEGTPFTVHFVNTGVPHAVVFSDSVDGLDLRRLGAALRY
HPHFSPAGTNANFASIIDRRTIHLRTYERGVEDETYACGTGAAATAFIAHTLGLTDASVG
VRTSGGEVLGIDIEDGSIFLSGKAVRVFSGEMHPEGLGLTLP
Or try a new SitesBLAST search
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