SitesBLAST
Comparing WP_015926942.1 NCBI__GCF_000022085.1:WP_015926942.1 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)
36% identity, 94% coverage: 8:283/293 of query aligns to 18:298/301 of 3ejxD
- active site: C89 (= C78), H180 (= H171), E235 (= E221), C244 (= C230), G247 (≠ A233)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N17), F29 (≠ I19), N80 (= N69), P86 (≠ S75), C89 (= C78), G90 (= G79), N91 (= N80), N178 (= N169), N217 (= N203), E235 (= E221), R236 (= R222), C244 (= C230), G245 (= G231), T246 (≠ S232)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
36% identity, 94% coverage: 8:283/293 of query aligns to 4:284/287 of 3ekmA
- active site: C75 (= C78), H166 (= H171), E221 (= E221), C230 (= C230), G233 (≠ A233)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N17), N66 (= N69), P72 (≠ S75), C75 (= C78), G76 (= G79), N77 (= N80), N164 (= N169), N203 (= N203), E221 (= E221), R222 (= R222), C230 (= C230), G231 (= G231), T232 (≠ S232)
2gkjA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor dl-azidap (see paper)
36% identity, 95% coverage: 8:285/293 of query aligns to 2:273/274 of 2gkjA
- active site: C73 (= C78), H159 (= H171), E208 (= E221), C217 (= C230), G220 (≠ A233)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N17), Q44 (= Q49), N64 (= N69), C73 (= C78), G74 (= G79), N75 (= N80), N157 (= N169), N190 (= N203), E208 (= E221), R209 (= R222), C217 (= C230), G218 (= G231), S219 (= S232)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
36% identity, 95% coverage: 8:285/293 of query aligns to 2:273/274 of 2gkeA
- active site: C73 (= C78), H159 (= H171), E208 (= E221), C217 (= C230), G220 (≠ A233)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N17), F13 (≠ I19), Q44 (= Q49), N64 (= N69), V70 (≠ S75), C73 (= C78), G74 (= G79), N75 (= N80), N157 (= N169), N190 (= N203), E208 (= E221), R209 (= R222), C217 (= C230), G218 (= G231), S219 (= S232)
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)
36% identity, 95% coverage: 8:285/293 of query aligns to 2:273/274 of P44859
- N11 (= N17) binding substrate
- Q44 (= Q49) binding substrate
- N64 (= N69) binding substrate
- C73 (= C78) 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 79:80) binding substrate
- N157 (= N169) binding substrate
- N190 (= N203) binding substrate
- ER 208:209 (= ER 221:222) binding substrate
- C217 (= C230) 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 (= GS 231:232) binding substrate
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
40% identity, 95% coverage: 8:284/293 of query aligns to 2:272/274 of P0A6K1
- Y268 (≠ W280) 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 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
29% identity, 72% coverage: 69:278/293 of query aligns to 74:269/277 of Q8NP73
- GN 84:85 (= GN 79:80) binding substrate
- N159 (= N169) binding substrate
- N194 (= N203) binding substrate
- ER 212:213 (= ER 221:222) binding substrate
- GT 222:223 (≠ GS 231:232) binding substrate
Sites not aligning to the query:
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
29% identity, 72% coverage: 69:278/293 of query aligns to 74:269/280 of 5m47A
- active site: C83 (= C78), H161 (= H171), E212 (= E221), C221 (= C230), G224 (≠ A233)
- binding 2,6-diaminopimelic acid: N74 (= N69), C83 (= C78), G84 (= G79), N85 (= N80), N159 (= N169), N194 (= N203), E212 (= E221), R213 (= R222), C221 (= C230), G222 (= G231), T223 (≠ S232)
Sites not aligning to the query:
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, 77% coverage: 61:285/293 of query aligns to 70:281/289 of P9WP19
- C87 (= C78) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C230) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>WP_015926942.1 NCBI__GCF_000022085.1:WP_015926942.1
MSPLAHRRFLKMNGLGNEIVVLDLRGTPHIVQPQEARAIAADPRSRFDQLMVLHDPVTAG
TDAALRIYNTDGSESGACGNGTRCVAWAMLEDPVMGRPAERLTLQSRAGLLAVTRVSATD
FTVDMGPPRLRWDEIPLAEPFPDTRRIELQIGPIDDPILHSPGVVSMGNPHAVFFVDRDP
ASYDLARIGPLLEAHPIFPERANISVAQVRGPEHIVLRVWERGAGLTRACGSAACAALVA
AARLRLTGRRAVVTLPGGDLVIDWGEDDHVRMTGPTELEWEGTLAPSLFAGAA
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