SitesBLAST
Comparing WP_022670029.1 NCBI__GCF_000420385.1:WP_022670029.1 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)
34% identity, 96% coverage: 6:271/277 of query aligns to 19:300/301 of 3ejxD
- active site: C89 (= C79), H180 (= H151), E235 (= E201), C244 (= C211), G247 (= G214)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N14), F29 (= F16), N80 (= N70), P86 (≠ V76), C89 (= C79), G90 (= G80), N91 (= N81), N178 (≠ V149), N217 (= N183), E235 (= E201), R236 (= R202), C244 (= C211), G245 (= G212), T246 (= T213)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
34% identity, 96% coverage: 6:271/277 of query aligns to 5:286/287 of 3ekmA
- active site: C75 (= C79), H166 (= H151), E221 (= E201), C230 (= C211), G233 (= G214)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N14), N66 (= N70), P72 (≠ V76), C75 (= C79), G76 (= G80), N77 (= N81), N164 (≠ V149), N203 (= N183), E221 (= E201), R222 (= R202), C230 (= C211), G231 (= G212), T232 (= T213)
2gkjA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor dl-azidap (see paper)
33% identity, 96% coverage: 4:268/277 of query aligns to 1:270/274 of 2gkjA
- active site: C73 (= C79), H159 (= H151), E208 (= E201), C217 (= C211), G220 (= G214)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N14), Q44 (≠ G52), N64 (= N70), C73 (= C79), G74 (= G80), N75 (= N81), N157 (≠ V149), N190 (= N183), E208 (= E201), R209 (= R202), C217 (= C211), G218 (= G212), S219 (≠ T213)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
33% identity, 96% coverage: 4:268/277 of query aligns to 1:270/274 of 2gkeA
- active site: C73 (= C79), H159 (= H151), E208 (= E201), C217 (= C211), G220 (= G214)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N14), F13 (= F16), Q44 (≠ G52), N64 (= N70), V70 (= V76), C73 (= C79), G74 (= G80), N75 (= N81), N157 (≠ V149), N190 (= N183), E208 (= E201), R209 (= R202), C217 (= C211), G218 (= G212), S219 (≠ T213)
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)
33% identity, 96% coverage: 4:268/277 of query aligns to 1:270/274 of P44859
- N11 (= N14) binding substrate
- Q44 (≠ G52) binding substrate
- N64 (= N70) binding substrate
- 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 (= GN 80:81) binding substrate
- N157 (≠ V149) binding substrate
- N190 (= N183) binding substrate
- ER 208:209 (= ER 201:202) binding substrate
- C217 (= C211) 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 212:213) binding substrate
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
33% identity, 95% coverage: 6:268/277 of query aligns to 3:270/274 of P0A6K1
- Y268 (= Y266) Important for dimerization; mutation to A: Significantly less active than the wild-type dimer and unable to dimerize.
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
29% identity, 90% coverage: 4:251/277 of query aligns to 5:261/280 of 5m47A
- active site: C83 (= C79), H161 (= H151), E212 (= E201), C221 (= C211), G224 (= G214)
- binding 2,6-diaminopimelic acid: N15 (= N14), N74 (= N70), C83 (= C79), G84 (= G80), N85 (= N81), N159 (≠ V149), N194 (= N183), E212 (= E201), R213 (= R202), C221 (= C211), G222 (= G212), T223 (= T213)
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, 90% coverage: 4:251/277 of query aligns to 5:261/277 of Q8NP73
- N15 (= N14) binding substrate
- GN 84:85 (= GN 80:81) binding substrate
- N159 (≠ V149) binding substrate
- N194 (= N183) binding substrate
- ER 212:213 (= ER 201:202) binding substrate
- GT 222:223 (= GT 212:213) binding substrate
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: 6:276/277 of query aligns to 3:286/289 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 (= C211) 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_022670029.1 NCBI__GCF_000420385.1:WP_022670029.1
MKKIPFFKMNGSGNDFIIINNRDKIVESLVDIPLEEFVQKVCKRGLSVGADGLILIEKDD
VYDFRWRFFNSDGSEVEMCGNGSRCAARFAYLNSIAPLNMKFSTLAGVIEAQITGLNTVR
VQLTNPKDYKAEIELEGIGMPASFINTGVPHVVYFVDNVDVIDVKEIGAKTRYHDYFKPE
GTNVNFAEIIDENTIKLRTYERGVEDETLACGTGATAAAVISVLQGKCESPVDVLTKGGK
TLKIYVYVDDSGIKKVYLEGEALLTYIGTMIEEAWNY
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