SitesBLAST
Comparing 3609846 FitnessBrowser__Dino:3609846 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
42% identity, 92% coverage: 12:270/282 of query aligns to 1:270/274 of P0A6K1
- Y268 (≠ F268) Important for dimerization; mutation to A: Significantly less active than the wild-type dimer and unable to dimerize.
3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
38% identity, 92% coverage: 12:270/282 of query aligns to 17:297/301 of 3ejxD
- active site: C89 (= C82), H180 (= H161), E235 (= E210), C244 (≠ S219), G247 (≠ S222)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N22), F29 (= F24), N80 (= N73), P86 (≠ S79), C89 (= C82), G90 (= G83), N91 (= N84), N178 (= N159), N217 (= N192), E235 (= E210), R236 (= R211), C244 (≠ S219), G245 (= G220), T246 (≠ S221)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
38% identity, 92% coverage: 12:270/282 of query aligns to 3:283/287 of 3ekmA
- active site: C75 (= C82), H166 (= H161), E221 (= E210), C230 (≠ S219), G233 (≠ S222)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N22), N66 (= N73), P72 (≠ S79), C75 (= C82), G76 (= G83), N77 (= N84), N164 (= N159), N203 (= N192), E221 (= E210), R222 (= R211), C230 (≠ S219), G231 (= G220), T232 (≠ S221)
2gkjA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor dl-azidap (see paper)
38% identity, 93% coverage: 12:273/282 of query aligns to 1:273/274 of 2gkjA
- active site: C73 (= C82), H159 (= H161), E208 (= E210), C217 (≠ S219), G220 (≠ S222)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N22), Q44 (= Q55), N64 (= N73), C73 (= C82), G74 (= G83), N75 (= N84), N157 (= N159), N190 (= N192), E208 (= E210), R209 (= R211), C217 (≠ S219), G218 (= G220), S219 (= S221)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
38% identity, 93% coverage: 12:273/282 of query aligns to 1:273/274 of 2gkeA
- active site: C73 (= C82), H159 (= H161), E208 (= E210), C217 (≠ S219), G220 (≠ S222)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N22), F13 (= F24), Q44 (= Q55), N64 (= N73), V70 (≠ S79), C73 (= C82), G74 (= G83), N75 (= N84), N157 (= N159), N190 (= N192), E208 (= E210), R209 (= R211), C217 (≠ S219), G218 (= G220), S219 (= S221)
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, 93% coverage: 12:273/282 of query aligns to 1:273/274 of P44859
- N11 (= N22) binding
- Q44 (= Q55) binding
- N64 (= N73) binding
- C73 (= C82) 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 83:84) binding
- N157 (= N159) binding
- N190 (= N192) binding
- ER 208:209 (= ER 210:211) binding
- C217 (≠ S219) 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 220:221) binding
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
28% identity, 93% coverage: 12:272/282 of query aligns to 5:275/280 of 5m47A
- active site: C83 (= C82), H161 (= H161), E212 (= E210), C221 (≠ S219), G224 (≠ S222)
- binding 2,6-diaminopimelic acid: N15 (= N22), N74 (= N73), C83 (= C82), G84 (= G83), N85 (= N84), N159 (= N159), N194 (= N192), E212 (= E210), R213 (= R211), C221 (≠ S219), G222 (= G220), T223 (≠ S221)
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, 93% coverage: 12:272/282 of query aligns to 5:275/277 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)
27% identity, 77% coverage: 12:227/282 of query aligns to 1:229/289 of P9WP19
- C87 (= C82) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C224) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>3609846 FitnessBrowser__Dino:3609846
MPAMTDTAPDGLPFFKMHGLGNDFVVIDARAAPRPVSDRLVAALADRHRGVGFDQLAVIA
PAPEADAHLTFYNADGSTSAACGNATRCIARMILDETGATALRLSTDRGLLLAEDAGDGL
TRVNMGQPQTLWSEVPLAEAMDTLELPIEGTPTATGMGNPHCTFFVADAEAIPLDTFGPR
YEHHPLYPQRTNVQVAQIVGPDHIRMRVWERGVGVTLASGSSSCATGVAAARRGLTGRKT
RIDLDGGTLWIDWREDGVWMTGPNMTVFEGRLTPQFLAETAR
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