SitesBLAST
Comparing WP_012040712.1 NCBI__GCF_000015165.1:WP_012040712.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 8 hits to proteins with known functional sites (download)
3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
37% identity, 93% coverage: 9:278/289 of query aligns to 19:297/301 of 3ejxD
- active site: C89 (= C76), H180 (= H166), E235 (= E216), C244 (= C225), G247 (≠ A228)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N17), F29 (≠ I19), N80 (= N67), P86 (≠ S73), C89 (= C76), G90 (= G77), N91 (= N78), N178 (= N164), N217 (= N198), E235 (= E216), R236 (= R217), C244 (= C225), G245 (= G226), T246 (≠ S227)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
37% identity, 93% coverage: 9:278/289 of query aligns to 5:283/287 of 3ekmA
- active site: C75 (= C76), H166 (= H166), E221 (= E216), C230 (= C225), G233 (≠ A228)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N17), N66 (= N67), P72 (≠ S73), C75 (= C76), G76 (= G77), N77 (= N78), N164 (= N164), N203 (= N198), E221 (= E216), R222 (= R217), C230 (= C225), G231 (= G226), T232 (≠ S227)
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
38% identity, 94% coverage: 8:278/289 of query aligns to 2:270/274 of P0A6K1
- Y268 (≠ F276) 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)
37% identity, 94% coverage: 8:278/289 of query aligns to 2:270/274 of 2gkjA
- active site: C73 (= C76), H159 (= H166), E208 (= E216), C217 (= C225), G220 (≠ A228)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N17), Q44 (= Q47), N64 (= N67), C73 (= C76), G74 (= G77), N75 (= N78), N157 (= N164), N190 (= N198), E208 (= E216), R209 (= R217), C217 (= C225), G218 (= G226), S219 (= S227)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
37% identity, 94% coverage: 8:278/289 of query aligns to 2:270/274 of 2gkeA
- active site: C73 (= C76), H159 (= H166), E208 (= E216), C217 (= C225), G220 (≠ A228)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N17), F13 (≠ I19), Q44 (= Q47), N64 (= N67), V70 (≠ S73), C73 (= C76), G74 (= G77), N75 (= N78), N157 (= N164), N190 (= N198), E208 (= E216), R209 (= R217), C217 (= C225), G218 (= G226), S219 (= S227)
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)
37% identity, 94% coverage: 8:278/289 of query aligns to 2:270/274 of P44859
- N11 (= N17) binding substrate
- Q44 (= Q47) binding substrate
- N64 (= N67) binding substrate
- C73 (= C76) 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 77:78) binding substrate
- N157 (= N164) binding substrate
- N190 (= N198) binding substrate
- ER 208:209 (= ER 216:217) binding substrate
- C217 (= C225) 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 226:227) binding substrate
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)
27% identity, 91% coverage: 9:270/289 of query aligns to 7:265/277 of Q8NP73
- N15 (= N17) binding substrate
- GN 84:85 (= GN 77:78) binding substrate
- N159 (= N164) binding substrate
- N194 (= N198) binding substrate
- ER 212:213 (= ER 216:217) binding substrate
- GT 222:223 (≠ GS 226:227) binding substrate
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
27% identity, 91% coverage: 9:270/289 of query aligns to 7:265/280 of 5m47A
- active site: C83 (= C76), H161 (= H166), E212 (= E216), C221 (= C225), G224 (≠ A228)
- binding 2,6-diaminopimelic acid: N15 (= N17), N74 (= N67), C83 (= C76), G84 (= G77), N85 (= N78), N159 (= N164), N194 (= N198), E212 (= E216), R213 (= R217), C221 (= C225), G222 (= G226), T223 (≠ S227)
Query Sequence
>WP_012040712.1 NCBI__GCF_000015165.1:WP_012040712.1
MSALANHSFVKMNGIGNEIVVLDLRDVKHVVTPDEARAVAARVPYDQLMVLQPPRLDGTE
AFIRIYNNDGSESGACGNGMRCVVRQVFEKTGQASATFETRAGLLNCWQGPAPDLYTVDM
GVPKFGWQEIPLAEEFRDTRYIELQIGPIDAPILHSPSVVNMGNPHAVFWVDGDVNSYDL
ERFGPLLENHPIFPERANITLAHIVDRDHITMRTWERGAGLTKACGSAACATAVAAARLK
RANRIVQMTLPGGELTIEWRERDDHVLMTGTATFEFEGRFEPQLFASVA
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