SitesBLAST
Comparing 5207806 FitnessBrowser__PV4:5207806 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)
69% identity, 99% coverage: 2:278/279 of query aligns to 1:273/274 of P0A6K1
- Y268 (= Y273) 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)
68% identity, 99% coverage: 2:277/279 of query aligns to 1:272/274 of 2gkjA
- active site: C73 (= C74), H159 (= H164), E208 (= E213), C217 (= C222), G220 (= G225)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N12), Q44 (= Q45), N64 (= N65), C73 (= C74), G74 (= G75), N75 (= N76), N157 (= N162), N190 (= N195), E208 (= E213), R209 (= R214), C217 (= C222), G218 (= G223), S219 (= S224)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
68% identity, 99% coverage: 2:277/279 of query aligns to 1:272/274 of 2gkeA
- active site: C73 (= C74), H159 (= H164), E208 (= E213), C217 (= C222), G220 (= G225)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N12), F13 (= F14), Q44 (= Q45), N64 (= N65), V70 (= V71), C73 (= C74), G74 (= G75), N75 (= N76), N157 (= N162), N190 (= N195), E208 (= E213), R209 (= R214), C217 (= C222), G218 (= G223), S219 (= S224)
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)
68% identity, 99% coverage: 2:277/279 of query aligns to 1:272/274 of P44859
- N11 (= N12) binding
- Q44 (= Q45) binding
- N64 (= N65) binding
- C73 (= C74) 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 75:76) binding
- N157 (= N162) binding
- N190 (= N195) binding
- ER 208:209 (= ER 213:214) binding
- C217 (= C222) 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 223:224) binding
3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
41% identity, 99% coverage: 1:276/279 of query aligns to 16:298/301 of 3ejxD
- active site: C89 (= C74), H180 (= H164), E235 (= E213), C244 (= C222), G247 (= G225)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N12), F29 (= F14), N80 (= N65), P86 (≠ V71), C89 (= C74), G90 (= G75), N91 (= N76), N178 (= N162), N217 (= N195), E235 (= E213), R236 (= R214), C244 (= C222), G245 (= G223), T246 (≠ S224)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
41% identity, 99% coverage: 1:276/279 of query aligns to 2:284/287 of 3ekmA
- active site: C75 (= C74), H166 (= H164), E221 (= E213), C230 (= C222), G233 (= G225)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N12), N66 (= N65), P72 (≠ V71), C75 (= C74), G76 (= G75), N77 (= N76), N164 (= N162), N203 (= N195), E221 (= E213), R222 (= R214), C230 (= C222), G231 (= G223), T232 (≠ S224)
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)
33% identity, 99% coverage: 2:278/279 of query aligns to 5:276/277 of Q8NP73
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
33% identity, 99% coverage: 2:278/279 of query aligns to 5:276/280 of 5m47A
- active site: C83 (= C74), H161 (= H164), E212 (= E213), C221 (= C222), G224 (= G225)
- binding 2,6-diaminopimelic acid: N15 (= N12), N74 (= N65), C83 (= C74), G84 (= G75), N85 (= N76), N159 (= N162), N194 (= N195), E212 (= E213), R213 (= R214), C221 (= C222), G222 (= G223), T223 (≠ S224)
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, 90% coverage: 4:255/279 of query aligns to 3:260/289 of P9WP19
- C87 (= C74) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C222) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>5207806 FitnessBrowser__PV4:5207806
MIHFTKMHGLGNDFMVVDGVTQNVYFSPEQIKRLADRNFGIGFDQLLLVEPPYDPDLDFH
YRIFNADGSEVEQCGNGARCFARFVKSKGLINKQKIKVSTSSGKMTLRLERDGSVTVNMG
IPVLEPSRIPFNAKKAEKTYLLQADMPEGMQTFLCGAVSMGNPHCVLEVDDVANADVERI
GSLLTKHERFPKGVNVGFMQVVDANHIKLRVYERGAAETLACGSGACAAVAVGQLQGKLA
RRVRVDLPGGSLTINWEGEGKPLWMTGPAEHVYDGQIQQ
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