SitesBLAST
Comparing 350076 FitnessBrowser__Btheta:350076 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)
42% identity, 98% coverage: 2:263/267 of query aligns to 14:297/301 of 3ejxD
- active site: C89 (= C75), H180 (= H152), E235 (= E201), C244 (= C210), G247 (= G213)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N15), F29 (≠ Y17), N80 (= N66), P86 (≠ A72), C89 (= C75), G90 (= G76), N91 (= N77), N178 (= N150), N217 (= N183), E235 (= E201), R236 (= R202), C244 (= C210), G245 (= G211), T246 (= T212)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
42% identity, 97% coverage: 5:263/267 of query aligns to 3:283/287 of 3ekmA
- active site: C75 (= C75), H166 (= H152), E221 (= E201), C230 (= C210), G233 (= G213)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N15), N66 (= N66), P72 (≠ A72), C75 (= C75), G76 (= G76), N77 (= N77), N164 (= N150), N203 (= N183), E221 (= E201), R222 (= R202), C230 (= C210), G231 (= G211), T232 (= T212)
2gkjA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor dl-azidap (see paper)
38% identity, 97% coverage: 5:263/267 of query aligns to 1:270/274 of 2gkjA
- active site: C73 (= C75), H159 (= H152), E208 (= E201), C217 (= C210), G220 (= G213)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N15), Q44 (≠ G48), N64 (= N66), C73 (= C75), G74 (= G76), N75 (= N77), N157 (= N150), N190 (= N183), E208 (= E201), R209 (= R202), C217 (= C210), G218 (= G211), S219 (≠ T212)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
38% identity, 97% coverage: 5:263/267 of query aligns to 1:270/274 of 2gkeA
- active site: C73 (= C75), H159 (= H152), E208 (= E201), C217 (= C210), G220 (= G213)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N15), F13 (≠ Y17), Q44 (≠ G48), N64 (= N66), V70 (≠ A72), C73 (= C75), G74 (= G76), N75 (= N77), N157 (= N150), N190 (= N183), E208 (= E201), R209 (= R202), C217 (= C210), G218 (= G211), S219 (≠ T212)
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, 97% coverage: 5:263/267 of query aligns to 1:270/274 of P44859
- N11 (= N15) binding
- Q44 (≠ G48) binding
- N64 (= N66) binding
- C73 (= C75) 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 76:77) binding
- N157 (= N150) binding
- N190 (= N183) binding
- ER 208:209 (= ER 201:202) binding
- C217 (= C210) 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 211:212) binding
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
37% identity, 97% coverage: 5:263/267 of query aligns to 1:270/274 of P0A6K1
- Y268 (≠ F261) 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 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
30% identity, 100% coverage: 1:266/267 of query aligns to 1:276/277 of Q8NP73
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
30% identity, 100% coverage: 1:266/267 of query aligns to 1:276/280 of 5m47A
- active site: C83 (= C75), H161 (= H152), E212 (= E201), C221 (= C210), G224 (= G213)
- binding 2,6-diaminopimelic acid: N15 (= N15), N74 (= N66), C83 (= C75), G84 (= G76), N85 (= N77), N159 (= N150), N194 (= N183), E212 (= E201), R213 (= R202), C221 (= C210), G222 (= G211), T223 (= T212)
P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
30% identity, 78% coverage: 7:213/267 of query aligns to 3:229/289 of P9WP19
- C87 (= C75) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C210) active site, Proton acceptor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
Query Sequence
>350076 FitnessBrowser__Btheta:350076
MTTKIKFTKMHGAGNDYIYVDTTRYPIAAPEKKAIEWSKFHTGIGSDGLILIGSSDKADF
SMRIFNADGSEAMMCGNGSRCVGKYVYEYGLTAKKEITLDTRSGIKVLKLHVEGGKVTAV
TVDMGSPLETEAVDFGDQFPFQSTRVSMGNPHLVTFVEDITQINLPEIGPQLENYHLFPD
RTNVEFAQIVGKDTIRMRVWERGSGITQACGTGACATAVAAVLHGLAGRKCDIIMDGGTV
TIEWEEATGHILMTGPATKVFDGEMEG
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