SitesBLAST
Comparing WP_057508891.1 NCBI__GCF_001431535.1:WP_057508891.1 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)
P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
46% identity, 93% coverage: 18:288/292 of query aligns to 1:270/274 of P0A6K1
- Y268 (≠ F286) 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)
44% identity, 93% coverage: 18:288/292 of query aligns to 1:270/274 of 2gkjA
- active site: C73 (= C90), H159 (= H177), E208 (= E226), C217 (= C235), G220 (= G238)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N28), Q44 (= Q61), N64 (= N81), C73 (= C90), G74 (= G91), N75 (= N92), N157 (= N175), N190 (= N208), E208 (= E226), R209 (= R227), C217 (= C235), G218 (= G236), S219 (= S237)
2gkeA Crystal structure of diaminopimelate epimerase in complex with an irreversible inhibitor ll-azidap (see paper)
44% identity, 93% coverage: 18:288/292 of query aligns to 1:270/274 of 2gkeA
- active site: C73 (= C90), H159 (= H177), E208 (= E226), C217 (= C235), G220 (= G238)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N11 (= N28), F13 (= F30), Q44 (= Q61), N64 (= N81), V70 (≠ S87), C73 (= C90), G74 (= G91), N75 (= N92), N157 (= N175), N190 (= N208), E208 (= E226), R209 (= R227), C217 (= C235), G218 (= G236), S219 (= S237)
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)
44% identity, 93% coverage: 18:288/292 of query aligns to 1:270/274 of P44859
- N11 (= N28) binding
- Q44 (= Q61) binding
- N64 (= N81) binding
- C73 (= C90) 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 91:92) binding
- N157 (= N175) binding
- N190 (= N208) binding
- ER 208:209 (= ER 226:227) binding
- C217 (= C235) 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 236:237) binding
3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
37% identity, 93% coverage: 18:288/292 of query aligns to 17:297/301 of 3ejxD
- active site: C89 (= C90), H180 (= H177), E235 (= E226), C244 (= C235), G247 (= G238)
- binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N28), F29 (= F30), N80 (= N81), P86 (≠ S87), C89 (= C90), G90 (= G91), N91 (= N92), N178 (= N175), N217 (= N208), E235 (= E226), R236 (= R227), C244 (= C235), G245 (= G236), T246 (≠ S237)
3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
37% identity, 93% coverage: 18:288/292 of query aligns to 3:283/287 of 3ekmA
- active site: C75 (= C90), H166 (= H177), E221 (= E226), C230 (= C235), G233 (= G238)
- binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N28), N66 (= N81), P72 (≠ S87), C75 (= C90), G76 (= G91), N77 (= N92), N164 (= N175), N203 (= N208), E221 (= E226), R222 (= R227), C230 (= C235), G231 (= G236), T232 (≠ S237)
5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
32% identity, 92% coverage: 20:289/292 of query aligns to 7:274/280 of 5m47A
- active site: C83 (= C90), H161 (= H177), E212 (= E226), C221 (= C235), G224 (= G238)
- binding 2,6-diaminopimelic acid: N15 (= N28), N74 (= N81), C83 (= C90), G84 (= G91), N85 (= N92), N159 (= N175), N194 (= N208), E212 (= E226), R213 (= R227), C221 (= C235), G222 (= G236), T223 (≠ S237)
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)
32% identity, 92% coverage: 20:289/292 of query aligns to 7:274/277 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)
30% identity, 93% coverage: 20:292/292 of query aligns to 3:287/289 of P9WP19
- C87 (= C90) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
- C226 (= C235) 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_057508891.1 NCBI__GCF_001431535.1:WP_057508891.1
MTAAGRQPGRQPPRGAPLRFSKMHGAGNDFIMIDLRDGTPPPSPQLAARLADRHTGVGCD
QIITIEPPRSATAVASYRIWNSDGSSSQQCGNGARCVAAWLVRNGDTADSEFAIDSPLAT
HPVRTLGEDHFAVEMGVPVFEPAQIPLIGFAHPRDEYLLPVQGETVRFGAVSMGNPHAVI
EVGLVDAAPVERLGASLQQHASFPESVNVGFAQVLEPDHARLRVYERGVGETLACGSGAC
AAAVSLMQRGRLGPDARISLPGGELRIQWAGEGQPVVMSGPSAFVFEGEWNA
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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