SitesBLAST

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)
36% identity, 99% coverage: 1:270/274 of query aligns to 1:270/274 of P44859

query
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P44859

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N11 (= N11) binding substrate
Q44 (≠ G45) binding substrate
N64 (= N63) binding substrate
C73 (= C72) 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 73:74) binding substrate
N157 (≠ V160) binding substrate
N190 (= N191) binding substrate
ER 208:209 (= ER 209:210) binding substrate
C217 (= C218) 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 219:220) 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)
33% identity, 100% coverage: 1:274/274 of query aligns to 5:277/277 of Q8NP73

query
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Q8NP73

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N15 (= N11) binding substrate
GN 84:85 (= GN 73:74) binding substrate
N159 (≠ V160) binding substrate
N194 (= N191) binding substrate
ER 212:213 (= ER 209:210) binding substrate
GT 222:223 (= GT 219:220) binding substrate

5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
33% identity, 100% coverage: 1:274/274 of query aligns to 5:277/280 of 5m47A

query
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5m47A

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active site: C83 (= C72), H161 (= H162), E212 (= E209), C221 (= C218), G224 (= G221)
binding 2,6-diaminopimelic acid: N15 (= N11), N74 (= N63), C83 (= C72), G84 (= G73), N85 (= N74), N159 (≠ V160), N194 (= N191), E212 (= E209), R213 (= R210), C221 (= C218), G222 (= G219), T223 (= T220)

P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
28% identity, 99% coverage: 1:271/274 of query aligns to 1:279/289 of P9WP19

query
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P9WP19

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C87 (= C72) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
C226 (= C218) 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_012101584.1 NCBI__GCF_000016505.1:WP_012101584.1
MKFTKMHGTGNDFIVIDDRENRFLGKEEELALRLCNRHFGIGADGVLIVRNSDIASIKMV
IINSDGSYASMCGNGIRCFAKYIWEENLVKDKILKIETGDGIKEAVVTIKNGKAEEITID
MGMPSFAPRKVPVEFKEEVIEKEVKIKNKNYIITTLFMGVPHTVIFGKLEDYDVAEGEYI
EKYPVFTQGTNVNFCEIVNEKEVKVKTWERGAGPTLACGTGSCACVVAANKIGLTGKEVK
VSVPGGILLVEIKDDNSVFMTGPAAISFKGEYDI

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