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)
48% identity, 98% coverage: 3:288/292 of query aligns to 1:274/274 of P44859

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P44859

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N11 (= N13) binding substrate
Q44 (= Q46) binding substrate
N64 (= N66) binding substrate
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 substrate
N157 (= N170) binding substrate
N190 (= N203) binding substrate
ER 208:209 (= ER 221:222) binding substrate
C217 (= C230) 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 231:232) binding substrate

P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
50% identity, 98% coverage: 3:288/292 of query aligns to 1:274/274 of P0A6K1

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P0A6K1

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Y268 (≠ F282) Important for dimerization; mutation to A: Significantly less active than the wild-type dimer and unable to dimerize.

3ejxD Crystal structure of diaminopimelate epimerase from arabidopsis thaliana in complex with ll-azidap (see paper)
39% identity, 97% coverage: 3:285/292 of query aligns to 17:298/301 of 3ejxD

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3ejxD

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active site: C89 (= C75), H180 (= H172), E235 (= E221), C244 (= C230), G247 (= G233)
binding (2s,6s)-2,6-diamino-2-methylheptanedioic acid: N27 (= N13), F29 (= F15), N80 (= N66), P86 (≠ V72), C89 (= C75), G90 (= G76), N91 (= N77), N178 (= N170), N217 (= N203), E235 (= E221), R236 (= R222), C244 (= C230), G245 (= G231), T246 (= T232)

3ekmA Crystal structure of diaminopimelate epimerase form arabidopsis thaliana in complex with irreversible inhibitor dl-azidap (see paper)
39% identity, 97% coverage: 3:285/292 of query aligns to 3:284/287 of 3ekmA

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3ekmA

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active site: C75 (= C75), H166 (= H172), E221 (= E221), C230 (= C230), G233 (= G233)
binding (2r,6s)-2,6-diamino-2-methylheptanedioic acid: N13 (= N13), N66 (= N66), P72 (≠ V72), C75 (= C75), G76 (= G76), N77 (= N77), N164 (= N170), N203 (= N203), E221 (= E221), R222 (= R222), C230 (= C230), G231 (= G231), T232 (= T232)

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)
31% identity, 99% coverage: 1:288/292 of query aligns to 3:277/277 of Q8NP73

query
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Q8NP73

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L

Q

T

I

I

R

P

F

F

T

A

K

K

M

G

Q

H

G

A

A

T

G

E

N
|
N

D

D

F

F

V

I

L

I

D

P

E

D

T

E

R

D

E

A

R

R

L

L

G

D

L

L

T

T

P

P

A

E

Q

M

Y

V

R

V

F

T

L

L

A

C

D

D

R

R

H

R

F

A

G

G

V

I

G

G

A

A

D

D

Q

G

I

I

L

L

-

R

T

V

V

V

R

K

P

A

S

A

P

D

A

V

E

E

G

G

I

S

D

T

F

V

E

D

Y

P

L

S

I

L

-

W

-

F

-

M

-

D

-

Y

H

R

N

N

A

A

D

D

G

G

G

S

Q

L

V

A

Q

E

Q

M

C

C

G
|
G

N
|
N

G

G

A

V

R

R

C

L

F

F

A

A

R

H

Y

W

V

L

R

Y

D

S

K

R

G

G

L

L

T

V

A

D

K

N

D

T

R

S

I

F

R

D

V

I

Q

G

T

T

M

R

A

A

G

G

V

V

I

R

A

H

P

V

E

D

-

I

L

L

T

Q

A

A

D

D

-

Q

-

H

-

S

G

A

R

Q

V

V

T

R

V

V

D

D

M

M

G

G

R

I

P

P

V

-

L

-

D

-

P

-

A

-

R

-

L

-

P

-

F

-

D

D

T

V

A

T

G

G

L

L

V

S

P

T

V

C

P

D

Q

-

G

-

S

-

V

-

K

-

W

-

P

-

L

-

A

-

L

I

D

N

G

G

Q

Q

A

V

P

F

Q

A

A

G

T

-

V

-

M

-

I

-

V

L

A

G

V

V

S

D

M

M

G

G

N
|
N

P

P

H

H

A

L

V

A

Q

C

L

V

V

V

D

P

D

G

V

L

D

S

S

A

A

S

P

A

V

L

A

A

R

D

T

M

-

E

-

L

-

R

G

A

P

P

L

T

I

F

E

D

G

-

H

Q

P

E

R

F

F

F

P

P

Q

H

R

G

V

V

N
|
N

A

V

G

E

Y

I

L

V

Q

T

V

E

V

L

G

E

R

D

T

D

E

A

V

V

R

S

L

M

R

R

V

V

Y

W

E
|
E

R
|
R

G

G

A

V

G

G

E

E

T

T

L

R

A

S

C

C

G
|
G

T
|
T

G

G

A

T

C

V

-

A

A

A

V

C

V

A

A

A

G

L

I

A

G

D

L

A

G

G

L

L

L

G

D

E

A

G

R

T

V

V

D

K

V

V

H

C

T

V

R

P

G

G

L

E

L

V

T

E

I

V

A

Q

W

I

A

-

G

-

L

F

Q

D

D

D

P

G

V

S

F

T

M

L

T

T

G

G

P

P

A

S

T

A

T

I

V

I

F

A

E

L

G

G

Q

E

I

V

D

Q

I

I

N15 (= N13) binding substrate
GN 84:85 (= GN 76:77) binding substrate
N159 (= N170) binding substrate
N194 (= N203) binding substrate
ER 212:213 (= ER 221:222) binding substrate
GT 222:223 (= GT 231:232) binding substrate

5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
31% identity, 99% coverage: 1:288/292 of query aligns to 3:277/280 of 5m47A

query
sites
5m47A

M

L

Q

T

I

I

R

P

F

F

T

A

K

K

M

G

Q

H

G

A

A

T

G

E

N
|
N

D

D

F

F

V

I

L

I

D

P

E

D

T

E

R

D

E

A

R

R

L

L

G

D

L

L

T

T

P

P

A

E

Q

M

Y

V

R

V

F

T

L

L

A

C

D

D

R

R

H

R

F

A

G

G

V

I

G

G

A

A

D

D

Q

G

I

I

L

L

-

R

T

V

V

V

R

K

P

A

S

A

P

D

A

V

E

E

G

G

I

S

D

T

F

V

E

D

Y

P

L

S

I

L

-

W

-

F

-

M

-

D

-

Y

H

R

N
|
N

A

A

D

D

G

G

G

S

Q

L

V

A

Q

E

Q

M

C
|
C

G
|
G

N
|
N

G

G

A

V

R

R

C

L

F

F

A

A

R

H

Y

W

V

L

R

Y

D

S

K

R

G

G

L

L

T

V

A

D

K

N

D

T

R

S

I

F

R

D

V

I

Q

G

T

T

M

R

A

A

G

G

V

V

I

R

A

H

P

V

E

D

-

I

L

L

T

Q

A

A

D

D

-

Q

-

H

-

S

G

A

R

Q

V

V

T

R

V

V

D

D

M

M

G

G

R

I

P

P

V

-

L

-

D

-

P

-

A

-

R

-

L

-

P

-

F

-

D

D

T

V

A

T

G

G

L

L

V

S

P

T

V

C

P

D

Q

-

G

-

S

-

V

-

K

-

W

-

P

-

L

-

A

-

L

I

D

N

G

G

Q

Q

A

V

P

F

Q

A

A

G

T

-

V

-

M

-

I

-

V

L

A

G

V

V

S

D

M

M

G

G

N
|
N

P

P

H
|
H

A

L

V

A

Q

C

L

V

V

V

D

P

D

G

V

L

D

S

S

A

A

S

P

A

V

L

A

A

R

D

T

M

-

E

-

L

-

R

G

A

P

P

L

T

I

F

E

D

G

-

H

Q

P

E

R

F

F

F

P

P

Q

H

R

G

V

V

N
|
N

A

V

G

E

Y

I

L

V

Q

T

V

E

V

L

G

E

R

D

T

D

E

A

V

V

R

S

L

M

R

R

V

V

Y

W

E
|
E

R
|
R

G

G

A

V

G

G

E

E

T

T

L

R

A

S

C
|
C

G
|
G

T
|
T

G
|
G

A

T

C

V

-

A

A

A

V

C

V

A

A

A

G

L

I

A

G

D

L

A

G

G

L

L

L

G

D

E

A

G

R

T

V

V

D

K

V

V

H

C

T

V

R

P

G

G

L

E

L

V

T

E

I

V

A

Q

W

I

A

-

G

-

L

F

Q

D

D

D

P

G

V

S

F

T

M

L

T

T

G

G

P

P

A

S

T

A

T

I

V

I

F

A

E

L

G

G

Q

E

I

V

D

Q

I

I

active site: C83 (= C75), H161 (= H172), E212 (= E221), C221 (= C230), G224 (= G233)
binding 2,6-diaminopimelic acid: N15 (= N13), N74 (= N66), C83 (= C75), G84 (= G76), N85 (= N77), N159 (= N170), N194 (= N203), E212 (= E221), R213 (= R222), C221 (= C230), G222 (= G231), T223 (= T232)

P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 78% coverage: 5:233/292 of query aligns to 3:229/289 of P9WP19

query
sites
P9WP19

F

F

T

A

K

K

M

G

Q

H

G

G

A

T

G

Q

N

N

D

D

F

F

V

V

V

L

L

L

D

P

E

D

T

V

R

D

E

A

R

E

L

L

G

V

L

L

T

T

P

A

A

A

Q

R

Y

V

R

A

F

A

L

L

A

C

D

D

R

R

H

R

F

K

G

G

V

L

G

G

A

A

D

D

Q

G

I

V

L

L

T

R

V

V

R

T

P

T

S

A

P

G

A

A

-

A

-

Q

-

A

-

V

-

G

-

V

-

L

-

D

-

S

-

L

-

P

E

E

G

G

I

V

-

R

-

V

-

T

D

D

F

W

E

Y

Y

M

L

D

I

Y

H

R

N

N

A

A

D

D

G

G

G

S

Q

A

V

A

Q

Q

Q

M

C
|
C

G

G

N

N

G

G

A

V

R

R

C

V

F

F

A

A

R

H

Y

Y

V

L

R

R

D

A

K

S

G

G

L

L

T

E

A

V

K

R

D

D

R

E

I

F

R

V

V

V

Q

G

T

S

M

L

A

A

G

G

-

P

-

R

-

P

V

V

I

T

A

C

P

H

E

H

L

V

T

E

A

A

D

A

-

Y

G

A

R

D

V

V

T

S

V

V

D

D

M

M

G

G

R

K

P

A

V

-

L

-

D

-

P

-

A

-

R

-

L

-

P

-

F

-

D

N

T

R

A

L

G

G

L

A

V

G

P

E

V

A

P

V

Q

V

G

G

S

G

V

R

K

R

K

F

W

H

P

G

L

L

A

A

L

V

D

D

G

-

Q

-

A

-

P

-

Q

-

A

-

T

-

V

-

M

-

I

-

V

-

A

-

V

-

S

-

M

V

G

G

N

N

P

P

H

H

A

-

V

L

Q

A

L

C

V

V

D

D

D

S

-

Q

-

L

-

T

V

V

D

D

S

G

A

L

P

A

V

A

A

L

R

D

T

V

G

G

-

A

P

P

L

V

I

S

E

F

G

D

H

G

P

A

R

Q

F

F

P

P

Q

D

R

G

V

V

N

N

A

V

G

E

Y

V

L

L

Q

T

V

A

V

P

G

V

R

D

T

G

E

A

V

V

R

W

L

M

R

R

V

V

Y

H

E

E

R

R

G

G

A

V

G

G

E

E

T

T

L

R

A

S

C
|
C

G

G

T

T

G

G

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 (= C230) 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_013723008.1 NCBI__GCF_000204645.1:WP_013723008.1
MQIRFTKMQGAGNDFVVLDETRERLGLTPAQYRFLADRHFGVGADQILTVRPSPAEGIDF
EYLIHNADGGQVQQCGNGARCFARYVRDKGLTAKDRIRVQTMAGVIAPELTADGRVTVDM
GRPVLDPARLPFDTAGLVPVPQGSVKKWPLALDGQAPQATVMIVAVSMGNPHAVQLVDDV
DSAPVARTGPLIEGHPRFPQRVNAGYLQVVGRTEVRLRVYERGAGETLACGTGACAAVVA
GIGLGLLDARVDVHTRGGLLTIAWAGGLQDPVFMTGPATTVFEGQIDIPETP

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