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)
41% identity, 99% coverage: 1:274/278 of query aligns to 1:271/274 of P44859

query
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P44859

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N11 (= N11) binding substrate
Q44 (≠ G44) binding substrate
N64 (= N62) binding substrate
C73 (= C71) 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 72:73) binding substrate
N157 (= N160) binding substrate
N190 (= N193) binding substrate
ER 208:209 (= ER 211:212) binding substrate
C217 (= C220) 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 221:222) binding substrate

P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
40% identity, 99% coverage: 1:274/278 of query aligns to 1:271/274 of P0A6K1

query
sites
P0A6K1

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Y268 (≠ F271) Important for dimerization; mutation to A: Significantly less active than the wild-type dimer and unable to dimerize.

5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
32% identity, 98% coverage: 1:273/278 of query aligns to 5:273/280 of 5m47A

query
sites
5m47A

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active site: C83 (= C71), H161 (= H162), E212 (= E211), C221 (= C220), G224 (= G223)
binding 2,6-diaminopimelic acid: N15 (= N11), N74 (= N62), C83 (= C71), G84 (= G72), N85 (= N73), N159 (= N160), N194 (= N193), E212 (= E211), R213 (= R212), C221 (= C220), G222 (= G221), T223 (= T222)

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)
32% identity, 98% coverage: 1:273/278 of query aligns to 5:273/277 of Q8NP73

query
sites
Q8NP73

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G

N15 (= N11) binding substrate
GN 84:85 (= GN 72:73) binding substrate
N159 (= N160) binding substrate
N194 (= N193) binding substrate
ER 212:213 (= ER 211:212) binding substrate
GT 222:223 (= GT 221:222) binding substrate

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, 98% coverage: 1:273/278 of query aligns to 1:278/289 of P9WP19

query
sites
P9WP19

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V

L

S

C

D

D

R

R

H

R

F

K

G

G

I

L

G

G

S

A

D

D

G

G

L

V

I

L

T

R

I

V

G

T

P

T

S

A

D

G

I

A

A

A

-

Q

-

A

-

V

-

G

-

V

-

L

-

D

-

S

-

L

-

P

-

E

-

G

-

V

-

R

-

V

-

T

D

D

F

W

R

Y

M

M

R

D

I

Y

Y

R

N

N

A

A

D

D

G

G

S

S

E

A

A

A

E

Q

M

M

C
|
C

G

G

N

N

G

G

I

V

R

R

C

V

V

F

A

A

K

H

Y

Y

V

L

Y

R

D

A

H

S

K

G

M

L

T

E

D

V

K

R

K

D

E

E

I

F

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V

I

V

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G

T

S

G

L

A

A

G

G

V

P

K

R

T

P

L

V

Q

T

L

C

T

H

V

H

A

V

D

E

G

A

K

A

V

Y

S

A

L

D

V

V

R

S

V

V

D

D

M

M

G

G

E

-

P

-

I

-

L

-

K

K

P

A

D

N

L

R

I

L

P

-

V

-

D

-

A

G

S

A

G

G

E

E

Q

A

V

V

D

G

E

-

P

-

I

-

E

-

V

-

E

-

G

G

R

R

E

R

W

F

K

H

M

G

T

L

C

A

V

V

S

D

M

V

G

G

N

N

P

P

H

H

A

-

V

-

I

L

F

A

V

C

E

V

D

D

T

S

E

Q

-

L

-

T

-

V

-

D

-

G

H

L

F

A

E

A

L

L

E

D

K

V

Y

G

G

A

P

P

E

V

F

S

E

F

H

D

H

G

P

A

R

Q

F

F

P

P

K

D

R

G

T

V

N

N

T

V

E

E

F

V

V

L

H

T

V

A

I

P

S

V

P

D

T

G

E

A

A

V

S

W

M

M

R

R

V

V

W

H

E

E

R

R

G

G

S

V

A

G

E

E

T

T

L

R

A

S

C
|
C

G

G

T

T

G

G

T

T

C

V

A

A

T

A

V

A

M

V

A

A

C

A

I

L

L

A

N

A

H

V

K

G

T

S

E

P

N

T

K

G

V

T

L

L

-

T

V

V

H

H

L

V

R

P

G

G

D

E

L

V

T

V

I

V

E

T

Y

V

D

T

P

D

D

A

N

T

N

S

H

-

I

-

Y

F

M

L

T

R

G

G

P

P

A

S

T

V

E

L

V

V

F

A

H

R

G

G

C87 (= C71) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
C226 (= C220) 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_022046423.1 NCBI__GCF_001406815.1:WP_022046423.1
MKFTKMHGCGNDYVYVNLFEEKIADPAKVSIAVSDRHFGIGSDGLITIGPSDIADFRMRI
YNADGSEAEMCGNGIRCVAKYVYDHKMTDKKEITIETGAGVKTLQLTVADGKVSLVRVDM
GEPILKPDLIPVDASGEQVVDEPIEVEGREWKMTCVSMGNPHAVIFVEDTEHFELEKYGP
EFEHHPRFPKRTNTEFVHVISPTEASMRVWERGSAETLACGTGTCATVMACILNHKTENK
VLVHLRGGDLTIEYDPDNNHIYMTGPATEVFHGIWEEN

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