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, 94% coverage: 10:284/292 of query aligns to 3:273/274 of P44859

query
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P44859

F

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N11 (= N18) binding substrate
Q44 (≠ G51) binding substrate
N64 (= N69) binding substrate
C73 (≠ S78) 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 79:80) binding substrate
N157 (= N169) binding substrate
N190 (= N202) binding substrate
ER 208:209 (= ER 220:221) binding substrate
C217 (≠ S229) 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 230:231) binding substrate

P0A6K1 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Escherichia coli (strain K12) (see paper)
33% identity, 94% coverage: 10:283/292 of query aligns to 3:272/274 of P0A6K1

query
sites
P0A6K1

F

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Y268 (≠ C279) 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 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
28% identity, 88% coverage: 10:266/292 of query aligns to 7:259/277 of Q8NP73

query
sites
Q8NP73

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N15 (= N18) binding substrate
GN 84:85 (= GN 79:80) binding substrate
N159 (= N169) binding substrate
N194 (= N202) binding substrate
ER 212:213 (= ER 220:221) binding substrate
GT 222:223 (≠ GS 230:231) binding substrate

5m47A Crystal structure of dapf from corynebacterium glutamicum in complex with d,l-diaminopimelate (see paper)
28% identity, 88% coverage: 10:266/292 of query aligns to 7:259/280 of 5m47A

query
sites
5m47A

F

F

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D

active site: C83 (≠ S78), H161 (= H171), E212 (= E220), C221 (≠ S229), G224 (≠ S232)
binding 2,6-diaminopimelic acid: N15 (= N18), N74 (= N69), C83 (≠ S78), G84 (= G79), N85 (= N80), N159 (= N169), N194 (= N202), E212 (= E220), R213 (= R221), C221 (≠ S229), G222 (= G230), T223 (≠ S231)

P9WP19 Diaminopimelate epimerase; DAP epimerase; PLP-independent amino acid racemase; EC 5.1.1.7 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
25% identity, 97% coverage: 9:291/292 of query aligns to 2:288/289 of P9WP19

query
sites
P9WP19

F

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A

-

V

-

G

-

V

-

L

-

D

-

S

-

L

-

P

-

E

-

G

-

V

-

R

-

V

-

T

D

D

F

W

K

Y

L

M

R

D

I

Y

F

R

N

N

P

A

D

D

G

G

S

S

E

A

A

A

E

Q

K

M

S
x
C

G

G

N

N

G

G

L

V

R

R

I

V

F

F

C

A

K

H

F

Y

L

L

Y

R

D

A

Y

S

G

G

Y

L

T

E

N

V

K

R

E

D

E

E

F

F

T

V

V

V

E

G

T

S

K

L

G

A

G

G

L

-

V

P

R

R

A

P

K

V

I

T

E

C

E

H

K

H

N

V

K

E

F

A

G

A

K

Y

A

A

K

D

V

V

I

-

T

S

V

V

D

D

M

M

G

G

K

K

A

A

I

-

F

-

E

-

A

-

S

-

K

-

I

-

P

-

V

-

K

-

T

-

D

-

K

N

K

R

E

L

F

G

L

A

G

G

E

E

K

A

V

V

K

-

V

V

G

G

D

G

K

R

E

R

Y

F

E

H

V

G

N

L

C

A

V

V

S

D

V

V

G

G

N

N

P

P

H

H

C

L

V

A

I

C

I

V

K

D

K

S

E

Q

L

L

N

T

E

V

E

D

E

G

I

L

K

A

T

A

Y

L

-

D

-

V

G

G

S

A

L

P

I

V

E

S

-

F

N

D

H

G

P

A

L

Q

F

F

P

P

N

D

R

G

I

V

N

N

V

V

Q

E

F

V

V

L

K

T

P

A

I

P

S

V

E

D

D

G

Q

A

A

V

E

W

I

M

L

R

I

V

W

H

E

E

R

R

G

G

A

V

G

G

F

E

T

T

Y

R

A

S

S
x
C

G

G

S

T

S

G

S

T

-

V

C

A

A

A

V

A

A

V

S

A

V

A

L

L

V

A

K

A

K

V

G

G

L

S

A

P

K

T

N

G

D

T

I

L

T

T

I

V

K

H

M

V

I

P

G

G

E

E

L

V

K

V

I

V

T

T

V

V

D

-

K

T

D

D

W

A

N

T

I

S

R

F

M

L

T

R

G

G

E

P

V

S

Q

V

E

L

I

V

C

A

R

R

G

G

I

D

I

L

S

A

E

D

F

W

L

W

E

N

S

A

I

M

C87 (≠ S78) active site, Proton donor; mutation to A: Completely abolishes the diaminopimelate epimerase activity.; mutation to S: Strongly reduces the diaminopimelate epimerase activity.
C226 (≠ S229) 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_228357427.1 NCBI__GCF_000021545.1:WP_228357427.1
MKRIMDKNFFVKSHGLGNDYIVIDSENITFEITQDFIKKICDVHYGIGSDGILVKYPSSV
ADFKLRIFNPDGSEAEKSGNGLRIFCKFLYDYGYTNKEEFTVETKGGLVRAKIEEKNKFG
KAKVITVDMGKAIFEASKIPVKTDKKEFLGEKVKVGDKEYEVNCVSVGNPHCVIIKKELN
EEEIKTYGSLIENHPLFPNRINVQFVKPISEDQAEILIWERGAGFTYASGSSSCAVASVL
VKKGLAKNDITIKMIGGELKITVDKDWNIRMTGEVQEICRGIISEEFLESIK

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