SitesBLAST

E86 (= E64) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
D96 (= D72) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
R130 (= R106) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
R134 (= R110) mutation to K: Complete loss of activity. Significant decrease in iron and sulfide and PLP content.; mutation to Q: Complete loss of activity. Slight decrease in iron and sulfide and PLP content.
R135 (≠ K111) mutation to K: Reduction in activity. Decrease in iron and sulfide and PLP content.; mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
R136 (= R112) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
D165 (= D140) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D172 (= D147) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
E236 (= E217) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D293 (≠ R274) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.

Sites not aligning to the query:

330 mutation D->A,N: Complete loss of activity. Decrease in iron and sulfide and PLP content.

2a5hB 2.1 angstrom x-ray crystal structure of lysine-2,3-aminomutase from clostridium subterminale sb4, with michaelis analog (l-alpha-lysine external aldimine form of pyridoxal-5'-phosphate). (see paper)
37% identity, 70% coverage: 40:302/374 of query aligns to 60:319/410 of 2a5hB

query
sites
2a5hB

Y

Y

L

L

S

S

L

L

I

I

N

D

H

P

N

N

N

D

P

P

N

N

D

D

P

P

I

V

K

R

R

K

I

Q

I

A

L

I

P

P

D

T

P

A

C

L

E

E

L

L

A

N

N

K

P

A

G

A

S

A

-

D

-

L

L

E

D

D

P

P

S
x
L

G

H

E

E

E

D

E

T

Y

D

S

S

P

P

L

V

P

P

G

G

V

L

Q
x
T

H

H

K
x
R

Y
|
Y

P

P

Q

D

T
x
R

A

V

M
x
L

L

L

V

I

S

T

N

D

T

M

C
|
C

G

S

G

M

I

Y

C
|
C

R

R

F
x
H

C
|
C

F
x
T

R
|
R

K

R

R

R

L

-

F

F

T

A

G

G

E

Q

-

S

-

D

N

D

P

S

P

M

P

P

I

M

C

E

D

R

T

I

K

D

K

K

A

A

V

I

D

D

Y

Y

L

I

Q

R

T

N

Q

T

K

P

D

Q

L

V

T

R

D

D

V

V

L
|
L

L

L

S
|
S

G

G

G
|
G

D

D

P

A

L

L

M

L

L

V

G

S

A

D

S

E

K

T

L

L

D

E

Q

Y

I

I

L

I

S

A

M

K

I

L

R

R

E

E

L

I

P

P

T

H

K

V

P

E

I

I

I

V

R
|
R

I

I

G
|
G

T

S

K
x
R

I

T

P

P

A

V

Y

V

D

L

P

P

H

Q

R

R

L

I

T

T

D

-

S

P

D

E

L

L

R

V

D

N

V

M

L

L

A

K

K

K

H

Y

T

-

S

-

P

-

E

-

E

H

K

P

I

V

Y

W

L

L

I

N

S

T

H
|
H

F

F

N

N

H

H

P

P

Q

N

E

E

I

I

T

T

S

E

S

S

K

T

A

R

A

A

I

C

S

Q

A

L

L

L

K

A

N

D

T

A

G

G

A

V

E

P

L

L

T

G

N

N

Q
|
Q

T

S

P
x
V

I

L

L

L

Q

R

G

G

I

V

N

N

N

D

E

C

P

V

D

H

I

V

M

M

A

K

S

E

L

L

F

V

N

N

I

K

L

L

S

V

K

K

L

I

G

R

V

V

P

R

P

P

Y
|
Y

V

I

F
x
Y

Q

Q

C
|
C

R
x
D

P

L

T

S

S

L

G

G

N

L

R

E

H

H

L

F

T

R

V

T

P

P

I

V

E

S

Q

K

A

G

M

I

H

E

V

I

I

I

H

E

E

G

A

L

Q

R

S

G

C

H

C

T

S

S

G

G

active site: R110 (≠ K88), Y111 (= Y89), R114 (≠ T92), C123 (= C101), C127 (= C105), C130 (= C108), R132 (= R110), D291 (≠ R274)
binding lysine: L96 (≠ S74), L116 (≠ M94), R132 (= R110), L165 (= L142), S167 (= S144), Y288 (≠ F271), D291 (≠ R274)
binding pyridoxal-5'-phosphate: T108 (≠ Q86), Y111 (= Y89), R114 (≠ T92), L116 (≠ M94), R196 (= R173), Y285 (= Y268), Y286 (= Y269)
binding s-adenosylmethionine: H129 (≠ F107), T131 (≠ F109), R132 (= R110), S167 (= S144), G169 (= G146), G198 (= G175), H228 (= H211), Q256 (= Q239), V258 (≠ P241), Y288 (≠ F271), C290 (= C273), D291 (≠ R274)
binding iron/sulfur cluster: C123 (= C101), C127 (= C105), C130 (= C108), G169 (= G146), R200 (≠ K177), H228 (= H211)

Sites not aligning to the query:

O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
34% identity, 73% coverage: 31:302/374 of query aligns to 62:330/471 of O34676

query
sites
O34676

R

K

V

T

Y

I

P

P

F

L

R

N

S

I

N

T

E

P

Y

Y

L

A

S

S

L

L

I

M

N

D

H

P

N

D

N

N

P

P

N

R

D

C

P

P

I

V

K

R

R

M

I

Q

I

S

L

V

P

P

D

L

P

S

C

E

E

E

L

M

A

H

N

K

P

T

G

K

S

Y

-

D

-

L

L

E

D

D

P

P

S

L

G

H

E

E

E

D

E

E

Y

D

S

S

P

P

L

V

P

P

G

G

V

L

Q

T

H

H

K

R

Y

Y

P

P

Q

D

T

R

A

V

M

L

L

F

L

L

V

V

S

T

N

N

T

Q

C

C

G

S

G

M

I

Y

C

C

R

R

F

Y

C

C

F

T

R

R

K

R

R

R

L

-

F

F

T

S

G

G

E

Q

-

I

-

G

N

M

P

G

P

V

P

P

I

K

C

K

D

Q

T

L

K

D

K

A

A

A

V

I

D

A

Y

Y

L

I

Q

R

T

E

Q

T

K

P

D

E

L

I

T

R

D

D

V

C

L

L

L

I

S

S

G

G

D

D

P

G

L

L

M

L

L

I

G

N

A

D

S

Q

K

I

L

L

D

E

Q

Y

I

I

L

L

S

K

M

E

I

L

R

R

E

S

L

I

P

P

T

H

K

L

P

E

I

V

I

I

R

R

I

I

G

G

T

T

K

R

I

A

P

P

A

V

Y

V

D

F

P

P

H

Q

R

R

L

I

T

T

D

D

D

H

S

-

D

-

L

L

R

C

D

E

V

I

L

L

A

K

K

K

H

Y

T

-

S

-

P

-

E

-

E

H

K

P

I

V

Y

W

L

L

I

N

S

T

H

H

F

F

N

N

H

T

P

S

Q

I

E

E

I

M

T

T

S

E

S

S

K

V

A

E

A

A

I

C

S

E

A

K

L

L

K

V

N

N

T

A

G

G

A

V

E

P

L

V

T

G

N

N

Q

Q

T

A

P

V

I

V

L

L

Q

A

G

G

I

I

N

N

N

D

E

S

P

V

D

P

I

I

M

M

A

K

S

K

L

L

F

M

N

H

I

D

L

L

S

V

K
|
K

L

I

G

R

V

V

P

R

P

P

Y

Y

V

I

F

Y

Q

Q

C

C

R

D

P

L

T

S

S

E

G

G

N

I

R

G

H

H

L

F

T

R

V

A

P

P

I

V

E

S

Q

K

A

G

M

L

H

E

V

I

I

I

H

E

E

G

A

L

Q

R

S

G

C

H

C

T

S

S

G

G

K290 (= K262) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.

Sites not aligning to the query:

346 K→Q: No activity and no bound PLP.
361 K→Q: 95% loss of activity, normal PLP binding capacity.

Query Sequence

>WP_109968124.1 NCBI__GCF_003173355.1:WP_109968124.1
MSTKYYNSVHETSLSDVLDPDQVLKMEDVERVYPFRSNEYYLSLINHNNPNDPIKRIILP
DPCELANPGSLDPSGEEEYSPLPGVQHKYPQTAMLLVSNTCGGICRFCFRKRLFTGENPP
PICDTKKAVDYLQTQKDLTDVLLSGGDPLMLGASKLDQILSMIRELPTKPIIRIGTKIPA
YDPHRLTDDSDLRDVLAKHTSPEEKIYLISHFNHPQEITSSSKAAISALKNTGAELTNQT
PILQGINNEPDIMASLFNILSKLGVPPYYVFQCRPTSGNRHLTVPIEQAMHVIHEAQSCC
SGLTKRARYIMSHKSGKIEIVGKTSKHIFMKYHQAASLSDLNSMLVFKPNSRARWLEDYQ
HRLTDMVPKMTWLF

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