SitesBLAST

E86 (= E82) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
D96 (= D92) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
R130 (= R125) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
R134 (= R129) 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 (= R130) 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 (≠ H131) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
D165 (≠ E159) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D172 (= D166) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
E236 (= E231) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D293 (= D288) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
D330 (≠ E325) 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)
34% identity, 94% coverage: 14:335/342 of query aligns to 17:338/410 of 2a5hB

query
sites
2a5hB

D

D

W

W

L

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W

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Q

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A

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N

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K

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A

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N

E

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A

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C

A

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R

K

R

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L

F

R

A

M

L

A

R

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P

P

R

-

A

Y

F

Y

I

L

A

S

R

L

M

I

E

D

P

P

G

N

N

D

P

P

N

N

D

D

P

P

L

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L

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R

K

Q

Q

V

A

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A

E

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N

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K

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A

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A

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A

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D

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L
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L

-

H

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D

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D

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S

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P

G

G

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L
x
T

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x
R

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Y

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N

D

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R

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L

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C
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C

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C
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C

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x
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C

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R

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G

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R

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x
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K

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V

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L

W

L

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N

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H
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H

I

F

N

N

H

H

A

P

N

N

E

E

I

I

D

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T

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A

A

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L

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A

A

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G

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N

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Q

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V

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R

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G

V

V

N

N

D

D

D

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D

E

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N

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D
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D

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A

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H

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E

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G

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Y

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A

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D

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G

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K

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V

active site: R110 (≠ K107), Y111 (= Y108), R114 (= R111), C123 (= C120), C127 (= C124), C130 (= C127), R132 (= R129), D291 (= D288), D328 (≠ E325), K335 (= K332)
binding lysine: L96 (= L94), L116 (= L113), R132 (= R129), L165 (≠ I161), S167 (= S163), Y288 (≠ H285), D291 (= D288), D328 (≠ E325)
binding pyridoxal-5'-phosphate: T108 (≠ L105), Y111 (= Y108), R114 (= R111), L116 (= L113), R196 (= R192), Y285 (= Y282), Y286 (= Y283), K335 (= K332)
binding s-adenosylmethionine: H129 (≠ Y126), T131 (≠ F128), R132 (= R129), S167 (= S163), G169 (= G165), G198 (≠ H194), H228 (= H225), Q256 (= Q253), V258 (= V255), Y288 (≠ H285), C290 (≠ L287), D291 (= D288)
binding iron/sulfur cluster: C123 (= C120), C127 (= C124), C130 (= C127), G169 (= G165), R200 (= R196), H228 (= H225)

Sites not aligning to the query:

binding zinc ion: 373, 375, 378

O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
34% identity, 94% coverage: 14:335/342 of query aligns to 28:349/471 of O34676

query
sites
O34676

D

D

W

W

L

L

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W

Q

Q

L

L

A

T

D

H

V

T

V

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D

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N

N

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D

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D

D

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E

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G

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Y

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Y

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A

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M

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D

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N

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Q

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D

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E

D

D

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P

L

L

-

H

E

E

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D

Q

E

H

D

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S

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V

P

P

G

G

L

L

L

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Y

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D

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G

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D

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V

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L

L

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N

N

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H

H

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N

N

H

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N

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E

I

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D

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A

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N

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Q

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N

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D

D

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x
K

A

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Y

Y

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D

D

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L

K290 (≠ D276) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
K346 (= K332) mutation to Q: No activity and no bound PLP.

Sites not aligning to the query:

361 K→Q: 95% loss of activity, normal PLP binding capacity.

Query Sequence

>BWI76_RS02410 FitnessBrowser__Koxy:BWI76_RS02410
MAHIVTLNTPSREDWLTQLADVVTSPDELLHLLNVDADANLLAGRDARRLFALRVPRAFI
ARMEPGNPNDPLLRQVLTSREEFVNAPGFTTDPLEEQHSVVPGLLHKYSNRALLLVKGGC
AVNCRYCFRRHFPYAENQGNKRNWQMAMEYIASHPELDEIIFSGGDPLMAKDPELDWLLT
QLEAIPHIKRLRIHSRLPIVIPARITDTLIARISASSLQVLLVNHINHANEIDAAFRTAM
KSLRIAGVTLLNQSVLLRGVNDDARTLADLSNALFDAGVMPYYLHVLDRVQGAAHFMVSD
EEARKIMRELLTMVSGYLVPKLAREIGGEPSKTPLDLGLKQR

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