SitesBLAST

Q94JQ4 Reactive Intermediate Deaminase A, chloroplastic; 2-iminobutanoate/2-iminopropanoate deaminase; EC 3.5.99.10 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
50% identity, 99% coverage: 2:124/124 of query aligns to 65:187/187 of Q94JQ4

query
sites
Q94JQ4

Q

E

V

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Y

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T

T

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E

K

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A

A

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G

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P

Y

Y

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S

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Q

A

A

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I

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K

Y

A

E

N

N

N

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F

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G

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Q

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N

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A

E

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A

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N

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N

A

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C

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A

A

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L

R165 (= R102) mutation to A: Loss of activity.

3vczB 1.80 angstrom resolution crystal structure of a putative translation initiation inhibitor from vibrio vulnificus cmcp6
46% identity, 98% coverage: 2:122/124 of query aligns to 2:125/127 of 3vczB

query
sites
3vczB

Q

K

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V

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Y

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T

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K

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A

A

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P

K

A

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A

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G

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Q

A

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N

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L

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G

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Q

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D

N

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A

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N

G

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E

F

-

V

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N

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A

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D

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A

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A

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Q

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A

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D

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N

I

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K

A

A

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E

E

A

A

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G

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L

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L

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N

G

H

D

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I

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K

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Y

F

L

V

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K

N
x
D

L

L

E
x
N

D

D

F

F

Q

G

V

T

V

V

N

N

E

E

I

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Y

Y

G

G

E

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Y

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F

F

K

D

D

E

H

H

K

N

-

V

-

A

-

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-

Y

P

P

A

A

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R

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S

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C

V

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E

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K

D

D

A

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E

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I

E

E

V

A

I

I

A

A

binding magnesium ion: D79 (≠ N80), N81 (≠ E82)

Q7CP78 2-iminobutanoate/2-iminopropanoate deaminase; Enamine/imine deaminase; EC 3.5.99.10 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
48% identity, 98% coverage: 2:122/124 of query aligns to 3:125/128 of Q7CP78

query
sites
Q7CP78

Q

K

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A

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Y

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N

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K

A

A

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A

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N

-

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R

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E

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E

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A

Y17 (= Y16) mutation to F: Deaminase activity is defective. At pH 8, strongly reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone. At pH 9.5, moderately reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone.
R105 (= R102) mutation to A: Deaminase activity is defective. At pH 8 and 9.5, strongly reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone.
E120 (= E117) Important for catalytic activity at high pH; mutation to A: Deaminase activity is defective. At pH 8, moderately reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone. At pH 9.5, strongly reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone.; mutation to K: Deaminase activity is defective. At pH 8, moderately reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone. At pH 9.5, strongly reduces the increase in rate of 2-ketobutyrate formation over the rate of IlvA alone.

2uynA Crystal structure of e. Coli tdcf with bound 2-ketobutyrate (see paper)
44% identity, 98% coverage: 2:122/124 of query aligns to 2:124/127 of 2uynA

query
sites
2uynA

Q

K

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D

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F

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A

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Y

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F

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S

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x
C

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L

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D

D

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L

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E

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I

A

A

binding 2-ketobutyric acid: F83 (= F84), R104 (= R102), S105 (= S103), C106 (≠ T104)

2uykC Crystal structure of e. Coli tdcf with bound serine (see paper)
44% identity, 98% coverage: 2:122/124 of query aligns to 2:124/127 of 2uykC

query
sites
2uykC

Q

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A

binding serine: R104 (= R102), S105 (= S103), C106 (≠ T104)

P52759 2-iminobutanoate/2-iminopropanoate deaminase; Liver perchloric acid-soluble protein; L-PSP; Reactive intermediate imine deaminase A homolog; Translation inhibitor L-PSP ribonuclease; UK114 antigen homolog; rp14.5; EC 3.5.99.10 from Rattus norvegicus (Rat) (see paper)
45% identity, 98% coverage: 2:122/124 of query aligns to 7:127/137 of P52759

query
sites
P52759

Q

K

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A

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylserine

P80601 2-iminobutanoate/2-iminopropanoate deaminase; 14.3 kDa perchloric acid soluble protein; Translation inhibitor L-PSP ribonuclease; UK114 antigen; EC 3.5.99.10; EC 3.1.-.- from Capra hircus (Goat) (see paper)
43% identity, 98% coverage: 2:122/124 of query aligns to 7:127/137 of P80601

query
sites
P80601

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I

A

A

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylserine

A0A1J1DL12 2-iminobutanoate/2-iminopropanoate deaminase; Allergen Der f 34; Enamine/imine deaminase; Allergen Der f 34.0101; EC 3.5.99.10 from Dermatophagoides farinae (American house dust mite) (see paper)
43% identity, 97% coverage: 2:121/124 of query aligns to 5:124/128 of A0A1J1DL12

query
sites
A0A1J1DL12

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R

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P

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E

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I

I

Y19 (= Y16) mutation to A: Loss of imine deaminase activity; when associated with A-33; A-59; A-91; A-105; A-114 and A-120.
G33 (= G30) mutation to A: Loss of imine deaminase activity; when associated with A-19; A-59; A-91; A-105; A-114 and A-120.
N59 (= N56) mutation to A: Loss of imine deaminase activity; when associated with A-19; A-33; A-91; A-105; A-114 and A-120.
N91 (= N88) mutation to A: Loss of imine deaminase activity; when associated with A-19; A-33; A-59; A-105; A-114 and A-120.
R105 (= R102) mutation to A: Loss of imine deaminase activity; when associated with A-19; A-33; A-59; A-91; A-114 and A-120.
P114 (= P111) mutation to A: Loss of imine deaminase activity; when associated with A-19; A-33; A-59; A-91; A-105 and A-120.
E120 (= E117) mutation to A: Loss of imine deaminase activity; when associated with A-19; A-33; A-59; A-91; A-105 and A-114.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

3k0tC Crystal structure of pspto -psp protein in complex with d-beta-glucose from pseudomonas syringae pv. Tomato str. Dc3000 (see paper)
45% identity, 96% coverage: 3:121/124 of query aligns to 3:120/124 of 3k0tC

query
sites
3k0tC

V

V

I

I

Y

T

T

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E

D

K

K

A

A

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K

A

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A

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Y

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A

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K

Y

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E

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N

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G

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I
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I

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V

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N

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F

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G

G

E

S

Y

Y

F

F

K

S

D

Q

H

P

K

Y

P

P

A

A

R
|
R

S

A

T

A

V

I

E

G

V

V

S

A

R

A

L

L

P

P

K
x
R

D

G

A

A

L

Q

V

V

E
|
E

I

M

E

D

V

A

I

I

binding beta-D-glucopyranose: Y16 (= Y16), G30 (= G30), I32 (= I32), F83 (= F84), R101 (= R102), R111 (≠ K112), E116 (= E117)

5hp8A Crystal structures of rida in complex with pyruvate (see paper)
48% identity, 87% coverage: 17:124/124 of query aligns to 1:108/108 of 5hp8A

query
sites
5hp8A

S

S

Q

Q

A

A

I

I

K

K

Y

A

E

N

N

N

L

L

I

V

F

F

I

L

S

S

G

G

Q

V

I

L

A

G

I

L

D

I

P

P

S

E

T

T

N

G

E

K

F

F

V

V

N

S

A

E

D

S

V

V

S

E

T

D

Q

Q

T

T

K

E

I

Q

I

V

M

L

E

K

N

N

I

M

K

G

A

E

I

I

L

L

E

K

E

A

A

S

G

G

L

A

N

D

L

Y

N

S

H

S

V

V

I

V

K

K

T

T

I

I

Y

M

L

L

K

A

N

D

L

L

E

A

D

D

F

F

Q

K

V

T

V

V

N

N

E

E

I

I

Y

Y

G

A

E

K

Y

Y

F

F

K

P

D

A

H

P

K

S

P

P

A

A

R
|
R

S

S

T
|
T

V

Y

E

Q

V

V

S

A

R

A

L

L

P

P

K

L

D

N

A

A

L

K

V

I

E

E

I

I

E

E

V

C

I

I

A

A

G

T

L

L

binding pyruvic acid: R86 (= R102), T88 (= T104)

P0AFQ5 3-aminoacrylate deaminase RutC; 3-AA deaminase; EC 3.5.-.- from Escherichia coli (strain K12) (see paper)
31% identity, 98% coverage: 2:122/124 of query aligns to 4:124/128 of P0AFQ5

query
sites
P0AFQ5

Q

S

V

V

I

I

Y

I

T

P

E

A

K

G

A

S

P

S

K

A

P

P

I

L

G

A

P

P

Y

F

S

V

Q

P

A

G

I

T

K

L

Y

A

E

D

N

G

L

V

I

V

F

Y

I

V

S

S

G

G

Q

T

I

L

A

A

I

F

D

D

P

Q

S

H

T

N

N

N

E

V

F

L

V

F

N

A

A

D

D

D

V

P

S

K

T

A

Q

Q

T

T

K

R

I

H

I

V

M

L

E

E

N

T

I

I

K

R

A

K

I

V

L

I

E

E

E

T

A

A

G

G

L

G

N

T

L

M

N

A

H

D

V

V

I

T

K

F

T

N

T

S

I

I

Y

F

L

I

K

T

N

D

L

W

E

K

D

N

F

Y

Q

A

V

A

V

I

N

N

E

E

I

I

Y

Y

G

A

E

E

Y

F

F

F

K

P

D

G

H

D

K

K

P

P

A

A

R
|
R

S

F

T

C

V

I

E

Q

V

C

S

G

R

L

L

V

P

K

K

P

D

D

A

A

L

L

V

V

E

E

I

I

E

A

V

T

I

I

A

A

R104 (= R102) mutation to A: Loss of activity.

3lybB Structure of putative endoribonuclease(kp1_3112) from klebsiella pneumoniae
27% identity, 86% coverage: 16:122/124 of query aligns to 1:132/137 of 3lybB

query
sites
3lybB

Y

Y

S

A

Q

A

A

W

I

R

K

R

Y

A

E

G

N

D

L

F

I

I

F

F

I

L

S

S

G

G

Q

I

I

I

A

P

I

V

D

N

P

P

S

L

T

T

N

G

E

T

F

I

V

V

N
|
N

A

G

-

F

-

Q

-
x
D

-

V

-

P

-

E

-

P

-

V

-

R

-

E

-

L

-

G

-

A

-

T

-

G

D

E

V

F

S

S

T

T

-

D

-

A

-

K

-

Q

-

G

-

P

-

I

-

L

-

A

Q

Q

T

S

K

W

I

Y

I

V

M

L

E

E

N

S

I

I

K

R

A

R

I

T

L

V

E

A

E

S

A

A

G

G

L

G

N

Q

L

M

N

S

H

D

V

V

I

I

K

K

T

L

T

V

I

Q

Y

Y

L

F

K

R

N

N

L

L

E

D

D

H

F

F

Q

P

V

Y

N

S

E

R

I

V

Y

R

G

K

E

L

Y

F

F

Y

K

P

D

D

H

Q

K

P

P

P

A

V

R

S

S

T

T

V

V

V

E

Q

V

V

S

S

R

E

L

M

P

L

K

P

D

D

A

A

L

T

V

V

E

L

I

I

E

E

V

V

I

E

A

A

binding calcium ion: N28 (= N43), D32 (vs. gap)

Q12429 Diphthine--ammonia ligase; Diphthamide synthase; Diphthamide synthetase; EC 6.3.1.14 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
26% identity, 61% coverage: 46:121/124 of query aligns to 335:415/685 of Q12429

query
sites
Q12429

V

V

S

E

T

K

Q

Q

T

S

K

E

I

D

I

I

M

F

E

T

N

E

I

L

K

A

A

D

I

I

L

L

E

H

E

S

A

N

G

Q

L

I

N

P

L

R

N

N

H

H

V

I

I

L

K

S

T

A

T

S

I

L

Y

L

L

I

K

R

N

D

L

M

E

S

D

N

F

F

Q

G

V

K

V

I

N

N

E

K

I

I

Y

Y

G

N

E

E

Y

F

F

L

K

D

D

L

H

S

K

K

-

Y

-

G

-

P

-

L

-

P

P

P

A

S

R

R

S

A

T

C

V

V

E

G

V

S

S

K

R

C

L

L

P

P

K

E

D

D

A

C

L

H

V

V

E

Q

I

L

E

S

V

V

I

V

Sites not aligning to the query:

216 G→N: Completely inactivates the enzyme.
220 mutation E->A,H: Completely inactivates the enzyme. Resistance to sordarin.

Query Sequence

>WP_028951281.1 NCBI__GCF_000619805.1:WP_028951281.1
MQVIYTEKAPKPIGPYSQAIKYENLIFISGQIAIDPSTNEFVNADVSTQTKIIMENIKAI
LEEAGLNLNHVIKTTIYLKNLEDFQVVNEIYGEYFKDHKPARSTVEVSRLPKDALVEIEV
IAGL

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