SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf1N1B4_2010 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2010 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

7kctA Crystal structure of the hydrogenobacter thermophilus 2-oxoglutarate carboxylase (ogc) biotin carboxylase (bc) domain dimer in complex with adenosine 5'-diphosphate magnesium salt (mgadp), adenosine 5'- diphosphate (adp, and bicarbonate anion (hydrogen carbonate/hco3-) (see paper)
55% identity, 95% coverage: 1:449/471 of query aligns to 3:452/453 of 7kctA

query
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7kctA

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active site: E276 (= E274), E289 (= E286), N291 (= N288), E297 (= E294), R339 (= R336)
binding adenosine-5'-diphosphate: K117 (= K115), L157 (≠ M155), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), I169 (= I167), E201 (= E199), Y203 (≠ C201), I204 (= I202), H209 (= H207), Q233 (= Q231), Q237 (= Q235), K238 (= K236), I278 (≠ L276), E289 (= E286), R293 (= R290), Q295 (= Q292), V296 (= V293), E297 (= E294), R339 (= R336)
binding bicarbonate ion: D116 (= D114), R119 (≠ E117)
binding magnesium ion: E276 (= E274), E289 (= E286)

2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
54% identity, 93% coverage: 3:442/471 of query aligns to 1:443/448 of 2vpqB

query
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2vpqB

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active site: V116 (≠ E117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E286), N289 (= N288), R291 (= R290), E295 (= E294), R337 (= R336)
binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (= I167), F200 (≠ C201), I201 (= I202), E273 (= E274), I275 (≠ L276), M286 (= M285), E287 (= E286)
binding magnesium ion: E273 (= E274), E287 (= E286)

A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
49% identity, 94% coverage: 2:445/471 of query aligns to 4:456/1150 of A0A0H3JRU9

query
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A0A0H3JRU9

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G

G

F

Y

A

A

L

I

Q

Q

F

C

R

R

I

I

N

T

A

T

E

E

D

D

P

P

K

L

N

N

N

D

F

F

L

M

P

P

S

D

F

T

G

G

K

T

I

I

T

I

R

A

Y

Y

Y

R

A

S

P

S

G

G

P

F

G

G

V

V

R

R

T

L

D

D

T

A

A

G

I

D

-

G

Y

F

T

Q

G

G

Y

A

T

E

I

I

P

S

P

P

F

Y

Y

Y

D

D

S

S

M

L

C

L

L

V

K

K

L

L

V

S

V

T

W

H

A

A

L

I

T

S

W

F

E

K

E

Q

A

A

M

E

D

E

R
x
K

G

M

L

V

R

R

A

S

L

L

D

R

D

E

M

M

R

R

L

I

Q

R

G

G

V

V

K

K

T

T

T

N

A

I

A

P

Y

F

Y

L

Q

I

E

N

I

V

L

M

R

K

N

N

P

K

E

K

F

F

R

T

S

S

G

G

Q

D

F

Y

N

T

T

T

S

K

F

F

V

I

E

E

S

E

H

T

P

P

E

E

L

L

R21 (= R19) mutation to A: Complete loss of catalytic activity.
K119 (= K115) binding ATP
K161 (= K157) binding ATP
H211 (= H207) binding ATP
E278 (= E274) binding ATP
K411 (≠ R400) mutation to A: Complete loss of catalytic activity.

Sites not aligning to the query:

541:545 binding substrate
542 binding Mn(2+)
580 A→T: Complete loss of catalytic activity.
614 R→A: Complete loss of catalytic activity.
621 Y→A: Complete loss of catalytic activity.
712 binding Mn(2+)
741 binding Mn(2+)
743 binding Mn(2+)
838 Q→A: About 2.5-fold loss of catalytic activity.
876 T→A: Complete loss of catalytic activity.
879 S→A: About 2-fold loss of catalytic activity.
880 K→T: Complete loss of catalytic activity.

4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
50% identity, 93% coverage: 1:440/471 of query aligns to 1:438/442 of 4mv4A

query
sites
4mv4A

V

M

I

L

K

E

K

K

I

V

L

V

I

I

A

A

N

N

R

R

G

G

E

E

I

I

A

A

V

L

R

R

I

I

V

L

R

R

A

A

C

C

A

K

E

E

M

L

G

G

I

I

R

K

S

T

V

V

A

A

I

V

Y

H

S

S

D

T

A

A

D

D

R

R

H

D

A

L

L

K

H

H

V

V

K

L

R

L

A

A

D

D

E

E

A

T

H

I

S

C

I

I

G

G

A

P

E

A

P

P

L

S

A

A

-

K

G

S

Y

Y

L

L

N

N

P

I

R

P

K

A

L

I

V

I

N

A

L

A

A

A

V

E

E

V

T

T

G

G

C

A

D

D

A

A

L

I

H

H

P

P

G

G

Y

Y

G

G

F

F

L

L

S

S

E

E

N

N

A

A

E

D

L

F

A

A

D

E

I

Q

C

V

A

E

E

R

R

S

G

G

I

F

K

T

F

F

I

I

G

G

P

P

S

T

A

A

E

D

V

V

I

I

R

R

R

L

M

M

G

G

D

D

K
|
K

T

V

E

S

A

A

R

I

R

K

S

A

M

M

I

K

K

K

A

A

G

G

V

V

P

P

V

C

T

V

P

P

G

G

T

S

E

D

G

G

N

P

V

V

S

S

G

N

-

D

I

I

E

A

E

K

A

N

L

K

T

E

E

I

G

A

D

K

R

R

I

I

G

G

Y

Y

P

P

V

I

M

I

L

I

K
|
K

A

A

T

S

S

G

G

G

G
|
G

G

G

G
x
M

R

R

G

V

I

V

R

R

R

-

C

-

N

-

S

S

R

E

E

D

E

A

L

L

E

E

Q

E

A

S

F

I

P

A

R

M

V

T

I

K

S

A

E

E

A

A

T

K

K

A

A

A

F

F

G

N

S

N

A
x
D

E

M

V

V

F

Y

L

M

E
|
E

K

K

C
x
Y

I
x
L

V

E

N

N

P

P

K

R

H
|
H

I

V

E

E

A

I

Q

Q

I

V

L

L

G

A

D

D

S

T

F

H

G

G

N

N

V

A

V

V

H

Y

L

L

F

A

E

E

R

R

D

D

C

C

S

S

I

M

Q

Q

R

R

R
|
R

N
x
H

Q

Q

K

K

L

V

I

V

E

E

I

E

A

A

P

P

S

A

P

P

Q

G

L

I

T

T

P

E

E

E

Q

V

R

R

A

R

Y

D

I

I

G

G

D

S

L

R

S

C

V

A

R

N

A

A

A

C

K

V

A

E

V

I

G

G

Y

Y

E

R

N

G

A

A

G

G

T
|
T

V

F

E
|
E

F

F

L
|
L

L

Y

A

E

E

N

G

G

E

E

V

F

Y

Y

F

F

M

I

E
|
E

M

M

N
|
N

T

T

R
|
R

V

I

Q

Q

V

V

E
|
E

H

H

T

P

I

V

T

T

E

E

E

M

I

I

T

T

G

G

I

V

D

D

I

L

V

V

R

K

E

E

Q

Q

I

L

R

R

I

I

A

A

S

A

G

G

L

L

P

P

L

I

S

S

V

F

K

K

Q

Q

E

E

D

D

I

I

Q

K

H

V

R

K

G

G

F

H

A

A

L

M

Q

E

F

C

R
|
R

I

I

N

N

A

A

E

E

D

D

P

P

K

K

N

-

N

T

F

F

L

L

P

P

S

S

F

P

G

G

K

K

I

V

T

N

R

H

Y

L

Y

H

A

S

P

P

G

G

P

L

G

G

V

V

R

R

T

W

D

D

T

S

A

H

I

V

Y

Y

T

G

G

G

Y

Y

T

T

I

V

P

P

F

H

Y

Y

D

D

S

S

M

M

C

I

L

A

K

K

L

L

V

I

V

T

W

Y

A

G

L

D

T

T

W

R

E

E

E

V

A

A

M

I

D

R

R

R

G

M

L

Q

R

N

A

A

L

L

D

S

D

E

M

T

R

I

L

I

Q

D

G

G

V

I

K

K

T

T

T

N

A

I

A

P

Y

L

Y

H

Q

E

E

L

I

I

L

L

R

E

N

D

P

E

E

N

F

F

R

Q

S

K

G

G

Q

G

F

T

N

N

T

I

S

H

F

Y

V

L

E

E

active site: K116 (= K115), K159 (= K157), D193 (≠ A194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E286), N287 (= N288), R289 (= R290), E293 (= E294), R335 (= R336)
binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (≠ G164), E198 (= E199), Y200 (≠ C201), L201 (≠ I202), H233 (≠ N234), L275 (= L276), E285 (= E286)
binding magnesium ion: E273 (= E274), E285 (= E286)

3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
48% identity, 94% coverage: 2:445/471 of query aligns to 2:447/1137 of 3bg5A

query
sites
3bg5A

I

I

K

K

I

L

L

L

I

V

A

A

N

N

R

R

G

G

E

E

I

I

A

A

V

I

R

R

I

I

V

F

R

R

A

A

C

A

A

A

E

E

M

L

G

D

I

I

R

S

S

T

V

V

A

A

I

I

Y

Y

S

S

D

N

A

E

D

D

R

K

H

S

A

S

L

L

H

H

V

R

K

Y

R

K

A

A

D

D

E

E

A

S

H

Y

S

L

I

V

G

G

A

S

E

D

-

L

-

G

P

P

L

A

A

E

G

S

Y

Y

L

L

N

N

P

I

R

E

K

R

L

I

V

I

N

D

L

V

A

A

V

K

E

Q

T

A

G

N

C

V

D

D

A

A

L

I

H

H

P

P

G

G

Y

Y

G

G

F

F

L

L

S

S

E

E

N

N

A

E

E

Q

L

F

A

A

D

R

I

R

C

C

A

A

E

E

R

E

G

G

I

I

K

K

F

F

I

I

G

G

P

P

S

H

A

L

E

E

V

H

I

L

R

D

R

M

M

F

G

G

D

D

K
|
K

T

V

E

K

A

A

R

R

R

T

S

T

M

A

I

I

K

K

A

A

G

D

V

L

P

P

V

V

T

I

P

P

G

G

T

T

E

D

G

G

N

P

V

I

S

K

G

S

I

Y

E

E

E

L

A

A

L

K

T

E

E

F

G

A

D

E

R

E

I

A

G

G

Y

F

P

P

V

L

M
|
M

L

I

K
|
K

A

A

T

T

S

S

G

-

R

-

G

-

I

-

R

R

R

I

C

V

N

R

S

E

R

E

E

S

E

E

L

L

E

E

Q

D

A

A

F

F

P

H

R

R

V

A

I

K

S

S

E

E

A

A

T

E

K

K

A

S

F

F

G

G

S

N

A
x
S

E

E

V

V

F

Y

L

I

E

E

K

R

C
x
Y

I
|
I

V

D

N

N

P

P

K

K

H
|
H

I

I

E

E

A

V

Q

Q

I

V

L

I

G

G

D

D

S

E

F

H

G

G

N

N

V

I

V

V

H

H

L

L

F

F

E

E

R

R

D

D

C

C

S

S

I

V

Q
|
Q

R

R

R
|
R

N
x
H

Q

Q

K

K

L

V

I

V

E

E

I

V

A

A

P

P

S

S

P

V

Q

G

L

L

T

S

P

P

E

T

Q

L

R

R

A

Q

Y

R

I

I

G

C

D

D

L

A

S

A

V

I

R

Q

A

L

A

M

K

E

A

N

V

I

G

K

Y

Y

E

V

N

N

A

A

G

G

T
|
T

V

V

E
|
E

F

F

L
|
L

L

V

A

S

E

G

G

D

E

E

V

F

Y

F

F

F

M

I

E
|
E

M

V

N
|
N

T

P

R
|
R

V

V

Q

Q

V

V

E
|
E

H

H

T

T

I

I

T

T

E

E

E

M

I

V

T

T

G

G

I

I

D

D

I

I

V

V

R

K

E

T

Q

Q

I

I

R

L

I

V

A

A

S

A

G

G

L

A

P

D

L

L

-

F

-

G

-

E

-

I

-

N

S

M

V

P

K

Q

Q

Q

E

K

D

D

I

I

Q

T

H

T

R

L

G

G

F

Y

A

A

L

I

Q

Q

F

C

R
|
R

I

I

N

T

A

T

E

E

D

D

P

P

K

L

N

N

N

D

F

F

L

M

P

P

S

D

F

T

G

G

K

T

I

I

T

I

R

A

Y

Y

Y

R

A

S

P

S

G

G

P

F

G

G

V

V

R

R

T

L

D

D

T

A

A

G

I

D

-

G

Y

F

T

Q

G

G

Y

A

T

E

I

I

P

S

P

P

F

Y

Y

Y

D

D

S

S

M

L

C

L

L

V

K

K

L

L

V

S

V

T

W

H

A

A

L

I

T

S

W

F

E

K

E

Q

A

A

M

E

D

E

R

K

G

M

L

V

R

R

A

S

L

L

D

R

D

E

M

M

R

R

L

I

Q

R

G

G

V

V

K

K

T

T

T

N

A

I

A

P

Y

F

Y

L

Q

I

E

N

I

V

L

M

R

K

N

N

P

K

E

K

F

F

R

T

S

S

G

G

Q

D

F

Y

N

T

T

T

S

K

F

F

V

I

E

E

S

E

H

T

P

P

E

E

L

L

active site: K117 (= K115), K159 (= K157), S189 (≠ A194), H202 (= H207), R228 (= R233), T267 (= T272), E269 (= E274), E281 (= E286), N283 (= N288), R285 (= R290), E289 (= E294), R337 (= R336)
binding adenosine-5'-triphosphate: K117 (= K115), M157 (= M155), K159 (= K157), Y196 (≠ C201), I197 (= I202), H202 (= H207), Q226 (= Q231), H229 (≠ N234), E269 (= E274), L271 (= L276), E281 (= E286), N283 (= N288)

Sites not aligning to the query:

active site: 533, 639, 703, 732, 734, 755, 761, 762, 801, 867, 869, 881, 883, 888
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 463, 471, 472, 473, 579
binding manganese (ii) ion: 533, 732, 734
binding pyruvic acid: 603, 703

2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 93% coverage: 1:440/471 of query aligns to 1:439/444 of 2vr1A

query
sites
2vr1A

V

M

I

L

K

D

K

K

I

I

L

V

I

I

A

A

N

N

R

R

G

G

E

E

I

I

A

A

V

L

R

R

I

I

V

L

R

R

A

A

C

C

A

K

E

E

M

L

G

G

I

I

R

K

S

T

V

V

A

A

I

V

Y

H

S

S

D

S

A

A

D

D

R

R

H

D

A

L

L

K

H

H

V

V

K

L

R

L

A

A

D

D

E

E

A

T

H

V

S

C

I

I

G

G

A

P

E

A

P

P

-

S

L

V

A

K

G

S

Y

Y

L

L

N

N

P

I

R

P

K

A

L

I

V

I

N

S

L

A

A

A

V

E

E

I

T

T

G

G

C

A

D

V

A

A

L

I

H

H

P

P

G

G

Y

Y

G

G

F

F

L

L

S

S

E

E

N

N

A

A

E

N

L

F

A

A

D

E

I

Q

C

V

A

E

E

R

R

S

G

G

I

F

K

I

F

F

I

I

G

G

P

P

S

K

A

A

E

E

V

T

I

I

R

R

R

L

M

M

G

G

D

D

K
|
K

T

V

E

S

A

A

R

I

R

A

S

A

M

M

I

K

K

K

A

A

G

G

V

V

P

P

V

C

T

V

P

P

G

G

T

S

E

D

G

G

N

P

V

L

-

G

S

D

G

D

I

M

E

D

E

K

A

N

L

R

T

A

E

I

G

A

D

K

R

R

I

I

G

G

Y

Y

P

P

V

V

M

I

L

I

K
|
K

A

A

T

S

S

-

G

-

G

G

R
|
R

G

G

I
x
M

R

R

R

V

C

V

N

R

S

G

R

D

E

A

E

E

L

L

E

A

Q

Q

A

S

F

I

P

S

R

M

V

T

I

R

S

A

E

E

A

A

T

K

K

A

A

A

F

F

G

S

S

N

A
x
D

E

M

V

V

F

Y

L

M

E

E

K

K

C
x
Y

I
x
L

V

E

N

N

P

P

K

R

H
|
H

I

V

E

E

A

I

Q

Q

I

V

L

L

G

A

D

D

S

G

F

Q

G

G

N

N

V

A

V

I

H

Y

L

L

F

A

E

E

R

R

D

D

C

C

S

S

I

M

Q

Q

R

R

R
|
R

N

H

Q

Q

K

K

L

V

I

V

E

E

I

E

A

A

P

P

S

A

P

P

Q

G

L

I

T

T

P

P

E

E

Q

L

R

R

A

R

Y

Y

I

I

G

G

D

E

L

R

S

C

V

A

R

K

A

A

A

C

K

V

A

D

V

I

G

G

Y

Y

E

R

N

G

A

A

G

G

T
|
T

V

F

E
|
E

F

F

L
|
L

L

F

A

E

E

N

G

G

E

E

V

F

Y

Y

F

F

M

I

E
|
E

M

M

N
|
N

T

T

R
|
R

V

I

Q

Q

V

V

E
|
E

H

H

T

P

I

V

T

T

E

E

E

M

I

I

T

T

G

G

I

V

D

D

I

L

V

I

R

K

E

E

Q

Q

I

L

R

R

I

I

A

A

S

A

G

G

L

Q

P

P

L

L

S

S

V

I

K

K

Q

Q

E

E

D

E

I

V

Q

H

H

V

R

R

G

G

F

H

A

A

L

V

Q

E

F

C

R
|
R

I

I

N

N

A

A

E

E

D

D

P

P

K

-

N

N

N

T

F

F

L

L

P

P

S

S

F

P

G

G

K

K

I

I

T

T

R

R

Y

F

Y

H

A

A

P

P

G

G

P

F

G

G

V

V

R

R

T

W

D

E

T

S

A

H

I

I

Y

Y

T

A

G

G

Y

Y

T

T

I

V

P

P

F

Y

Y

Y

D

D

S

S

M

M

C

I

L

G

K

K

L

L

V

I

V

C

W

Y

A

G

L

E

T

N

W

R

E

D

E

V

A

A

M

I

D

A

R

R

G

M

L

K

R

N

A

A

L

L

D

Q

D

E

M

L

R

I

L

I

Q

D

G

G

V

I

K

K

T

T

T

N

A

V

A

D

Y

L

Y

Q

Q

I

E

R

I

I

L

M

R

N

N

D

P

E

E

N

F

F

R

Q

S

H

G

G

Q

G

F

T

N

N

T
x
I

S

H

F

Y

V

L

E

E

active site: K116 (= K115), K159 (= K157), D194 (≠ A194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E286), N288 (= N288), R290 (= R290), E294 (= E294), R336 (= R336)
binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (= R165), M167 (≠ I167), Y201 (≠ C201), L202 (≠ I202), E274 (= E274), L276 (= L276), E286 (= E286), N288 (= N288), I435 (≠ T436)

Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
49% identity, 94% coverage: 2:445/471 of query aligns to 37:487/1178 of Q05920

query
sites
Q05920

I

I

K

K

K
|
K

I

V

L

M

I

V

A

A

N

N

R

R

G

G

E

E

I

I

A

A

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I

R

R

I

V

V

F

R

R

A

A

C

C

A

T

E

E

M

L

G

G

I

I

R

R

S

T

V

V

A

A

I

V

Y

Y

S

S

D

E

A

Q

D

D

R

T

H

G

A

Q

L

M

H

H

V

R

K

Q

R
x
K

A

A

D

D

E

E

A

A

H

Y

S

L

I

I

G

G

-

R

-

G

A

L

E

A

P

P

L

V

A

Q

G

A

Y

Y

L

L

N

H

P

I

R

P

K

D

L

I

V

I

N

K

L

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A

A

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E

E

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N

G

G

C

V

D

D

A

A

L

V

H

H

P

P

G

G

Y

Y

G

G

F

F

L

L

S

S

E

E

N

R

A

A

E

D

L

F

A

A

D

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I

A

C

C

A

Q

E

D

R

A

G

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I

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K

R

F

F

I

I

G

G

P

P

S

S

A

P

E

E

V

V

I

V

R

R

R
x
K

M

M

G

G

D

D

K
|
K

T

V

E

E

A

A

R

R

R

A

S

I

M

A

I

I

K

A

A

A

G

G

V

V

P

P

V

V

T

V

P

P

G

G

T

T

E

D

G

S

N

P

V

I

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S

G

S

I

L

E

H

E

E

A

A

L

H

T

E

E

F

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D

N

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I

F

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F

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I

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A

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Y

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R

G

G

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M

R

R

R

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N

H

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R

Y

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E

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L

E

E

Q

E

A

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F

Y

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A

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S

E

E

A

A

T

L

K

A

A

A

F

F

G

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N

A

G

E

A

V

L

F

F

L

V

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E

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K

C

F

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x
K

P

P

K

R

H

H

I

I

E

E

A

V

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Q

I

I

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L

G

G

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N

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F

Y

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N

H

Q

Q

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D

P

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D

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K

A

L

A

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Q

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G

G

Y

Y

E

E

N

N

A

A

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E

F

F

L

L

L

V

-

D

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A

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E

G

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-

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-

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A

L

I

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Q

F

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-

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A

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F

T

Q

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G

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A

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Y

D

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A

W

H

A

G

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x
K

T

D

W

H

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P

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A

A

M

A

D

T

R

K

G

M

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S

R

R

A

A

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A

D

E

M

F

R

R

L

V

Q

R

G

G

V

V

K

K

T

T

T

N

A

I

A

P

Y

F

Y

L

Q

Q

E

N

I

V

L

L

R

N

N

N

P

Q

E

Q

F

F

R

L

S

A

G

G

Q

T

F

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N

D

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S

Q

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E

D

S

E

H

N

P

P

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E

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L

K39 (= K4) modified: N6-acetyllysine
K79 (≠ R44) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
K148 (≠ R111) modified: N6-acetyllysine
K152 (= K115) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
K241 (≠ N204) modified: N6-acetyllysine
K434 (≠ L392) modified: N6-acetyllysine

Sites not aligning to the query:

35 modified: N6-acetyllysine
589 modified: N6-acetyllysine
717 modified: N6-acetyllysine
748 modified: N6-acetyllysine; K→Q: Reduced pyruvate carboxylase activity.
892 modified: N6-acetyllysine
969 modified: N6-acetyllysine

P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
49% identity, 94% coverage: 2:445/471 of query aligns to 37:487/1178 of P11498

query
sites
P11498

I

I

K

K

I

V

L

M

I

V

A

A

N

N

R

R

G

G

E

E

I

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A

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A

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K

Q

R

K

A

A

D

D

E

E

A

A

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I

G

G

-

R

-

G

A

L

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A

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P

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G

A

Y

Y

L

L

N

H

P

I

R

P

K

D

L

I

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I

N

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L

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A

A

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E

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N

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A

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H

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P

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G

Y

Y

G

G

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F

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L

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E

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A

A

E

D

L

F

A

A

D

Q

I

A

C

C

A

Q

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A

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G

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K

R

F

F

I

I

G

G

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P

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S

A

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E

V
|
V

I

V

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R

R

K

M

M

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G

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D

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K

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V

E

E

A

A

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|
R

R

A

S

I

M

A

I

I

K

A

A

A

G

G

V

V

P

P

V

V

T

V

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P

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G

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I

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E

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E

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A

A

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N

R

T

I

Y

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A

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E

A

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A

A

A

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F

G

G

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N

A

G

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A

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A

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Q

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G

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N

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L

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R
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R

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A

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A

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Y
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Y

E

E

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N

A

A

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G

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T

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E

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-

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-

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A

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A

A

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R

L

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R

G

G

V

V

K

K

T

T

T

N

A

I

A

A

Y

F

Y

L

Q

Q

E

N

I

V

L

L

R

N

N

N

P

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E

Q

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F

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A

G

G

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F

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N

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P

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L

L

V145 (= V108) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
R156 (= R119) to Q: in PC deficiency; dbSNP:rs119103241
R270 (= R233) to W: in PC deficiency; dbSNP:rs1258494752
Y304 (= Y267) to C: in PC deficiency
R451 (= R409) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143

Sites not aligning to the query:

572 binding Mn(2+)
583 R → L: in PC deficiency; dbSNP:rs119103242
610 A → T: in PC deficiency; mild; dbSNP:rs28940589
631 R → Q: in PC deficiency; dbSNP:rs113994145
741 binding via carbamate group; modified: N6-carboxylysine
743 M → I: in PC deficiency; mild; dbSNP:rs28940590
771 binding Mn(2+)
773 binding Mn(2+)
1077 mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
1131:1133 natural variant: Missing (in PC deficiency)
1144 modified: N6-biotinyllysine

7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
49% identity, 94% coverage: 2:445/471 of query aligns to 5:455/1146 of 7wtdC

query
sites
7wtdC

I

I

K

K

I

V

L

M

I

V

A

A

N

N

R

R

G

G

E

E

I

I

A

A

V

I

R

R

I

V

V
x
F

R
|
R

A

A

C

C

A
x
T

E

E

M

L

G

G

I

I

R

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V

V

A

A

I

I

Y

Y

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A

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D

D

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A

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H

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x
R

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x
Q

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x
K

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A

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D

E
|
E

A

A

H

Y

S

L

I

I

G

G

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R

-

G

A

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L

binding adenosine-5'-triphosphate: K162 (= K157), G167 (= G162), G168 (= G163), F206 (≠ C201), Q236 (= Q231), H239 (≠ N234), E292 (= E286)
binding coenzyme a: F21 (≠ V18), R22 (= R19), T25 (≠ A22), R45 (≠ V42), Q46 (≠ K43), K47 (≠ R44), A48 (= A45), D49 (= D46), E50 (= E47), R366 (≠ Y357), R413 (= R403), A416 (≠ D406), R419 (= R409)

Sites not aligning to the query:

binding coenzyme a: 462, 464, 465, 466, 1024, 1053

7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
49% identity, 94% coverage: 2:445/471 of query aligns to 6:456/1147 of 7wtbB

query
sites
7wtbB

I

I

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