SitesBLAST

W12 (= W12) mutation to M: No changes in biotinylation in E.coli.
K35 (= K35) modified: N6-biotinyllysine; alternate; modified: N6-lipoyllysine; alternate

2b8gA Solution structure of bacillus subtilis blap biotinylated-form (energy minimized mean structure)
100% identity, 99% coverage: 2:73/73 of query aligns to 1:72/72 of 2b8gA

query
sites
2b8gA

T

T

V

V

S

S

I

I

Q

Q

M

M

A

A

G

G

N

N

L

L

W
|
W

K

K

V

V

H

H

V

V

K

K

A

A

G

G

D

D

Q

Q

I

I

E

E

K

K

G

G

Q

Q

E

E

V

V

A

A

I

I

L

L

E

E

S

S

M

M

K
|
K

M

M

E

E

I

I

P

P

I

I

V

V

A

A

D

D

R

R

S

S

G

G

I

I

V

V

K

K

E

E

V

V

K

K

E

E

G

G

D

D

F

F

V

V

N

N

E

E

G

G

D

D

V

V

L

L

E

E

L

L

S

S

N

N

S

S

T

T

Q

Q

binding biotin: W11 (= W12), K34 (= K35)

1z6hA Solution structure of bacillus subtilis blap biotinylated-form (see paper)
100% identity, 99% coverage: 2:73/73 of query aligns to 1:72/72 of 1z6hA

query
sites
1z6hA

T

T

V

V

S

S

I

I

Q

Q

M

M

A

A

G

G

N

N

L

L

W
|
W

K

K

V

V

H

H

V

V

K

K

A

A

G

G

D

D

Q

Q

I

I

E

E

K

K

G

G

Q

Q

E

E

V

V

A

A

I

I

L

L

E

E

S

S

M

M

K
|
K

M

M

E

E

I

I

P

P

I

I

V

V

A

A

D

D

R

R

S

S

G

G

I

I

V

V

K

K

E

E

V

V

K

K

E

E

G

G

D

D

F

F

V

V

N

N

E

E

G

G

D

D

V

V

L

L

E

E

L

L

S

S

N

N

S

S

T

T

Q

Q

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: W11 (= W12), K34 (= K35)

P05165 Propionyl-CoA carboxylase alpha chain, mitochondrial; PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.3 from Homo sapiens (Human) (see 6 papers)
45% identity, 85% coverage: 7:68/73 of query aligns to 666:727/728 of P05165

query
sites
P05165

M

M

A

P

G
|
G

N

V

L

V

W

V

K

A

V

V

H

S

V

V

K

K

A

P

G

G

D

D

Q

A

I

V

E

A

K

E

G

G

Q

Q

E

E

V

I

A

C

I

V

L

I

E

E

S

A

M

M

K
|
K

M

M

E

Q

I

N

P

S

I

M

V

T

A

A

D

G

R

K

S

T

G

G

I

T

V

V

K

K

E

S

V

V

K

H

K
x
C

K

Q

E

A

G

G

D

D

F

T

V

V

N

G

E

E

G

G

D

D

V

L

L

L

L

V

E

E

L

L

G668 (= G9) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
K694 (= K35) modified: N6-biotinyllysine; by HLCS
C712 (≠ K53) natural variant: Missing (in PA-1; loss of biotinylation)

Sites not aligning to the query:

1:52 modified: transit peptide, Mitochondrion
75 A → P: in PA-1; dbSNP:rs794727479
77 R → W: in PA-1; loss of function; dbSNP:rs141371306
138 A → T: in PA-1; loss of function; dbSNP:rs202247814
164 I → T: in PA-1; loss of function; dbSNP:rs202247815
197 G → E: in PA-1
229 M → K: in PA-1; dbSNP:rs375628794
297 Q → R: in PA-1; dbSNP:rs2063109875
368 D → G: in PA-1
373 M → K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
379 G → V: in PA-1; dbSNP:rs794727087
398 C → R: in PA-1
399 R → Q: in PA-1; dbSNP:rs1301904623
423 P → L: in PA-1; dbSNP:rs1443858896
532 natural variant: Missing (in PA-1)
551 V → F: in dbSNP:rs61749895
559 W → L: in PA-1; dbSNP:rs118169528
631 G → R: in PA-1; loss of function; dbSNP:rs796052018

8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
45% identity, 85% coverage: 7:68/73 of query aligns to 606:667/668 of 8xl5A

query
sites
8xl5A

M

M

A

P

G

G

N

V

L

V

W

V

K

A

V

V

H

S

V

V

K

K

A

P

G

G

D

D

Q

A

I

V

E

A

K

E

G

G

Q

Q

E

E

V

I

A

C

I

V

L

I

E

E

S

A

M
|
M

K
|
K

M

M

E

Q

I

N

P

S

I

M

V

T

A

A

D

G

R

K

S

T

G

G

I

T

V

V

K

K

E

S

V

V

K

H

K

C

K

Q

E

A

G

G

D

D

F

T

V

V

N

G

E

E

G

G

D

D

V

L

L

L

L

V

E

E

L

L

binding biotin: M633 (= M34), K634 (= K35)

7ybuA Human propionyl-coenzyme a carboxylase (see paper)
45% identity, 85% coverage: 7:68/73 of query aligns to 608:669/670 of 7ybuA

query
sites
7ybuA

M

M

A

P

G

G

N

V

L

V

W

V

K

A

V

V

H

S

V

V

K

K

A

P

G

G

D

D

Q

A

I

V

E

A

K

E

G

G

Q

Q

E

E

V

I

A

C

I

V

L

I

E

E

S

A

M
|
M

K
|
K

M

M

E

Q

I

N

P

S

I

M

V

T

A

A

D

G

R

K

S

T

G

G

I

T

V

V

K

K

E

S

V

V

K

H

K

C

K

Q

E

A

G

G

D

D

F

T

V

V

N

G

E

E

G

G

D

D

V

L

L

L

L

V

E

E

L

L

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M635 (= M34), K636 (= K35)

2ejfC Crystal structure of the biotin protein ligase (mutations r48a and k111a) and biotin carboxyl carrier protein complex from pyrococcus horikoshii ot3 (see paper)
43% identity, 93% coverage: 2:69/73 of query aligns to 2:69/69 of 2ejfC

query
sites
2ejfC

T

V

V

V

S

S

I

A

Q

P

M

M

A

P

G

G

N

K

L

V

W

L

K

R

V

V

H

L

V

V

K

R

A

V

G

G

D

D

Q

R

I

V

E

R

K

V

G

G

Q

Q

E

G

V

L

A

L

I

V

L

L

E

E

S

A

M
|
M

K
|
K

M

M

E

E

I

N

P

E

I

I

V

P

A

S

D

P

R

R

S

D

G

G

I

V

V

V

K

K

E

R

V

I

K

L

K

V

K

K

E

E

G

G

D

E

F

A

V

V

N

D

E

T

G

G

D

Q

V

P

L

L

L

I

E

E

L

L

S

G

binding biotin: M34 (= M34), K35 (= K35)

5ks8F Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
39% identity, 90% coverage: 3:68/73 of query aligns to 415:480/482 of 5ks8F

query
sites
5ks8F

V

V

S

T

I

T

Q

A

M

M

A

P

G

G

N

T

L

I

W

V

K

D

V

V

H

K

V

V

K

N

A

V

G

G

D

D

Q

K

I

V

E

S

K

A

G

G

Q

D

E

A

V

V

A

L

I

V

L

I

E

E

S

A

M

M

K

K

M

M

E

E

I

N

P

E

I

I

V

Q

A

A

D

S

R

K

S

S

G

G

I

V

V

V

K

V

E

A

V

I

K

N

K

V

K

K

E

K

G

G

D

D

F

S

V

V

N

T

E

P

G

D

D

E

V

A

L

L

E

E

L

I

Sites not aligning to the query:

active site: 11, 115, 172, 201, 203
binding manganese (ii) ion: 11, 172, 174, 201, 203

5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
39% identity, 90% coverage: 3:68/73 of query aligns to 513:578/580 of 5ks8D

query
sites
5ks8D

V

V

S

T

I

T

Q

A

M

M

A

P

G

G

N

T

L

I

W

V

K

D

V

V

H

K

V

V

K

N

A

V

G

G

D

D

Q

K

I

V

E

S

K

A

G

G

Q

D

E

A

V

V

A

L

I

V

L

I

E

E

S

A

M

M

K

K

M

M

E

E

I

N

P

E

I

I

V

Q

A

A

D

S

R

K

S

S

G

G

I

V

V

V

K

V

E

A

V

I

K

N

K

V

K

K

E

K

G

G

D

D

F

S

V

V

N

T

E

P

G

D

D

E

V

A

L

L

E

E

L

I

Sites not aligning to the query:

active site: 12, 116, 173, 202, 204
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 51, 56, 299, 337, 340, 341
binding manganese (ii) ion: 12, 173, 202, 204
binding pyruvic acid: 15, 47, 80, 82, 337

A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
36% identity, 96% coverage: 3:72/73 of query aligns to 1080:1149/1150 of A0A0H3JRU9

query
sites
A0A0H3JRU9

V

I

S

G

I

A

Q

Q

M

M

A

P

G

G

N

S

L

V

W

T

K

E

V

V

H

K

V

V

K

S

A

V

G

G

D

E

Q

T

I

V

E

K

K

A

G

N

Q

Q

E

P

V

L

A

L

I

I

L

T

E

E

S

A

M

M

K

K

M

M

E

E

I

T

P

T

I

I

V

Q

A

A

D

P

R

F

S

D

G

G

I

V

V

I

K

K

E

Q

V

V

K

T

K

V

K

N

E

N

G

G

D

D

F

T

V

I

N

A

E

T

G

G

D

D

V

L

L

L

L

I

E

E

L

I

S

E

N

K

S

A

T

T

Sites not aligning to the query:

21 R→A: Complete loss of catalytic activity.
119 binding ATP
161 binding ATP
211 binding ATP
278 binding ATP
411 K→A: Complete loss of catalytic activity.
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.

5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
39% identity, 92% coverage: 2:68/73 of query aligns to 534:600/603 of 5ks8C

query
sites
5ks8C

T

C

V

V

S

T

I

T

Q

A

M

M

A

P

G

G

N

T

L

I

W

V

K

D

V

V

H

K

V

V

K

N

A

V

G

G

D

D

Q

K

I

V

E

S

K

A

G

G

Q

D

E

A

V

V

A

L

I

V

L

I

E

E

S

A

M

M

K

K

M

M

E

E

I

N

P

E

I

I

V

Q

A

A

D

S

R

K

S

S

G

G

I

V

V

V

K

V

E

A

V

I

K

N

K

V

K

K

E

K

G

G

D

D

F

S

V

V

N

T

E

P

G

D

D

E

V

A

L

L

E

E

L

I

Sites not aligning to the query:

active site: 11, 115, 172, 201, 203
binding manganese (ii) ion: 11, 172, 201, 203
binding pyruvic acid: 79, 81, 114, 174

3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
36% identity, 90% coverage: 3:68/73 of query aligns to 1008:1073/1074 of 3bg5B

query
sites
3bg5B

V

I

S

G

I

A

Q

Q

M

M

A

P

G

G

N

S

L

V

W

T

K

E

V

V

H

K

V

V

K

S

A

V

G

G

D

E

Q

T

I

V

E

K

K

A

G

N

Q

Q

E

P

V

L

A

L

I

I

L

T

E

E

S

A

M

M

K

K

M

M

E

E

I

T

P

T

I

I

V

Q

A

A

D

P

R

F

S

D

G

G

I

V

V

I

K

K

E

Q

V

V

K

T

K

V

K

N

E

N

G

G

D

D

F

T

V

I

N

A

E

T

G

G

D

D

V

L

L

L

L

I

E

E

L

I

Sites not aligning to the query:

active site: 117, 139, 165, 204, 206, 218, 220, 222, 226, 274, 470, 576, 640, 669, 671, 692, 698, 699, 738, 804, 806, 818, 820, 825
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 403, 408, 409, 410, 516, 518
binding manganese (ii) ion: 470, 669, 671
binding pyruvic acid: 473, 640, 804

3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
36% identity, 90% coverage: 3:68/73 of query aligns to 1067:1132/1133 of 3hb9A

query
sites
3hb9A

V

I

S

G

I

A

Q

Q

M

M

A

P

G

G

N

S

L

V

W

T

K

E

V

V

H

K

V

V

K

S

A

V

G

G

D

E

Q

T

I

V

E

K

K

A

G

N

Q

Q

E

P

V

L

A

L

I

I

L

T

E

E

S

A

M

M

K

K

M

M

E

E

I

T

P

T

I

I

V

Q

A

A

D

P

R

F

S

D

G

G

I

V

V

I

K

K

E

Q

V

V

K

T

K

V

K

N

E

N

G

G

D

D

F

T

V

I

N

A

E

T

G

G

D

D

V

L

L

L

L

I

E

E

L

I

Sites not aligning to the query:

active site: 117, 159, 198, 224, 263, 265, 277, 279, 281, 285, 333, 529, 635, 699, 728, 730, 751, 757, 758, 797, 863, 865, 877, 879, 884
binding adenosine-5'-diphosphate: 117, 157, 192, 193, 198, 222, 225, 267, 276, 277
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 459, 462, 467, 468, 575, 577
binding manganese (ii) ion: 529, 728, 730

4hnvB Crystal structure of r54e mutant of s. Aureus pyruvate carboxylase (see paper)
36% identity, 90% coverage: 3:68/73 of query aligns to 967:1032/1033 of 4hnvB

query
sites
4hnvB

V

I

S

G

I

A

Q

Q

M

M

A

P

G

G

N

S

L

V

W

T

K

E

V

V

H

K

V

V

K

S

A

V

G

G

D

E

Q

T

I

V

E

K

K

A

G

N

Q

Q

E

P

V

L

A

L

I

I

L

T

E

E

S

A

M

M

K

K

M

M

E

E

I

T

P

T

I

I

V

Q

A

A

D

P

R

F

S

D

G

G

I

V

V

I

K

K

E

Q

V

V

K

T

K

V

K

N

E

N

G

G

D

D

F

T

V

I

N

A

E

T

G

G

D

D

V

L

L

L

L

I

E

E

L

I

Sites not aligning to the query:

active site: 117, 139, 165, 204, 206, 218, 220, 222, 226, 274, 429, 535, 599, 628, 630, 651, 657, 658, 697, 763, 765, 777, 779, 784
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 362, 368, 369, 475, 477
binding manganese (ii) ion: 429, 599, 628, 630

3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
36% identity, 90% coverage: 3:68/73 of query aligns to 1071:1136/1137 of 3bg5A

query
sites
3bg5A

V

I

S

G

I

A

Q

Q

M

M

A

P

G

G

N

S

L

V

W

T

K

E

V

V

H

K

V

V

K

S

A

V

G

G

D

E

Q

T

I

V

E

K

K

A

G

N

Q

Q

E

P

V

L

A

L

I

I

L

T

E

E

S

A

M

M

K

K

M

M

E

E

I

T

P

T

I

I

V

Q

A

A

D

P

R

F

S

D

G

G

I

V

V

I

K

K

E

Q

V

V

K

T

K

V

K

N

E

N

G

G

D

D

F

T

V

I

N

A

E

T

G

G

D

D

V

L

L

L

L

I

E

E

L

I

Sites not aligning to the query:

active site: 117, 159, 189, 202, 228, 267, 269, 281, 283, 285, 289, 337, 533, 639, 703, 732, 734, 755, 761, 762, 801, 867, 869, 881, 883, 888
binding adenosine-5'-triphosphate: 117, 157, 159, 196, 197, 202, 226, 229, 269, 271, 281, 283
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

4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
39% identity, 92% coverage: 3:69/73 of query aligns to 1014:1080/1081 of 4qshC

query
sites
4qshC

V

V

S

G

I

A

Q

T

M

M

A

T

G

G

N

S

L

V

W

I

K

Q

V

V

H

V

V

V

K

K

A

K

G

G

D

D

Q

S

I

V

E

K

K

K

G

G

Q

D

E

P

V

L

A

L

I

I

L

T

E

E

S

A

M

M

K

K

M

M

E

E

I

T

P

T

I

I

V

Q

A

A

D

P

R

F

S

D

G

G

I

E

V

V

K

S

E

S

V

I

K

Y

K

V

K

S

E

D

G

G

D

D

F

T

V

I

N

E

E

S

G

G

D

D

V

L

L

L

L

I

E

E

L

V

S

N

Sites not aligning to the query:

P11154 Pyruvate carboxylase 1; Pyruvic carboxylase 1; PCB 1; EC 6.4.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
40% identity, 96% coverage: 1:70/73 of query aligns to 1101:1170/1178 of P11154

query
sites
P11154

M

L

T

H

V

I

S

G

I

A

Q

P

M

M

A

A

G

G

N

V

L

I

W

V

K

E

V

V

H

K

V

V

K

H

A

K

G

G

D

S

Q

L

I

I

E

K

K

K

G

G

Q

Q

E

P

V

V

A

A

I

V

L

L

E

S

S

A

M

M

K
|
K

M

M

E

E

I

M

P

I

I

I

V

S

A

S

D

P

R

S

S

D

G

G

I

Q

V

V

K

K

E

E

V

V

K

F

K

V

K

S

E

D

G

G

D

E

F

N

V

V

N

D

E

S

G

S

D

D

V

L

L

L

L

V

E

L

L

L

S

E

N

D

K1135 (= K35) modified: N6-biotinyllysine

3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
38% identity, 82% coverage: 6:65/73 of query aligns to 1067:1126/1130 of 3va7A

query
sites
3va7A

Q

E

M

Y

A

T

G

G

N

R

L

F

W

W

K

K

V

P

H

V

V

A

K

A

A

V

G

G

D

D

Q

H

I

V

E

E

K

A

G

G

Q

D

E

G

V

V

A

I

I

I

L

I

E

E

S

A

M

M

K
|
K

M

T

E

E

I

M

P

V

I

V

V

G

A

A

D

T

R

K

S

S

G

G

I

K

V

V

K

Y

E

K

V

I

K

L

K

H

K

K

E

N

G

G

D

D

F

M

V

V

N

E

E

A

G

G

D

D

V

L

L

V

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: K1096 (= K35)

Sites not aligning to the query:

active site: 138, 205, 219, 221, 226, 227, 269, 550, 648, 730, 760, 762, 895
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 633, 641, 653, 656, 658, 943, 944
binding urea: 893, 937, 944, 945, 946

8k2vA 3-methylcrotonyl-coa carboxylase in mccd state with acetyl coa (see paper)
39% identity, 85% coverage: 7:68/73 of query aligns to 150:211/214 of 8k2vA

query
sites
8k2vA

M

M

A

T

G

G

N

T

L

I

W

E

K

K

V

V

H

F

V

V

K

K

A

A

G

G

D

D

Q

K

I

V

E

K

K

A

G

G

Q

D

E

S

V

L

A

M

I

V

L

M

E

I

S

A

M
|
M

K
|
K

M

M

E

E

I

H

P

T

I

I

V

K

A

S

D

P

R

K

S

D

G

G

I

T

V

V

K

K

E

K

V

V

K

F

K

Y

K

R

E

E

G

G

D

A

F

Q

V

A

N

N

E

R

G

H

D

T

V

P

L

L

L

V

E

E

L

F

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M177 (= M34), K178 (= K35)

P02904 Methylmalonyl-CoA carboxyltransferase 1.3S subunit; Biotin carboxyl carrier protein of transcarboxylase; Transcarboxylase, 1.3S subunit; EC 2.1.3.1 from Propionibacterium freudenreichii subsp. shermanii (see 2 papers)
41% identity, 90% coverage: 3:68/73 of query aligns to 57:122/123 of P02904

query
sites
P02904

V

I

S

P

I

A

Q

P

M

L

A

A

G

G

N

T

L

V

W

S

K

K

V

I

H

L

V

V

K

K

A

E

G

G

D

D

Q

T

I

V

E

K

K

A

G

G

Q

Q

E

T

V

V

A

L

I

V

L

L

E

E

S
x
A

M
|
M

K
|
K

M
|
M

E

E

I

T

P

E

I

I

V

N

A

A

D

P

R

T

S

D

G

G

I

K

V

V

K

E

E

K

V

V

K

L

K

V

K

K

E

E

G

R

D

D

F

A

V

V

N

Q

E

G

G

G

D

Q

V

G

L

L

L

I

E

K

L

I

A87 (≠ S33) mutation to M: Reduces activity 10-fold; when associated with L-88.
M88 (= M34) mutation M->A,C,T,L: Reduces activity at least 10-fold.
K89 (= K35) modified: N6-biotinyllysine
M90 (= M36) mutation to L: No effect.

Query Sequence

>73 a.a. (MTVSIQMAGN...)
MTVSIQMAGNLWKVHVKAGDQIEKGQEVAILESMKMEIPIVADRSGIVKEVKKKEGDFVN
EGDVLLELSNSTQ

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