SitesBLAST

2ejfC Crystal structure of the biotin protein ligase (mutations r48a and k111a) and biotin carboxyl carrier protein complex from pyrococcus horikoshii ot3 (see paper)
53% identity, 40% coverage: 99:164/164 of query aligns to 3:68/69 of 2ejfC

query
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2ejfC

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binding biotin: M34 (= M130), K35 (= K131)

4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
35% identity, 62% coverage: 62:163/164 of query aligns to 982:1078/1081 of 4qshC

query
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4qshC

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Sites not aligning to the query:

Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
42% identity, 40% coverage: 99:163/164 of query aligns to 1112:1176/1178 of Q05920

query
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Q05920

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Sites not aligning to the query:

35 modified: N6-acetyllysine
39 modified: N6-acetyllysine
79 modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
148 modified: N6-acetyllysine
152 modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
241 modified: N6-acetyllysine
434 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

3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
42% identity, 41% coverage: 97:163/164 of query aligns to 1069:1135/1137 of 3bg5A

query
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3bg5A

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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

A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
42% identity, 41% coverage: 97:163/164 of query aligns to 1078:1144/1150 of A0A0H3JRU9

query
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Sites not aligning to the query:

21 R→A: Complete loss of catalytic activity.
119 binding
161 binding
211 binding
278 binding
411 K→A: Complete loss of catalytic activity.
541:545 binding
542 binding
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
741 binding
743 binding
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.

4hnvB Crystal structure of r54e mutant of s. Aureus pyruvate carboxylase (see paper)
42% identity, 41% coverage: 97:163/164 of query aligns to 965:1031/1033 of 4hnvB

query
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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

3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
42% identity, 41% coverage: 97:163/164 of query aligns to 1065:1131/1133 of 3hb9A

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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

3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
42% identity, 41% coverage: 97:163/164 of query aligns to 1006:1072/1074 of 3bg5B

query
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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

7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
35% identity, 65% coverage: 57:163/164 of query aligns to 1031:1136/1138 of 7zz3A

query
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7zz3A

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binding acetyl coenzyme *a: R1045 (≠ A71)
binding biotin: K1104 (= K131)

Sites not aligning to the query:

binding acetyl coenzyme *a: 22, 43, 44, 45, 46, 48, 363, 413, 414, 416, 418, 459, 461, 1016, 1017, 1018
binding adenosine-5'-triphosphate: 117, 156, 158, 163, 164, 165, 168, 200, 202, 203, 208, 232, 235, 277, 287, 289, 443
binding bicarbonate ion: 237, 291, 293, 295
binding biotin: 84, 294, 342
binding magnesium ion: 275, 287, 520, 523, 754
binding manganese (ii) ion: 535, 704, 733, 735
binding pyruvic acid: 534, 538, 605, 704, 868

5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
35% identity, 65% coverage: 57:163/164 of query aligns to 1037:1142/1144 of 5vyzA

query
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Sites not aligning to the query:

8hwlA Human pyruvate carboxylase
42% identity, 40% coverage: 99:163/164 of query aligns to 875:939/941 of 8hwlA

query
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binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: K907 (= K131)

Sites not aligning to the query:

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 373, 414, 636, 671

P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
42% identity, 40% coverage: 99:163/164 of query aligns to 1112:1176/1178 of P11498

query
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VAK 1131:1133 (≠ VEK 118:120) natural variant: Missing (in PC deficiency)
K1144 (= K131) modified: N6-biotinyllysine

Sites not aligning to the query:

145 V → A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
156 R → Q: in PC deficiency; dbSNP:rs119103241
270 R → W: in PC deficiency; dbSNP:rs1258494752
304 Y → C: in PC deficiency
451 R → C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
572 binding
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
773 binding
1077 mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.

5vyzC Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
35% identity, 65% coverage: 57:163/164 of query aligns to 976:1081/1083 of 5vyzC

query
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5vyzC

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L

F

K

N

I

L

N

N

N

G

K

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R

A

R

E

E

V

V

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V

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D

D

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-

S

-

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-

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F

A

D

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L

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L

A

E

K

K

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E

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T

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G

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N

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P

N

N

A

-

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M

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E

N

T

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F

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K

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D

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L

L

L

I

I

Q

E

Sites not aligning to the query:

3bg3A Crystal structure of human pyruvate carboxylase (missing the biotin carboxylase domain at the n-terminus) (see paper)
31% identity, 65% coverage: 57:163/164 of query aligns to 578:678/680 of 3bg3A

query
sites
3bg3A

A

A

A

G

K

Q

K

R

E

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T

F

L

F

K

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N

N

N

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D

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F

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D

A

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E

E

K

K

A

L

L

-

K

G

D

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N

K

G

G

Q

Q

A

-

N

-

A

-

K

-

L

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-

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A

A

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P

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A

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M

M

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E

N

T

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S

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E

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K

D

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D

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L

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L

Q

E

Sites not aligning to the query:

active site: 79, 185, 248, 278, 280, 415
binding manganese (ii) ion: 79, 248, 278, 280
binding pyruvic acid: 78, 82, 149, 151, 415

7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
42% identity, 40% coverage: 99:163/164 of query aligns to 1080:1144/1146 of 7wtdC

query
sites
7wtdC

I

I

T

G

A

A

P

P

M

M

P

P

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G

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L

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M

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E

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 162, 167, 168, 206, 236, 239, 292
binding coenzyme a: 21, 22, 25, 45, 46, 47, 48, 49, 50, 366, 413, 416, 419, 462, 464, 465, 466, 1024, 1053

7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
42% identity, 40% coverage: 99:163/164 of query aligns to 1081:1145/1147 of 7wtbB

query
sites
7wtbB

I

I

T

G

A

A

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M

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P

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Sites not aligning to the query:

binding acetyl coenzyme *a: 22, 26, 46, 47, 48, 49, 50, 367, 414, 418, 420, 422, 462, 463, 465, 1025
binding phosphoaminophosphonic acid-adenylate ester: 163, 168, 169, 173, 207, 208, 211, 240
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 582, 839, 877, 880, 881

8pn8G Engineered glycolyl-coa carboxylase (l100n variant) with bound coa (see paper)
26% identity, 95% coverage: 10:164/164 of query aligns to 58:213/213 of 8pn8G

query
sites
8pn8G

N

N

F

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E

D

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P

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G

G

G

D

D

D

F

L

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L

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N

-

G

-

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M

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D

D

W

G

E

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N

A

P

P

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S

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W

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R

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-

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W

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Y

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-

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N

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M
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M

K
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K

M

M

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E

N

N

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F

F

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M179 (= M130), K180 (= K131)

8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
39% identity, 45% coverage: 91:164/164 of query aligns to 583:656/657 of 8sgxX

query
sites
8sgxX

Q

E

A

A

N

T

A

T

K

N

L

T

T

K

S

Q

I

I

T

L

A

S

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P

M

M

P

P

G

G

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V

I

I

L

V

E

A

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I

N

K

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V

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G

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E

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M

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K

M

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N

N

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A

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D

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L

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L

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M622 (= M130), K623 (= K131)

3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
40% identity, 38% coverage: 102:164/164 of query aligns to 528:590/591 of 3n6rA

query
sites
3n6rA

P

P

M

M

P

P

G

G

L

L

I

I

L

V

E

K

I

V

N

D

V

V

Q

E

E

V

G

G

D

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E

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G

Q

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A

M

L

V

C

I

T

L

I

E

E

A

A

M
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M

K
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K

M

M

E

E

N

N

I

I

I

L

K

R

S

A

P

E

G

K

D

K

G

G

I

V

V

V

K

A

K

K

I

I

L

N

V

A

T

S

T

A

G

G

E

N

S

S

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L

E

A

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D

I

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L

I

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M

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E

F

F

binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M130), K557 (= K131)

Sites not aligning to the query:

active site: 115, 138, 164, 203, 205, 218, 220, 222, 226, 268, 464

Query Sequence

>Echvi_0275 FitnessBrowser__Cola:Echvi_0275
MYSVTVNEKNFSIEQDGGDFLINGTIMDWEINPIDNRHFQIIKGQKSYVVELVKLDAAKK
ELTLKINNKSAEVKIQDKFDLLLEKLGMNGQANAKLTSITAPMPGLILEINVQEGDTVEK
DQPMVILEAMKMENIIKSPGDGIVKKILVTTGESVEKKQILIQF

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