SitesBLAST
Comparing CCNA_03320 FitnessBrowser__Caulo:CCNA_03320 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)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
44% identity, 42% coverage: 2:449/1078 of query aligns to 3:455/1150 of A0A0H3JRU9
- R21 (= R20) mutation to A: Complete loss of catalytic activity.
- K119 (= K116) binding
- K161 (= K155) binding
- H211 (= H205) binding
- E278 (= E268) binding
- K411 (≠ R405) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 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.
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
44% identity, 41% coverage: 3:444/1078 of query aligns to 2:446/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ A23), F43 (≠ S44), K44 (≠ A45), A45 (= A46), D46 (= D47), S48 (≠ A49), R363 (≠ T362), H413 (≠ T411), E414 (= E412), R416 (≠ K414), R418 (≠ A416)
- binding adenosine-5'-triphosphate: K117 (= K116), M156 (= M153), K158 (= K155), G163 (= G160), G164 (= G161), G165 (= G162), M168 (= M165), E200 (= E197), Y202 (≠ L199), I203 (= I200), H208 (= H205), Q232 (= Q228), N235 (= N231), L277 (= L270), E287 (= E287), N289 (= N289), T443 (= T441)
- binding bicarbonate ion: K237 (= K233), R291 (= R291), Q293 (= Q293), E295 (= E295)
- binding biotin: G84 (= G83), V294 (= V294), R342 (= R339)
- binding magnesium ion: E275 (= E268), E287 (= E287)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 459, 461, 1016, 1017, 1018, 1045
- binding biotin: 1104
- binding magnesium ion: 520, 523, 754
- binding manganese (ii) ion: 535, 704, 733, 735
- binding pyruvic acid: 534, 538, 605, 704, 868
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
44% identity, 41% coverage: 3:444/1078 of query aligns to 2:446/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R20), N22 (≠ A23), F43 (≠ S44), K44 (≠ A45), A45 (= A46), R363 (≠ T362), E414 (= E412), R416 (≠ K414), R418 (≠ A416)
- binding adenosine-5'-diphosphate: K158 (= K155), G163 (= G160), G164 (= G161), M168 (= M165), E200 (= E197), K201 (= K198), Y202 (≠ L199), I203 (= I200), H208 (= H205), Q232 (= Q228), N235 (= N231), E275 (= E268), L277 (= L270), E287 (= E287), T443 (= T441)
- binding bicarbonate ion: R291 (= R291), Q293 (= Q293), V294 (= V294), E295 (= E295)
- binding magnesium ion: E275 (= E268), E287 (= E287)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 459, 460, 461, 1016, 1017, 1018, 1041, 1045
- binding magnesium ion: 520, 523, 754
- binding manganese (ii) ion: 535, 704, 733, 735
- binding pyruvic acid: 538, 572, 605, 607, 704, 868
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
44% identity, 41% coverage: 3:444/1078 of query aligns to 8:452/1144 of 5vyzA
- binding adenosine-5'-diphosphate: K123 (= K116), M162 (= M153), K164 (= K155), G168 (= G159), G170 (= G161), G171 (= G162), M174 (= M165), Y208 (≠ L199), I209 (= I200), H214 (= H205), Q238 (= Q228), N241 (= N231), L283 (= L270), E293 (= E287), T449 (= T441)
- binding magnesium ion: E281 (= E268), E293 (= E287)
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 719, 722, 752, 753, 756
- binding manganese (ii) ion: 541, 710, 739, 741
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
45% identity, 42% coverage: 3:451/1078 of query aligns to 37:488/1178 of Q05920
- K39 (≠ R5) modified: N6-acetyllysine
- K79 (≠ A45) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ T112) modified: N6-acetyllysine
- K152 (= K116) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ R202) modified: N6-acetyllysine
- K434 (≠ R397) 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
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
43% identity, 41% coverage: 3:444/1078 of query aligns to 3:453/1129 of 3tw6B
- active site: K124 (= K116), K162 (= K155), H212 (= H205), R238 (= R230), T277 (= T266), E279 (= E268), E293 (= E287), N295 (= N289), R297 (= R291), E301 (= E295), R349 (= R339)
- binding adenosine-5'-diphosphate: K124 (= K116), K162 (= K155), G167 (= G160), G169 (= G162), M172 (= M165), E204 (= E197), L206 (= L199), V207 (≠ I200), H212 (= H205), Q236 (= Q228), N239 (= N231), L281 (= L270), E293 (= E287), T450 (= T441)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R339), D395 (= D386)
- binding magnesium ion: E279 (= E268), E293 (= E287)
Sites not aligning to the query:
- active site: 544, 650, 713, 742, 744, 877
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 1102
- binding magnesium ion: 529, 530, 532, 763
- binding zinc ion: 544, 713, 742, 744
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
45% identity, 42% coverage: 3:451/1078 of query aligns to 6:457/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A19), T26 (≠ A23), R46 (≠ V43), Q47 (≠ S44), K48 (≠ A45), A49 (= A46), D50 (= D47), R367 (≠ T362), R414 (= R408), E418 (= E412), R420 (≠ K414), R422 (≠ A416)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K155), G168 (= G160), G169 (= G161), M173 (= M165), F207 (≠ L199), I208 (= I200), P211 (≠ A203), H240 (≠ N231)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
45% identity, 42% coverage: 3:451/1078 of query aligns to 5:456/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K155), G167 (= G160), G168 (= G161), F206 (≠ L199), Q236 (= Q228), H239 (≠ N231), E292 (= E287)
- binding coenzyme a: F21 (≠ A19), R22 (= R20), T25 (≠ A23), R45 (≠ V43), Q46 (≠ S44), K47 (≠ A45), A48 (= A46), D49 (= D47), E50 (≠ H48), R366 (≠ T362), R413 (= R408), A416 (≠ T411), R419 (≠ K414)
Sites not aligning to the query:
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
45% identity, 42% coverage: 3:451/1078 of query aligns to 37:488/1178 of P11498
- V145 (≠ H109) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R120) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R230) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y261) to C: in PC deficiency
- R451 (≠ K414) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
Sites not aligning to the query:
- 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.
- 1131:1133 natural variant: Missing (in PC deficiency)
- 1144 modified: N6-biotinyllysine
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
43% identity, 42% coverage: 2:449/1078 of query aligns to 1:446/1137 of 3bg5A
- active site: K117 (= K116), K159 (= K155), S189 (≠ G192), H202 (= H205), R228 (= R230), T267 (= T266), E269 (= E268), E281 (= E287), N283 (= N289), R285 (= R291), E289 (= E295), R337 (= R339)
- binding adenosine-5'-triphosphate: K117 (= K116), M157 (= M153), K159 (= K155), Y196 (≠ L199), I197 (= I200), H202 (= H205), Q226 (= Q228), H229 (≠ N231), E269 (= E268), L271 (= L270), E281 (= E287), N283 (= N289)
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
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
46% identity, 43% coverage: 6:464/1078 of query aligns to 5:456/456 of 8hz4A
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
44% identity, 42% coverage: 6:453/1078 of query aligns to 5:452/654 of P9WPQ3
- K322 (≠ R319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
42% identity, 42% coverage: 2:449/1078 of query aligns to 1:442/1133 of 3hb9A
- active site: K117 (= K116), K159 (= K155), H198 (= H205), R224 (= R230), T263 (= T266), E265 (= E268), E277 (= E287), N279 (= N289), R281 (= R291), E285 (= E295), R333 (= R339)
- binding adenosine-5'-diphosphate: K117 (= K116), M157 (= M153), Y192 (≠ L199), I193 (= I200), H198 (= H205), Q222 (= Q228), H225 (≠ N231), L267 (= L270), I276 (= I286), E277 (= E287)
Sites not aligning to the query:
- active site: 529, 635, 699, 728, 730, 751, 757, 758, 797, 863, 865, 877, 879, 884
- 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
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
40% identity, 41% coverage: 4:448/1078 of query aligns to 1:444/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K155), H206 (= H205), R232 (= R230), T271 (= T266), E273 (= E268), E287 (= E287), N289 (= N289), R291 (= R291), E295 (= E295), R337 (= R339)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M153), K156 (= K155), G161 (= G160), G163 (= G162), I166 (≠ M165), F200 (≠ L199), I201 (= I200), E273 (= E268), I275 (≠ L270), M286 (≠ I286), E287 (= E287)
- binding magnesium ion: E273 (= E268), E287 (= E287)
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)
43% identity, 41% coverage: 4:444/1078 of query aligns to 20:465/1178 of P11154
Sites not aligning to the query:
- 1135 modified: N6-biotinyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase
42% identity, 42% coverage: 2:449/1078 of query aligns to 1:437/1041 of 8gk8A
Sites not aligning to the query:
- binding acetyl coenzyme *a: 445, 447, 1026, 1030
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 457, 462, 463, 464, 570, 572
- binding manganese (ii) ion: 524, 694, 723, 725
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)
41% identity, 41% coverage: 3:447/1078 of query aligns to 4:445/453 of 7kctA
- active site: E276 (= E268), E289 (= E287), N291 (= N289), E297 (= E295), R339 (= R339)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (≠ M153), K159 (= K155), G164 (= G160), G165 (= G161), G166 (= G162), I169 (≠ M165), E201 (= E197), Y203 (≠ L199), I204 (= I200), H209 (= H205), Q233 (= Q228), Q237 (= Q232), K238 (= K233), I278 (≠ L270), E289 (= E287), R293 (= R291), Q295 (= Q293), V296 (= V294), E297 (= E295), R339 (= R339)
- binding bicarbonate ion: D116 (= D115), R119 (≠ A118)
- binding magnesium ion: E276 (= E268), E289 (= E287)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
38% identity, 41% coverage: 1:447/1078 of query aligns to 3:445/445 of 3ouzA
- active site: K161 (= K155), G167 (= G161), G168 (= G162), H211 (= H205), K240 (= K233), T276 (= T266), E278 (= E268), E291 (= E287), N293 (= N289), V298 (= V294), E299 (= E295), R340 (= R339)
- binding adenosine-5'-diphosphate: K119 (= K116), I159 (≠ M153), K161 (= K155), G166 (= G160), G168 (= G162), M171 (= M165), E203 (= E197), Y205 (≠ L199), I206 (= I200), H211 (= H205), Q235 (= Q228), L280 (= L270), E291 (= E287), T439 (= T441)
- binding magnesium ion: E278 (= E268), E291 (= E287)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
38% identity, 41% coverage: 1:447/1078 of query aligns to 4:446/446 of 3ouuA
- active site: K162 (= K155), G168 (= G161), G169 (= G162), H212 (= H205), K241 (= K233), T277 (= T266), E279 (= E268), E292 (= E287), N294 (= N289), V299 (= V294), E300 (= E295), R341 (= R339)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K116), I160 (≠ M153), K162 (= K155), G167 (= G160), G168 (= G161), G169 (= G162), M172 (= M165), E204 (= E197), Y206 (≠ L199), I207 (= I200), H212 (= H205), Q236 (= Q228), H239 (≠ N231), L281 (= L270), E292 (= E287), T440 (= T441)
- binding calcium ion: E279 (= E268), E292 (= E287)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
41% identity, 40% coverage: 3:429/1078 of query aligns to 2:425/447 of 2vqdA
- active site: K116 (= K116), K159 (= K155), P196 (≠ G192), H209 (= H205), R235 (= R230), T274 (= T266), E276 (= E268), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R339)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M153), K159 (= K155), G164 (= G160), G166 (= G162), F203 (≠ L199), L204 (≠ I200), H209 (= H205), Q233 (= Q228), H236 (≠ N231), L278 (= L270), E288 (= E287)
- binding magnesium ion: E276 (= E268), E288 (= E287)
Sites not aligning to the query:
Query Sequence
>CCNA_03320 FitnessBrowser__Caulo:CCNA_03320
MSLSRVLIANRGEIAVRIARTAAEAGLESVAIYAADDAQSPHVSAADHAVALPGAGARAY
LDIAAVVAAAKAQGCDALHPGYGFLSENPHLARACAEAGIVFIGPSPEHLTTFGDKAAAR
ALAAERGLPLIPGTGAITLEAARAFQAEHGAIMLKARAGGGGRGMRMVLDPGELDAAFAA
CEREALAAFGDGGLYAEKLIERARHIEVQIVGDGDQVLALGDRDCSLQRRNQKLVEIAPA
ALPDNLRAALAGWSERLCAGYRGLATVEFLVDADPHSPSGGEAFFIEVNPRLQVEHTVTE
EVTGLDLVRLQFDLAAGKRLGELELTNTPPPFGVAIQARINAETLTPEGQVRPSTGTLSA
WTPPGGPGVRVDAGVAAGLTIGAAYDSLLAKVIVRGRTPSEAASRLDRALTELKVAGVAT
TAPLVRAILAHPTAVTGEATTTFIAQHAETLAAEAQRLTPETTASVTRFEVLAGAEPVVA
PLAATVGAITIREGDLVRPGQALAVLEAMKMEHLVSASAGGRVVKIVVQGGATVAEGQPL
VFLEPAEVESALDGETVEQDLDALRPDLAEVVARHRHTLDEARPEAVAKRRKTGHRTARE
NIDDLVDPGSFLEYGALAIAAQKRRRSTEDLIANTPADGLITGIGTVNGALFPPDKARTA
ALAYDFTVLAGTQGAMNHRKSDRLMALIADQKLPVVWFAEGGGGRPGDTDTTAVAGLDVP
TFRSFAQLSGLVPKIAIVAGRCFAGNAAIAGLSEIIIATRDSNLGMGGPAMIEGGGLGVF
RPEEIGPSAHQWKNGVIDILADDEAHATRLAKQALSYFQGTLSTWTAPDQRRLRHAIPEN
RLRVYDVRGLINHLVDEGSFLELRGGFAAGMVTGLIRIEGRPMGLIANDPRHLGGAIDCE
GAEKAARFLQLCDAFALPVLSLCDTPGFMVGPDSEDAAAVRRVSRQFIAGAKLRSPLFTI
VTRKGYGLGAQAMAGGSFHSPAFIAAWPTGEFGGMGLEGAVKLGYRKELEAETDPVKQKA
LYDQLVARLYAAGKATSMAAALEIDAVIDPADTRRWVIGGLDAAAGVSRPWEVRVDSF
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