SitesBLAST
Comparing RR42_RS18165 FitnessBrowser__Cup4G11:RR42_RS18165 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)
42% identity, 43% coverage: 4:485/1112 of query aligns to 5:477/1150 of A0A0H3JRU9
- R21 (= R20) mutation to A: Complete loss of catalytic activity.
- K119 (= K116) binding
- K161 (= K162) binding
- H211 (= H212) binding
- E278 (= E279) binding
- K411 (≠ Q418) 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.
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
44% identity, 41% coverage: 4:458/1112 of query aligns to 38:482/1178 of Q05920
- K39 (= K5) modified: N6-acetyllysine
- K79 (= K45) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L112) modified: N6-acetyllysine
- K152 (= K116) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ A209) modified: N6-acetyllysine
- K434 (≠ G410) 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
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
45% identity, 41% coverage: 4:458/1112 of query aligns to 6:450/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K162), G167 (= G167), G168 (= G168), F206 (≠ I206), Q236 (= Q236), H239 (= H239), E292 (= E298)
- binding coenzyme a: F21 (≠ A19), R22 (= R20), T25 (≠ A23), R45 (≠ V43), Q46 (≠ R44), K47 (= K45), A48 (= A46), D49 (= D47), E50 (≠ G48), R366 (≠ E373), R413 (= R421), A416 (≠ C424), R419 (= R427)
Sites not aligning to the query:
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
45% identity, 41% coverage: 4:458/1112 of query aligns to 7:451/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A19), T26 (≠ A23), R46 (≠ V43), Q47 (≠ R44), K48 (= K45), A49 (= A46), D50 (= D47), R367 (≠ E373), R414 (= R421), E418 (= E425), R420 (= R427), R422 (≠ E429)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K162), G168 (= G167), G169 (= G168), M173 (= M172), F207 (≠ I206), I208 (≠ V207), P211 (= P210), H240 (= H239)
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, 41% coverage: 4:458/1112 of query aligns to 38:482/1178 of P11498
- V145 (= V109) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R120) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R238) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y272) to C: in PC deficiency
- R451 (= R427) 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)
41% identity, 43% coverage: 4:485/1112 of query aligns to 3:468/1137 of 3bg5A
- active site: K117 (= K116), K159 (= K162), S189 (≠ G199), H202 (= H212), R228 (= R238), T267 (= T277), E269 (= E279), E281 (= E298), N283 (= N300), R285 (= R302), E289 (= E306), R337 (= R350)
- binding adenosine-5'-triphosphate: K117 (= K116), M157 (= M160), K159 (= K162), Y196 (≠ I206), I197 (≠ V207), H202 (= H212), Q226 (= Q236), H229 (= H239), E269 (= E279), L271 (= L281), E281 (= E298), N283 (= N300)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (≠ A480)
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: 471, 472, 473, 579
- binding manganese (ii) ion: 533, 732, 734
- binding pyruvic acid: 603, 703
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
42% identity, 43% coverage: 4:485/1112 of query aligns to 3:473/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ A23), F43 (≠ R44), K44 (= K45), A45 (= A46), D46 (= D47), S48 (≠ A49), R363 (≠ E373), H413 (≠ C424), E414 (= E425), R416 (= R427), R418 (≠ E429), R459 (≠ G471), R461 (≠ P473)
- binding adenosine-5'-triphosphate: K117 (= K116), M156 (= M160), K158 (= K162), G163 (= G167), G164 (= G168), G165 (= G169), M168 (= M172), E200 (= E204), Y202 (≠ I206), I203 (≠ V207), H208 (= H212), Q232 (= Q236), N235 (≠ H239), L277 (= L281), E287 (= E298), N289 (= N300), T443 (= T454)
- binding bicarbonate ion: K237 (= K241), R291 (= R302), Q293 (= Q304), E295 (= E306)
- binding biotin: G84 (= G83), V294 (= V305), R342 (= R350)
- binding magnesium ion: E275 (= E279), E287 (= E298)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 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)
42% identity, 43% coverage: 4:485/1112 of query aligns to 3:473/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R20), N22 (≠ A23), F43 (≠ R44), K44 (= K45), A45 (= A46), R363 (≠ E373), E414 (= E425), R416 (= R427), R418 (≠ E429), R459 (≠ G471), D460 (= D472), R461 (≠ P473)
- binding adenosine-5'-diphosphate: K158 (= K162), G163 (= G167), G164 (= G168), M168 (= M172), E200 (= E204), K201 (≠ R205), Y202 (≠ I206), I203 (≠ V207), H208 (= H212), Q232 (= Q236), N235 (≠ H239), E275 (= E279), L277 (= L281), E287 (= E298), T443 (= T454)
- binding bicarbonate ion: R291 (= R302), Q293 (= Q304), V294 (= V305), E295 (= E306)
- binding magnesium ion: E275 (= E279), E287 (= E298)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 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)
42% identity, 43% coverage: 4:485/1112 of query aligns to 9:479/1144 of 5vyzA
- binding adenosine-5'-diphosphate: K123 (= K116), M162 (= M160), K164 (= K162), G168 (= G166), G170 (= G168), G171 (= G169), M174 (= M172), Y208 (≠ I206), I209 (≠ V207), H214 (= H212), Q238 (= Q236), N241 (≠ H239), L283 (= L281), E293 (= E298), T449 (= T454)
- binding magnesium ion: E281 (= E279), E293 (= E298)
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
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
43% identity, 41% coverage: 4:458/1112 of query aligns to 1:441/448 of 2vpqB
- active site: V116 (≠ R118), K156 (= K162), H206 (= H212), R232 (= R238), T271 (= T277), E273 (= E279), E287 (= E298), N289 (= N300), R291 (= R302), E295 (= E306), R337 (= R350)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M160), K156 (= K162), G161 (= G167), G163 (= G169), I166 (≠ M172), F200 (≠ I206), I201 (≠ V207), E273 (= E279), I275 (≠ L281), M286 (= M297), E287 (= E298)
- binding magnesium ion: E273 (= E279), E287 (= E298)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
40% identity, 43% coverage: 4:485/1112 of query aligns to 3:464/1133 of 3hb9A
- active site: K117 (= K116), K159 (= K162), H198 (= H212), R224 (= R238), T263 (= T277), E265 (= E279), E277 (= E298), N279 (= N300), R281 (= R302), E285 (= E306), R333 (= R350)
- binding adenosine-5'-diphosphate: K117 (= K116), M157 (= M160), Y192 (≠ I206), I193 (≠ V207), H198 (= H212), Q222 (= Q236), H225 (= H239), L267 (= L281), I276 (≠ M297), E277 (= E298)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (≠ A480), N462 (≠ A483)
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: 467, 468, 575, 577
- binding manganese (ii) ion: 529, 728, 730
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
46% identity, 41% coverage: 3:458/1112 of query aligns to 2:444/654 of P9WPQ3
- K322 (≠ H333) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
48% identity, 39% coverage: 3:433/1112 of query aligns to 2:413/456 of 8hz4A
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
41% identity, 42% coverage: 5:472/1112 of query aligns to 5:467/1129 of 3tw6B
- active site: K124 (= K116), K162 (= K162), H212 (= H212), R238 (= R238), T277 (= T277), E279 (= E279), E293 (= E298), N295 (= N300), R297 (= R302), E301 (= E306), R349 (= R350)
- binding adenosine-5'-diphosphate: K124 (= K116), K162 (= K162), G167 (= G167), G169 (= G169), M172 (= M172), E204 (= E204), L206 (≠ I206), V207 (= V207), H212 (= H212), Q236 (= Q236), N239 (≠ H239), L281 (= L281), E293 (= E298), T450 (= T454)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R350), D395 (= D397)
- binding magnesium ion: E279 (= E279), E293 (= E298)
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
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
42% identity, 41% coverage: 5:461/1112 of query aligns to 4:442/444 of 2vr1A
- active site: K116 (= K116), K159 (≠ L164), D194 (≠ G199), H207 (= H212), R233 (= R238), T272 (= T277), E274 (= E279), E286 (= E298), N288 (= N300), R290 (= R302), E294 (= E306), R336 (= R350)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (≠ L164), R165 (= R170), M167 (= M172), Y201 (≠ I206), L202 (≠ V207), E274 (= E279), L276 (= L281), E286 (= E298), N288 (= N300), I435 (≠ T454)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
42% identity, 41% coverage: 3:461/1112 of query aligns to 2:441/442 of 4mv4A
- active site: K116 (= K116), K159 (≠ L164), D193 (≠ G199), H206 (= H212), R232 (= R238), T271 (= T277), E273 (= E279), E285 (= E298), N287 (= N300), R289 (= R302), E293 (= E306), R335 (= R350)
- binding phosphomethylphosphonic acid adenylate ester: K159 (≠ L164), G164 (= G169), M166 (= M172), E198 (= E204), Y200 (≠ I206), L201 (≠ V207), H233 (= H239), L275 (= L281), E285 (= E298)
- binding magnesium ion: E273 (= E279), E285 (= E298)
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)
42% identity, 43% coverage: 4:482/1112 of query aligns to 20:489/1178 of P11154
Sites not aligning to the query:
- 1135 modified: N6-biotinyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase
40% identity, 43% coverage: 4:485/1112 of query aligns to 3:459/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E425), R402 (= R427), R404 (≠ E429), L445 (≠ G471), R447 (≠ P473)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (≠ A483)
- binding coenzyme a: R42 (≠ V43), Y43 (≠ R44), A45 (= A46), D46 (= D47), E47 (≠ G48), S48 (≠ A49)
Sites not aligning to the query:
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
42% identity, 41% coverage: 3:461/1112 of query aligns to 2:444/447 of 2vqdA
- active site: K116 (= K116), K159 (= K162), P196 (≠ G199), H209 (= H212), R235 (= R238), T274 (= T277), E276 (= E279), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R350)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M160), K159 (= K162), G164 (= G167), G166 (= G169), F203 (≠ I206), L204 (≠ V207), H209 (= H212), Q233 (= Q236), H236 (= H239), L278 (= L281), E288 (= E298), I437 (≠ T454)
- binding magnesium ion: E276 (= E279), E288 (= E298)
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
42% identity, 41% coverage: 3:461/1112 of query aligns to 2:444/448 of P43873
- K116 (= K116) binding
- K159 (= K162) binding
- EKYL 201:204 (≠ ERIV 204:207) binding
- E276 (= E279) binding ; binding
- E288 (= E298) binding ; binding
- N290 (= N300) binding
Query Sequence
>RR42_RS18165 FitnessBrowser__Cup4G11:RR42_RS18165
MTFRKLLIANRGEIAIRIARAAAAMDLQSMALYSEDDRDALHVRKADGAVALPGTGPRAY
LDIAQVVDAARRSGCDVIHPGYGLLSENAEFAQACLDAGLAFVGPAPDVLRLFGDKARAR
ALARECDVPVVPGSTGPTTLAATHAFFASLQAPGKAAGMMIKALAGGGGRGMRAVHAAAD
IDEAYARCVSEATAAFGNGAVYVERIVHAPRHIEIQVVADAAGGVIALGERECSLQRRHQ
KLVEVAPSPSLDAGMRARLAQAAITLARASAYRGIGTFEFLLGADGADGADGEFWFMEAN
PRLQVEHTVTEMVTGVDLVQVQLAIAAGQDLGHLGLAQAPAPRGIAVQLRINAEHLDAQG
QLRPASGRIDAYEPPSGPGVRVDGAGHAGMTVNPRFDSLLAKLIVHEPGGDYARALAQAY
RALCEFRIEGIDTNRRLLQDLLLRDDVRRNAVHTQYLDAALPALAAQSQGGDPGHPALHA
VAAASSTQALASTLPDDLPDDAALLSAPMDGALAAVQVRPGDRVRRGQSLAIIEAMKMEH
PLEAPGAGEVLRVLAAPGDVLRAGAPVIVLSLDEGGHHGAQAGAAVDPAHIRADLRDALA
RHALTQDAARPQAVDKHHARGGRTARENIAQLCDAGSFIEYGALAIAAQRQRRSVEDLER
ATPADGIVTGIGTVNAERFPATDARCMVLAYDYTVLAGTQGFYGHKKLDRMLALARQWRL
PVVLFAEGGGGRPGDTDTPVVAGLDCTSFIQFARLSGQVPLVGIVSGRCFAGNAALLGCA
DVIIATRNATIGMGGPAMIEGGGLGVFAAEEVGPVSVQAPNGVIDVLVDDEIAAVETARR
YLSYFQGDLPDWEAGDARALRHLIPENRLRSYDMRGVLAALADHDSVLELRAAFGAGIIT
ALIRIEGRAFGCIANNPRHLGGAIDADAADKAARFMQLCDAHGLPIVSLCDTPGFMVGPE
AEKTATVRHVSRLFVTAGALRVPFFTVVLRKGYGLGAQAMAGGSFSAPFFTAAWPSGEFG
AMGIEGSIRLGFRKELEAVADPDEREALFARMIEGAYRRGRALNMASHLEIDAVIDPADT
RHWLLRGLASALPASAARDTPAAGSRRFIDTW
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