SitesBLAST
Comparing 5210426 Shew_2867 pyruvate carboxylase, propionyl-CoA carboxylase (RefSeq) 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)
43% identity, 41% coverage: 7:451/1094 of query aligns to 6:451/1150 of A0A0H3JRU9
- R21 (≠ Q22) mutation to A: Complete loss of catalytic activity.
- K119 (= K118) binding
- K161 (= K161) binding
- H211 (= H211) binding
- E278 (= E278) binding
- K411 (= K411) 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)
43% identity, 41% coverage: 6:451/1094 of query aligns to 38:482/1178 of Q05920
- K39 (≠ R7) modified: N6-acetyllysine
- K79 (= K47) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L114) modified: N6-acetyllysine
- K152 (= K118) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ H208) modified: N6-acetyllysine
- K434 (≠ E403) 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)
43% identity, 41% coverage: 6:451/1094 of query aligns to 38:482/1178 of P11498
- V145 (≠ L111) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R122) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R237) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y271) to C: in PC deficiency
- R451 (≠ N420) 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
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
43% identity, 41% coverage: 6:451/1094 of query aligns to 6:450/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K161), G167 (= G166), G168 (= G167), F206 (≠ L205), Q236 (= Q235), H239 (≠ N238), E292 (= E293)
- binding coenzyme a: F21 (≠ A21), R22 (≠ Q22), T25 (≠ A25), R45 (≠ T45), Q46 (≠ K46), K47 (= K47), A48 (= A48), D49 (= D49), E50 (≠ Q50), R366 (≠ Q368), R413 (≠ L414), A416 (≠ K417), R419 (≠ N420)
Sites not aligning to the query:
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
43% identity, 41% coverage: 6:451/1094 of query aligns to 7:451/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A21), T26 (≠ A25), R46 (≠ T45), Q47 (≠ K46), K48 (= K47), A49 (= A48), D50 (= D49), R367 (≠ Q368), R414 (≠ L414), E418 (≠ A418), R420 (≠ N420), R422 (≠ D422)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K161), G168 (= G166), G169 (= G167), M173 (= M171), F207 (≠ L205), I208 (≠ V206), P211 (≠ A209), H240 (≠ N238)
Sites not aligning to the query:
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
42% identity, 41% coverage: 7:451/1094 of query aligns to 4:447/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ A25), F43 (≠ K46), K44 (= K47), A45 (= A48), D46 (= D49), S48 (≠ A51), R363 (≠ Q368), H413 (≠ K417), E414 (≠ A418), R416 (≠ N420), R418 (≠ D422)
- binding adenosine-5'-triphosphate: K117 (= K118), M156 (= M159), K158 (= K161), G163 (= G166), G164 (= G167), G165 (= G168), M168 (= M171), E200 (= E203), Y202 (≠ L205), I203 (≠ V206), H208 (= H211), Q232 (= Q235), N235 (= N238), L277 (= L280), E287 (= E293), N289 (= N295), T443 (= T447)
- binding bicarbonate ion: K237 (= K240), R291 (= R297), Q293 (= Q299), E295 (= E301)
- binding biotin: G84 (= G85), V294 (= V300), R342 (= R345)
- binding magnesium ion: E275 (= E278), E287 (= E293)
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
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
42% identity, 41% coverage: 7:451/1094 of query aligns to 10:453/1144 of 5vyzA
- binding adenosine-5'-diphosphate: K123 (= K118), M162 (= M159), K164 (= K161), G168 (= G165), G170 (= G167), G171 (= G168), M174 (= M171), Y208 (≠ L205), I209 (≠ V206), H214 (= H211), Q238 (= Q235), N241 (= N238), L283 (= L280), E293 (= E293), T449 (= T447)
- binding magnesium ion: E281 (= E278), E293 (= E293)
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
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
42% identity, 41% coverage: 7:451/1094 of query aligns to 4:447/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (≠ Q22), N22 (≠ A25), F43 (≠ K46), K44 (= K47), A45 (= A48), R363 (≠ Q368), E414 (≠ A418), R416 (≠ N420), R418 (≠ D422)
- binding adenosine-5'-diphosphate: K158 (= K161), G163 (= G166), G164 (= G167), M168 (= M171), E200 (= E203), K201 (≠ Q204), Y202 (≠ L205), I203 (≠ V206), H208 (= H211), Q232 (= Q235), N235 (= N238), E275 (= E278), L277 (= L280), E287 (= E293), T443 (= T447)
- binding bicarbonate ion: R291 (= R297), Q293 (= Q299), V294 (= V300), E295 (= E301)
- binding magnesium ion: E275 (= E278), E287 (= E293)
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
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
41% identity, 41% coverage: 7:451/1094 of query aligns to 4:442/1137 of 3bg5A
- active site: K117 (= K118), K159 (= K161), S189 (≠ G198), H202 (= H211), R228 (= R237), T267 (= T276), E269 (= E278), E281 (= E293), N283 (= N295), R285 (= R297), E289 (= E301), R337 (= R345)
- binding adenosine-5'-triphosphate: K117 (= K118), M157 (= M159), K159 (= K161), Y196 (≠ L205), I197 (≠ V206), H202 (= H211), Q226 (= Q235), H229 (≠ N238), E269 (= E278), L271 (= L280), E281 (= E293), N283 (= N295)
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
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
41% identity, 41% coverage: 7:451/1094 of query aligns to 4:438/1133 of 3hb9A
- active site: K117 (= K118), K159 (= K161), H198 (= H211), R224 (= R237), T263 (= T276), E265 (= E278), E277 (= E293), N279 (= N295), R281 (= R297), E285 (= E301), R333 (= R345)
- binding adenosine-5'-diphosphate: K117 (= K118), M157 (= M159), Y192 (≠ L205), I193 (≠ V206), H198 (= H211), Q222 (= Q235), H225 (≠ N238), L267 (= L280), I276 (≠ M292), E277 (= E293)
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
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
40% identity, 41% coverage: 5:451/1094 of query aligns to 3:454/1129 of 3tw6B
- active site: K124 (= K118), K162 (= K161), H212 (= H211), R238 (= R237), T277 (= T276), E279 (= E278), E293 (= E293), N295 (= N295), R297 (= R297), E301 (= E301), R349 (= R345)
- binding adenosine-5'-diphosphate: K124 (= K118), K162 (= K161), G167 (= G166), G169 (= G168), M172 (= M171), E204 (= E203), L206 (= L205), V207 (= V206), H212 (= H211), Q236 (= Q235), N239 (= N238), L281 (= L280), E293 (= E293), T450 (= T447)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R345), D395 (= D392)
- binding magnesium ion: E279 (= E278), E293 (= E293)
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
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
38% identity, 40% coverage: 4:436/1094 of query aligns to 1:426/447 of 2vqdA
- active site: K116 (= K118), K159 (= K161), P196 (≠ G198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R345)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K118), I157 (≠ M159), K159 (= K161), G164 (= G166), G166 (= G168), F203 (≠ L205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (≠ N238), L278 (= L280), E288 (= E293)
- binding magnesium ion: E276 (= E278), E288 (= E293)
Sites not aligning to the query:
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 42% coverage: 4:459/1094 of query aligns to 1:452/654 of P9WPQ3
- K322 (≠ E328) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
38% identity, 41% coverage: 4:454/1094 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K118), K159 (= K161), D194 (≠ G198), H207 (= H211), R233 (= R237), T272 (= T276), E274 (= E278), E286 (= E293), N288 (= N295), R290 (= R297), E294 (= E301), R336 (= R345)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K161), R165 (= R169), M167 (= M171), Y201 (≠ L205), L202 (≠ V206), E274 (= E278), L276 (= L280), E286 (= E293), N288 (= N295), I435 (≠ T447)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
40% identity, 41% coverage: 7:453/1094 of query aligns to 2:443/448 of 2vpqB
- active site: V116 (≠ T120), K156 (= K161), H206 (= H211), R232 (= R237), T271 (= T276), E273 (= E278), E287 (= E293), N289 (= N295), R291 (= R297), E295 (= E301), R337 (= R345)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K118), I154 (≠ M159), K156 (= K161), G161 (= G166), G163 (= G168), I166 (≠ M171), F200 (≠ L205), I201 (≠ V206), E273 (= E278), I275 (≠ L280), M286 (= M292), E287 (= E293)
- binding magnesium ion: E273 (= E278), E287 (= E293)
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)
38% identity, 41% coverage: 3:453/1094 of query aligns to 2:445/453 of 7kctA
- active site: E276 (= E278), E289 (= E293), N291 (= N295), E297 (= E301), R339 (= R345)
- binding adenosine-5'-diphosphate: K117 (= K118), L157 (≠ M159), K159 (= K161), G164 (= G166), G165 (= G167), G166 (= G168), I169 (≠ M171), E201 (= E203), Y203 (≠ L205), I204 (≠ V206), H209 (= H211), Q233 (= Q235), Q237 (= Q239), K238 (= K240), I278 (≠ L280), E289 (= E293), R293 (= R297), Q295 (= Q299), V296 (= V300), E297 (= E301), R339 (= R345)
- binding bicarbonate ion: D116 (≠ N117), R119 (≠ T120)
- binding magnesium ion: E276 (= E278), E289 (= E293)
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, 41% coverage: 6:451/1094 of query aligns to 20:466/1178 of P11154
Sites not aligning to the query:
- 1135 modified: N6-biotinyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase
40% identity, 41% coverage: 7:451/1094 of query aligns to 4:433/1041 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
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
38% identity, 41% coverage: 4:454/1094 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K118), K159 (= K161), D196 (≠ G198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R345)
- binding adenosine-5'-diphosphate: Y82 (= Y84), G83 (= G85), K116 (= K118), K159 (= K161), G164 (= G166), G164 (= G166), G165 (= G167), G166 (= G168), R167 (= R169), M169 (= M171), F193 (= F195), E201 (= E203), K202 (≠ Q204), Y203 (≠ L205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (≠ N238), K238 (= K240), L278 (= L280), E288 (= E293), R292 (= R297), V295 (= V300), E296 (= E301), R338 (= R345), D382 (= D392), I437 (≠ T447)
- binding calcium ion: E87 (= E89), E276 (= E278), E288 (= E293), E288 (= E293), N290 (= N295)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
38% identity, 41% coverage: 4:454/1094 of query aligns to 1:444/444 of 3g8cA
- active site: K116 (= K118), K159 (= K161), D196 (≠ G198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R345)
- binding adenosine-5'-diphosphate: I157 (≠ M159), K159 (= K161), G164 (= G166), M169 (= M171), E201 (= E203), K202 (≠ Q204), Y203 (≠ L205), L204 (≠ V206), Q233 (= Q235), H236 (≠ N238), L278 (= L280), E288 (= E293), I437 (≠ T447)
- binding bicarbonate ion: K238 (= K240), R292 (= R297), Q294 (= Q299), V295 (= V300), E296 (= E301)
- binding biotin: Y82 (= Y84), F84 (= F86), R292 (= R297), V295 (= V300), R338 (= R345), D382 (= D392)
- binding magnesium ion: E276 (= E278), E288 (= E293)
Query Sequence
>5210426 Shew_2867 pyruvate carboxylase, propionyl-CoA carboxylase (RefSeq)
MTRVFNRILIANRGEIAIRIAQTCADMGIDSLAIYAEDDSQSLHTKKADQAVALKGRGVK
AYLDIEQLIAVAKAHGCDAVHPGYGFLSENSSFSKRCHEEGICFIGSSAELLDLLGNKAT
ARETALRSDTPLTGGINKPCSLEEVQAFFTSLGDGAAVMIKALAGGGGRGMRPVSRYEDL
AEAYRQCREEAIIAFGSGELYVEQLVQHARHIEVQILGDGTGAAVHAWERECTLQRRNQK
LLEIAPSPSLDDATRMPIIESALQLASDVKYQGLGTFEFLLDADDHSKFYFMEINPRIQV
EHTITEEITGLNLVKLQILLGAGKTLAELSLTEAPIKRGCAIQARINLEQMLPDGSTKPA
SGVIKAYQVPNGHNVRVDDYLYAGYKVSPSYDSLGAKIIAKGEDFSAALNKVYLSLKALN
IDGVQSNKALLMNLLQREEVQHNRLSTRFVEAHMAELLADDDHHEHFFNIASDQQETVQA
VNIPAGCEGVKSPTAGVLVQVNIESGDEVFAGQEIAVIEAMKMEIPVKSEHAGIVTEVLT
GNIGEVIDEHQILAVIQPGEVSVTGGQTEMEIDLDYIRANLAEFFDRRDKTLDESRSEAV
AKRHSEGKRTARENLNDLLDEGSFNEYGQLAIAAQRQKHAIDKLVEISPADGKITGIGTV
NADSFGEEAARCAVMSYDYTVMAGSQGLVNHKKTDRLLELCKKWKLPLVIFAEGAGGRPS
DTDYPGVAFLNLHTFSSLGELSGLVPTVGIAAGNCFAGNAALYGVCDLTIATRQASIGMA
GPAMIEGGGLGVFKPEEVGPPSVLSPNGVIDILVEDEAEAVAVTKKYLSYFQGDLSEWQV
ADQRRLRHLIPENRMAIYDIREVIDTLCDKDSVLELRREFAKNMITAMVRIEGKAYGLYA
NDPRFLGGAIDADAGDKLARFIQLCDAHDIPMISLCDTPGFMVGPESEKRATVRHISRLF
VHGANSTVPLFALVLRKGYGLGVMGMTGGGFTAPVFTASWPSGEFGAMGIEGAVRIAAKR
QLEAIADPDEREATFKAMVDKLYSHGSAINTASYLELDAVIDPMESRDWIVRGLACLPKP
EKRSGKKRNCIDTW
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