SitesBLAST
Comparing Ac3H11_4479 FitnessBrowser__acidovorax_3H11:Ac3H11_4479 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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, 41% coverage: 9:457/1095 of query aligns to 6:452/1150 of A0A0H3JRU9
- R21 (= R24) mutation to A: Complete loss of catalytic activity.
- K119 (= K120) binding
- K161 (= K162) binding
- H211 (= H212) binding
- E278 (= E278) binding
- K411 (≠ R416) 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.
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
46% identity, 41% coverage: 9:457/1095 of query aligns to 39:483/1178 of P11498
- V145 (≠ Q113) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R124) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R237) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y271) to C: in PC deficiency
- R451 (= R425) 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
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
46% identity, 41% coverage: 9:457/1095 of query aligns to 8:452/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ V23), T26 (≠ H27), R46 (≠ V47), Q47 (= Q48), K48 (≠ A49), A49 (= A50), D50 (≠ S51), R367 (≠ D371), R414 (= R419), E418 (= E423), R420 (= R425), R422 (≠ D427)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K162), G168 (= G167), G169 (= G168), M173 (= M172), F207 (≠ L206), I208 (≠ M207), P211 (≠ A210), H240 (≠ F238)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
46% identity, 41% coverage: 9:457/1095 of query aligns to 7:451/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K162), G167 (= G167), G168 (= G168), F206 (≠ L206), Q236 (= Q235), H239 (≠ F238), E292 (= E294)
- binding coenzyme a: F21 (≠ V23), R22 (= R24), T25 (≠ H27), R45 (≠ V47), Q46 (= Q48), K47 (≠ A49), A48 (= A50), D49 (≠ S51), E50 (≠ A52), R366 (≠ D371), R413 (= R419), A416 (= A422), R419 (= R425)
Sites not aligning to the query:
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
46% identity, 41% coverage: 9:457/1095 of query aligns to 39:483/1178 of Q05920
- K39 (= K9) modified: N6-acetyllysine
- K79 (≠ A49) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L116) modified: N6-acetyllysine
- K152 (= K120) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N209) modified: N6-acetyllysine
- K434 (≠ R406) 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
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
42% identity, 41% coverage: 9:457/1095 of query aligns to 4:443/1137 of 3bg5A
- active site: K117 (= K120), K159 (= K162), S189 (≠ D199), H202 (= H212), R228 (= R237), T267 (= T276), E269 (= E278), E281 (= E294), N283 (= N296), R285 (= R298), E289 (= E302), R337 (= R348)
- binding adenosine-5'-triphosphate: K117 (= K120), M157 (≠ V160), K159 (= K162), Y196 (≠ L206), I197 (≠ M207), H202 (= H212), Q226 (= Q235), H229 (≠ F238), E269 (= E278), L271 (= L280), E281 (= E294), N283 (= N296)
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)
42% identity, 41% coverage: 9:457/1095 of query aligns to 4:439/1133 of 3hb9A
- active site: K117 (= K120), K159 (= K162), H198 (= H212), R224 (= R237), T263 (= T276), E265 (= E278), E277 (= E294), N279 (= N296), R281 (= R298), E285 (= E302), R333 (= R348)
- binding adenosine-5'-diphosphate: K117 (= K120), M157 (≠ V160), Y192 (≠ L206), I193 (≠ M207), H198 (= H212), Q222 (= Q235), H225 (≠ F238), L267 (= L280), I276 (= I293), E277 (= E294)
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
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
43% identity, 42% coverage: 1:460/1095 of query aligns to 2:457/1144 of 5vyzA
- binding adenosine-5'-diphosphate: K123 (= K120), M162 (≠ V160), K164 (= K162), G168 (= G166), G170 (= G168), G171 (= G169), M174 (= M172), Y208 (≠ L206), I209 (≠ M207), H214 (= H212), Q238 (= Q235), N241 (≠ F238), L283 (= L280), E293 (= E294), T449 (= T452)
- binding magnesium ion: E281 (= E278), E293 (= E294)
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
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
44% identity, 41% coverage: 9:460/1095 of query aligns to 4:451/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ H27), F43 (≠ Q48), K44 (≠ A49), A45 (= A50), D46 (vs. gap), S48 (= S51), R363 (≠ D371), H413 (≠ A422), E414 (= E423), R416 (= R425), R418 (≠ D427)
- binding adenosine-5'-triphosphate: K117 (= K120), M156 (≠ V160), K158 (= K162), G163 (= G167), G164 (= G168), G165 (= G169), M168 (= M172), E200 (= E204), Y202 (≠ L206), I203 (≠ M207), H208 (= H212), Q232 (= Q235), N235 (≠ F238), L277 (= L280), E287 (= E294), N289 (= N296), T443 (= T452)
- binding bicarbonate ion: K237 (= K240), R291 (= R298), Q293 (= Q300), E295 (= E302)
- binding biotin: G84 (= G87), V294 (= V301), R342 (= R348)
- binding magnesium ion: E275 (= E278), E287 (= E294)
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: 9:460/1095 of query aligns to 4:451/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R24), N22 (≠ H27), F43 (≠ Q48), K44 (≠ A49), A45 (= A50), R363 (≠ D371), E414 (= E423), R416 (= R425), R418 (≠ D427)
- binding adenosine-5'-diphosphate: K158 (= K162), G163 (= G167), G164 (= G168), M168 (= M172), E200 (= E204), K201 (≠ R205), Y202 (≠ L206), I203 (≠ M207), H208 (= H212), Q232 (= Q235), N235 (≠ F238), E275 (= E278), L277 (= L280), E287 (= E294), T443 (= T452)
- binding bicarbonate ion: R291 (= R298), Q293 (= Q300), V294 (= V301), E295 (= E302)
- binding magnesium ion: E275 (= E278), E287 (= E294)
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
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
40% identity, 41% coverage: 9:456/1095 of query aligns to 2:441/448 of 2vpqB
- active site: V116 (≠ Q122), K156 (= K162), H206 (= H212), R232 (= R237), T271 (= T276), E273 (= E278), E287 (= E294), N289 (= N296), R291 (= R298), E295 (= E302), R337 (= R348)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K120), I154 (≠ V160), K156 (= K162), G161 (= G167), G163 (= G169), I166 (≠ M172), F200 (≠ L206), I201 (≠ M207), E273 (= E278), I275 (≠ L280), M286 (≠ I293), E287 (= E294)
- binding magnesium ion: E273 (= E278), E287 (= E294)
8gk8A R21a staphylococcus aureus pyruvate carboxylase
42% identity, 41% coverage: 9:457/1095 of query aligns to 4:434/1041 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
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
41% identity, 41% coverage: 6:459/1095 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K120), K159 (= K162), D193 (= D199), H206 (= H212), R232 (= R237), T271 (= T276), E273 (= E278), E285 (= E294), N287 (= N296), R289 (= R298), E293 (= E302), R335 (= R348)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K162), G164 (= G167), M166 (= M172), E198 (= E204), Y200 (≠ L206), L201 (≠ M207), H233 (≠ F238), L275 (= L280), E285 (= E294)
- binding magnesium ion: E273 (= E278), E285 (= E294)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
38% identity, 44% coverage: 7:490/1095 of query aligns to 3:500/1129 of 3tw6B
- active site: K124 (= K120), K162 (= K162), H212 (= H212), R238 (= R237), T277 (= T276), E279 (= E278), E293 (= E294), N295 (= N296), R297 (= R298), E301 (= E302), R349 (= R348)
- binding adenosine-5'-diphosphate: K124 (= K120), K162 (= K162), G167 (= G167), G169 (= G169), M172 (= M172), E204 (= E204), L206 (= L206), V207 (≠ M207), H212 (= H212), Q236 (= Q235), N239 (≠ F238), L281 (= L280), E293 (= E294), T450 (= T452)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R348), D395 (= D395)
- binding magnesium ion: E279 (= E278), E293 (= E294)
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
6oi8A Crystal structure of haemophilus influenzae biotin carboxylase complexed with 7-((1r,5s,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)- 6-(2-chloro-6-(pyridin-3-yl)phenyl)pyrido[2,3-d]pyrimidin-2-amine (see paper)
40% identity, 41% coverage: 6:459/1095 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K120), K159 (= K162), D191 (= D199), H204 (= H212), R230 (= R237), T269 (= T276), E271 (= E278), E283 (= E294), N285 (= N296), R287 (= R298), E291 (= E302), R333 (= R348)
- binding 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-6-[2-chloro-6-(pyridin-3-yl)phenyl]pyrido[2,3-d]pyrimidin-2-amine: I157 (≠ V160), K159 (= K162), M164 (= M172), E196 (= E204), Y198 (≠ L206), L199 (≠ M207), H204 (= H212), Q228 (= Q235), E271 (= E278), L273 (= L280), E283 (= E294), I432 (≠ T452)
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)
40% identity, 41% coverage: 6:457/1095 of query aligns to 3:444/453 of 7kctA
- active site: E276 (= E278), E289 (= E294), N291 (= N296), E297 (= E302), R339 (= R348)
- binding adenosine-5'-diphosphate: K117 (= K120), L157 (≠ V160), K159 (= K162), G164 (= G167), G165 (= G168), G166 (= G169), I169 (≠ M172), E201 (= E204), Y203 (≠ L206), I204 (≠ M207), H209 (= H212), Q233 (= Q235), Q237 (= Q239), K238 (= K240), I278 (≠ L280), E289 (= E294), R293 (= R298), Q295 (= Q300), V296 (= V301), E297 (= E302), R339 (= R348)
- binding bicarbonate ion: D116 (= D119), R119 (≠ Q122)
- binding magnesium ion: E276 (= E278), E289 (= E294)
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, 40% coverage: 6:441/1095 of query aligns to 1:429/654 of P9WPQ3
- K322 (≠ R326) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
44% identity, 40% coverage: 8:443/1095 of query aligns to 20:453/1178 of P11154
Sites not aligning to the query:
- 1135 modified: N6-biotinyllysine
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: 6:459/1095 of query aligns to 1:444/448 of P43873
- K116 (= K120) binding
- K159 (= K162) binding
- EKYL 201:204 (≠ ERLM 204:207) binding
- E276 (= E278) binding ; binding
- E288 (= E294) binding ; binding
- N290 (= N296) binding
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
42% identity, 41% coverage: 6:459/1095 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K120), K159 (= K162), D196 (= D199), H209 (= H212), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R348)
- binding calcium ion: E276 (= E278), E288 (= E294), N290 (= N296)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K162), M169 (= M172), E201 (= E204), Y203 (≠ L206), L204 (≠ M207), H236 (≠ F238), L278 (= L280), E288 (= E294), I437 (≠ T452)
Query Sequence
>Ac3H11_4479 FitnessBrowser__acidovorax_3H11:Ac3H11_4479
MPSSVLFTKVLVANRGEIALRTVRALHDLGVASVAVYADDDAASPHVQAASAAVALGATG
PAAYLDGARLVAIAQAQGCDAVHPGYGFLSERADFARACAEAGLRFIGPTPAQLALFGDK
AQARALAQQQGVPLMPGTQAAVTLEEAQAFFAQHAHAGIVIKAIGGGGGRGMRAVASADD
VPAAYARCRSEAQAAFGVDGVYVERLMGNARHIEVQVLGDGRAVIALGERECTLQRRFQK
VVEIAPSPSLPGALRERITTAALSMARAVDYQGLGTFEFLVDLASNDLPFVFIECNPRLQ
VEHTITEEVTGVDLVQAQIALAAGRRLQDIGLDPAAPPAVQGFAVQWRINAETLDAQGNA
TPGSGTLRRFDLPAGPGVRVDTHGAAGATPSPHYDTLLAKLIVHTRSPRFADALRRSQRA
LAECRIDGVATNLALLQALAARPEMESQQVHTRWLESVLSQLLGAIKNVAIEAYAERGEG
QKTLNSSAPPPAGAVLAPMPARVVQLSVAEGDVVAAGAELAVLEAMKMEHVLLTPHAGRV
GALLAVAGGYVAQGQPLLVLDAMDDAAGVEVQGSAANDPDHIRADLQRVIDRHAFTFDAA
RPEAIAKRHAQGGRTARENIADLCDNGSFIEYGALAIAAQARRRSKEDLIANTPADGMVT
GIGGINGALFGDEKSRAVVMSYDATVLAGTQGARNHAKTDRMLGIALAQKLPVVLFAEGG
GGRPGDTDMPIVAGLHVHTFASYAALSGQVPVIGIAAGRCFAGNAALLGCSDVIIATRGS
NIGMGGPAMIEGGGLGVFKPEQIGPSRVQHANGVIDVLVDDEAGAVQAARHYLSFFQGRT
PEWSAPDQRLLRAVVPENRLRVYDTRTAMAGLVDDASLLPLRTGFGAGIHTALARIEGRP
VGLLANNPQHLGGAIDADAADKGARFMQLCNAHGLPIVSLVDTPGFMVGPEVEATAQVRH
VSRLFVTAASLRVPTFSVVLRKGYGLGAMGMTAGGFHAPVFTVAWPTGEFGAMGLEGAVR
LGFRKELEALPEGAERDALFAKLLAKSYANGEAMHMAATLEIDAVIDPADTRAWLARGLA
SAQVAPQGHRFIDTW
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