SitesBLAST
Comparing WP_037919564.1 NCBI__GCF_000619805.1:WP_037919564.1 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)
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)
59% identity, 92% coverage: 14:459/484 of query aligns to 5:450/453 of 7kctA
- active site: E276 (= E285), E289 (= E298), N291 (= N300), E297 (= E306), R339 (= R348)
- binding adenosine-5'-diphosphate: K117 (= K126), L157 (≠ I166), K159 (= K168), G164 (= G173), G165 (= G174), G166 (= G175), I169 (≠ M178), E201 (= E210), Y203 (= Y212), I204 (≠ V213), H209 (= H218), Q233 (= Q242), Q237 (= Q246), K238 (= K247), I278 (≠ L287), E289 (= E298), R293 (= R302), Q295 (= Q304), V296 (= V305), E297 (= E306), R339 (= R348)
- binding bicarbonate ion: D116 (= D125), R119 (≠ A128)
- binding magnesium ion: E276 (= E285), E289 (= E298)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
50% identity, 93% coverage: 11:461/484 of query aligns to 2:460/1150 of A0A0H3JRU9
- R21 (= R30) mutation to A: Complete loss of catalytic activity.
- K119 (= K126) binding ATP
- K161 (= K168) binding ATP
- H211 (= H218) binding ATP
- E278 (= E285) binding ATP
- K411 (≠ R412) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding substrate
- 542 binding Mn(2+)
- 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 Mn(2+)
- 741 binding Mn(2+)
- 743 binding Mn(2+)
- 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.
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
52% identity, 91% coverage: 14:454/484 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ A128), K156 (= K168), H206 (= H218), R232 (= R244), T271 (= T283), E273 (= E285), E287 (= E298), N289 (= N300), R291 (= R302), E295 (= E306), R337 (= R348)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K126), I154 (= I166), K156 (= K168), G161 (= G173), G163 (= G175), I166 (≠ M178), F200 (≠ Y212), I201 (≠ V213), E273 (= E285), I275 (≠ L287), M286 (≠ I297), E287 (= E298)
- binding magnesium ion: E273 (= E285), E287 (= E298)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
52% identity, 92% coverage: 13:455/484 of query aligns to 2:441/442 of 4mv4A
- active site: K116 (= K126), K159 (= K168), D193 (≠ G205), H206 (= H218), R232 (= R244), T271 (= T283), E273 (= E285), E285 (= E298), N287 (= N300), R289 (= R302), E293 (= E306), R335 (= R348)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K168), G164 (≠ R176), M166 (= M178), E198 (= E210), Y200 (= Y212), L201 (≠ V213), H233 (= H245), L275 (= L287), E285 (= E298)
- binding magnesium ion: E273 (= E285), E285 (= E298)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
52% identity, 92% coverage: 13:455/484 of query aligns to 2:438/439 of 4mv3A
- active site: K116 (= K126), K159 (= K168), D190 (≠ G205), H203 (= H218), R229 (= R244), T268 (= T283), E270 (= E285), E282 (= E298), N284 (= N300), R286 (= R302), E290 (= E306), R332 (= R348)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K168), M163 (= M178), E195 (= E210), Y197 (= Y212), L198 (≠ V213), E270 (= E285), L272 (= L287), E282 (= E298)
- binding bicarbonate ion: R286 (= R302), Q288 (= Q304), V289 (= V305)
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)
52% identity, 92% coverage: 13:455/484 of query aligns to 2:439/440 of 6oi8A
- active site: K116 (= K126), K159 (= K168), D191 (≠ G205), H204 (= H218), R230 (= R244), T269 (= T283), E271 (= E285), E283 (= E298), N285 (= N300), R287 (= R302), E291 (= E306), 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 (= I166), K159 (= K168), M164 (= M178), E196 (= E210), Y198 (= Y212), L199 (≠ V213), H204 (= H218), Q228 (= Q242), E271 (= E285), L273 (= L287), E283 (= E298), I432 (≠ T448)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
51% identity, 92% coverage: 13:455/484 of query aligns to 2:444/447 of 2vqdA
- active site: K116 (= K126), K159 (= K168), P196 (≠ G205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K126), I157 (= I166), K159 (= K168), G164 (= G173), G166 (= G175), F203 (≠ Y212), L204 (≠ V213), H209 (= H218), Q233 (= Q242), H236 (= H245), L278 (= L287), E288 (= E298), I437 (≠ T448)
- binding magnesium ion: E276 (= E285), E288 (= E298)
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
49% identity, 93% coverage: 13:461/484 of query aligns to 2:451/1137 of 3bg5A
- active site: K117 (= K126), K159 (= K168), S189 (≠ G205), H202 (= H218), R228 (= R244), T267 (= T283), E269 (= E285), E281 (= E298), N283 (= N300), R285 (= R302), E289 (= E306), R337 (= R348)
- binding adenosine-5'-triphosphate: K117 (= K126), M157 (≠ I166), K159 (= K168), Y196 (= Y212), I197 (≠ V213), H202 (= H218), Q226 (= Q242), H229 (= H245), E269 (= E285), L271 (= L287), E281 (= E298), N283 (= N300)
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
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
53% identity, 92% coverage: 13:455/484 of query aligns to 2:444/445 of 6ojhA
- active site: K116 (= K126), K159 (= K168), D196 (≠ G205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding calcium ion: E276 (= E285), E288 (= E298), N290 (= N300)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K168), M169 (= M178), E201 (= E210), Y203 (= Y212), L204 (≠ V213), H236 (= H245), L278 (= L287), E288 (= E298), I437 (≠ T448)
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)
53% identity, 92% coverage: 13:455/484 of query aligns to 2:444/448 of P43873
- K116 (= K126) binding ATP
- K159 (= K168) binding ATP
- EKYL 201:204 (≠ EKYV 210:213) binding ATP
- E276 (= E285) binding ATP; binding Mg(2+)
- E288 (= E298) binding ATP; binding Mg(2+)
- N290 (= N300) binding Mg(2+)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
51% identity, 92% coverage: 13:455/484 of query aligns to 2:430/430 of 4mv1A
- active site: K116 (= K126), K159 (= K168), D182 (≠ K199), H195 (= H218), R221 (= R244), T260 (= T283), E262 (= E285), E274 (= E298), N276 (= N300), R278 (= R302), E282 (= E306), R324 (= R348)
- binding adenosine-5'-diphosphate: K159 (= K168), E187 (= E210), K188 (= K211), Y189 (= Y212), L190 (≠ V213), L264 (= L287)
- binding phosphate ion: K224 (= K247), R278 (= R302), Q280 (= Q304), V281 (= V305), E282 (= E306)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 92% coverage: 13:455/484 of query aligns to 2:442/444 of 2vr1A
- active site: K116 (= K126), K159 (= K168), D194 (≠ G205), H207 (= H218), R233 (= R244), T272 (= T283), E274 (= E285), E286 (= E298), N288 (= N300), R290 (= R302), E294 (= E306), R336 (= R348)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K168), R165 (= R176), M167 (= M178), Y201 (= Y212), L202 (≠ V213), E274 (= E285), L276 (= L287), E286 (= E298), N288 (= N300), I435 (≠ T448)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
49% identity, 93% coverage: 11:460/484 of query aligns to 35:490/1178 of Q05920
- K35 (= K11) modified: N6-acetyllysine
- K39 (= K15) modified: N6-acetyllysine
- K79 (= K55) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L122) modified: N6-acetyllysine
- K152 (= K126) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N215) modified: N6-acetyllysine
- K434 (≠ L404) modified: N6-acetyllysine
Sites not aligning to the query:
- 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
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
48% identity, 93% coverage: 13:461/484 of query aligns to 2:447/1133 of 3hb9A
- active site: K117 (= K126), K159 (= K168), H198 (= H218), R224 (= R244), T263 (= T283), E265 (= E285), E277 (= E298), N279 (= N300), R281 (= R302), E285 (= E306), R333 (= R348)
- binding adenosine-5'-diphosphate: K117 (= K126), M157 (≠ I166), Y192 (= Y212), I193 (≠ V213), H198 (= H218), Q222 (= Q242), H225 (= H245), L267 (= L287), I276 (= I297), E277 (= E298)
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
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
49% identity, 93% coverage: 11:460/484 of query aligns to 35:490/1178 of P11498
- V145 (≠ H119) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (≠ K130) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R244) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y278) to C: in PC deficiency
- R451 (≠ I421) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
Sites not aligning to the query:
- 572 binding Mn(2+)
- 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 Mn(2+)
- 773 binding Mn(2+)
- 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)
49% identity, 93% coverage: 11:460/484 of query aligns to 4:459/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ I29), T26 (≠ K33), R46 (≠ V53), Q47 (≠ K54), K48 (= K55), A49 (= A56), D50 (= D57), R367 (≠ H369), R414 (= R415), E418 (= E419), R420 (≠ I421), R422 (= R423)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K168), G168 (= G173), G169 (= G174), M173 (= M178), F207 (≠ Y212), I208 (≠ V213), P211 (= P216), H240 (= H245)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
49% identity, 93% coverage: 11:460/484 of query aligns to 3:458/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K168), G167 (= G173), G168 (= G174), F206 (≠ Y212), Q236 (= Q242), H239 (= H245), E292 (= E298)
- binding coenzyme a: F21 (≠ I29), R22 (= R30), T25 (≠ K33), R45 (≠ V53), Q46 (≠ K54), K47 (= K55), A48 (= A56), D49 (= D57), E50 (= E58), R366 (≠ H369), R413 (= R415), A416 (≠ D418), R419 (≠ I421)
Sites not aligning to the query:
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
48% identity, 93% coverage: 13:460/484 of query aligns to 2:455/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ K33), F43 (≠ K54), K44 (= K55), A45 (= A56), D46 (= D57), S48 (≠ A59), R363 (≠ H369), H413 (≠ D418), E414 (= E419), R416 (≠ I421), R418 (= R423)
- binding adenosine-5'-triphosphate: K117 (= K126), M156 (≠ I166), K158 (= K168), G163 (= G173), G164 (= G174), G165 (= G175), M168 (= M178), E200 (= E210), Y202 (= Y212), I203 (≠ V213), H208 (= H218), Q232 (= Q242), N235 (≠ H245), L277 (= L287), E287 (= E298), N289 (= N300), T443 (= T448)
- binding bicarbonate ion: K237 (= K247), R291 (= R302), Q293 (= Q304), E295 (= E306)
- binding biotin: G84 (= G93), V294 (= V305), R342 (= R348)
- binding magnesium ion: E275 (= E285), E287 (= E298)
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
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
48% identity, 92% coverage: 14:459/484 of query aligns to 3:445/456 of 8hz4A
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
50% identity, 92% coverage: 13:455/484 of query aligns to 2:444/444 of 3rupA
- active site: K116 (= K126), K159 (= K168), D196 (≠ G205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding adenosine-5'-diphosphate: Y82 (= Y92), G83 (= G93), K116 (= K126), K159 (= K168), G164 (= G173), G164 (= G173), G165 (= G174), G166 (= G175), R167 (= R176), M169 (= M178), F193 (= F202), E201 (= E210), K202 (= K211), Y203 (= Y212), L204 (≠ V213), H209 (= H218), Q233 (= Q242), H236 (= H245), K238 (= K247), L278 (= L287), E288 (= E298), R292 (= R302), V295 (= V305), E296 (= E306), R338 (= R348), D382 (= D393), I437 (≠ T448)
- binding calcium ion: E87 (= E97), E276 (= E285), E288 (= E298), E288 (= E298), N290 (= N300)
Query Sequence
>WP_037919564.1 NCBI__GCF_000619805.1:WP_037919564.1
MSKVKTFTFTKDIKKVLVANRGEIATRIIRACKELGIKTVAIYSEADAKSIYVKKADEAY
LIPGDPIQAYLNYFRIVDLAKQTKCDAIHPGYGFLSENPEFAEYCWKQGIISIGPHPDHI
ALFGDKMAAKKKMRELGVPVLPGSDEPISDIKKAKKIADEIGYPVILKAAFGGGGRGMRI
VREESEFEDLFKSAFNEAKKFFGRGDVFIEKYVENPRHIEIQIMADKYGNVVHLGERDCS
IQRRHQKVVEIARSPTLNEDVKKELYRTSVKAMFKVGYENVGTIEYLVDEKDNFYFIEMN
TRLQVEHTVTEMVTGVDIVQQMIKIAQGEKLGFLQEDISMRGYAIEFRVNAEDPKRNFAP
SVGAITSYHSPGGPGVRVDAAVYKDYVIPPYYDSMIAKLSVWALTWDQVVNRARRALDEF
IVRGVPTNLPLLRAIVRDEDFIKGKFTTRYIEEKLPTFNLEDKTANLEDLVAAIAGAIAA
YHKI
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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