SitesBLAST
Comparing WP_058930563.1 NCBI__GCF_001484605.1:WP_058930563.1 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)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
53% identity, 73% coverage: 1:431/591 of query aligns to 2:429/456 of 8hz4A
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 73% coverage: 1:429/591 of query aligns to 2:427/442 of 4mv4A
- active site: K116 (= K115), K159 (= K157), D193 (≠ G194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (≠ R165), M166 (≠ L167), E198 (= E199), Y200 (= Y201), L201 (= L202), H233 (= H234), L275 (= L276), E285 (= E287)
- binding magnesium ion: E273 (= E274), E285 (= E287)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
49% identity, 73% coverage: 1:429/591 of query aligns to 2:424/439 of 4mv3A
- active site: K116 (= K115), K159 (= K157), D190 (≠ G194), H203 (= H207), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E287), N284 (= N289), R286 (= R291), E290 (= E295), R332 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (≠ L167), E195 (= E199), Y197 (= Y201), L198 (= L202), E270 (= E274), L272 (= L276), E282 (= E287)
- binding bicarbonate ion: R286 (= R291), Q288 (= Q293), V289 (= V294)
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)
49% identity, 73% coverage: 1:429/591 of query aligns to 2:425/440 of 6oi8A
- active site: K116 (= K115), K159 (= K157), D191 (≠ G194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E287), N285 (= N289), R287 (= R291), E291 (= E295), R333 (= R336)
- 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 (≠ A155), K159 (= K157), M164 (≠ L167), E196 (= E199), Y198 (= Y201), L199 (= L202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (= L276), E283 (= E287)
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, 79% coverage: 1:465/591 of query aligns to 37:496/1178 of Q05920
- K39 (= K3) modified: N6-acetyllysine
- K79 (≠ A43) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ Q111) modified: N6-acetyllysine
- K152 (= K115) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ R204) modified: N6-acetyllysine
- K434 (≠ A392) 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
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
50% identity, 73% coverage: 1:429/591 of query aligns to 2:430/445 of 6ojhA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R336)
- binding calcium ion: E276 (= E274), E288 (= E287), N290 (= N289)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K157), M169 (≠ L167), E201 (= E199), Y203 (= Y201), L204 (= L202), H236 (= H234), L278 (= L276), E288 (= E287)
Sites not aligning to the query:
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)
50% identity, 73% coverage: 1:429/591 of query aligns to 2:430/448 of P43873
- K116 (= K115) binding ATP
- K159 (= K157) binding ATP
- EKYL 201:204 (≠ ERYL 199:202) binding ATP
- E276 (= E274) binding ATP; binding Mg(2+)
- E288 (= E287) binding ATP; binding Mg(2+)
- N290 (= N289) binding Mg(2+)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
48% identity, 73% coverage: 1:429/591 of query aligns to 2:416/430 of 4mv1A
- active site: K116 (= K115), K159 (= K157), D182 (≠ E186), H195 (= H207), R221 (= R233), T260 (= T272), E262 (= E274), E274 (= E287), N276 (= N289), R278 (= R291), E282 (= E295), R324 (= R336)
- binding adenosine-5'-diphosphate: K159 (= K157), E187 (= E199), K188 (≠ R200), Y189 (= Y201), L190 (= L202), L264 (= L276)
- binding phosphate ion: K224 (= K236), R278 (= R291), Q280 (= Q293), V281 (= V294), E282 (= E295)
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
45% identity, 79% coverage: 1:465/591 of query aligns to 37:496/1178 of P11498
- V145 (≠ A108) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R119) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R233) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y267) to C: in PC deficiency
- R451 (≠ E409) 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)
45% identity, 79% coverage: 1:465/591 of query aligns to 6:465/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A17), T26 (≠ E21), R46 (≠ V41), Q47 (≠ G42), K48 (≠ A43), A49 (= A44), D50 (≠ T45), R367 (≠ S357), R414 (= R403), E418 (= E407), R420 (≠ E409), R422 (≠ T411), A462 (≠ D462), Q463 (≠ G463), R465 (= R465)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K157), G168 (= G162), G169 (= G163), M173 (≠ L167), F207 (≠ Y201), I208 (≠ L202), P211 (= P205), H240 (= H234)
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, 79% coverage: 1:465/591 of query aligns to 5:464/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K157), G167 (= G162), G168 (= G163), F206 (≠ Y201), Q236 (= Q231), H239 (= H234), E292 (= E287)
- binding coenzyme a: F21 (≠ A17), R22 (= R18), T25 (≠ E21), R45 (≠ V41), Q46 (≠ G42), K47 (≠ A43), A48 (= A44), D49 (≠ T45), E50 (= E46), R366 (≠ S357), R413 (= R403), A416 (= A406), R419 (≠ E409), Q462 (≠ G463), R464 (= R465)
Sites not aligning to the query:
4rzqA Structural analysis of substrate, reaction intermediate and product binding in haemophilus influenzae biotin carboxylase (see paper)
48% identity, 73% coverage: 1:429/591 of query aligns to 3:406/422 of 4rzqA
- active site: K117 (= K115), K155 (= K157), H185 (= H207), R211 (= R233), T250 (= T272), E252 (= E274), E264 (= E287), N266 (= N289), R268 (= R291), E272 (= E295), R314 (= R336)
- binding adenosine-5'-diphosphate: Y179 (= Y201), L180 (= L202), L254 (= L276)
- binding methyl (3aS,4S,6aR)-4-(5-methoxy-5-oxopentyl)-2-oxohexahydro-1H-thieno[3,4-d]imidazole-1-carboxylate: N10 (= N8), R11 (= R9), Y83 (= Y81), F85 (= F83), K214 (= K236), R268 (= R291), Q270 (= Q293), V271 (= V294), E272 (= E295), R314 (= R336), D358 (= D381)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
43% identity, 73% coverage: 2:431/591 of query aligns to 1:432/448 of 2vpqB
- active site: V116 (≠ T117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E287), N289 (= N289), R291 (= R291), E295 (= E295), R337 (= R336)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ A155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ L167), F200 (≠ Y201), I201 (≠ L202), E273 (= E274), I275 (≠ L276), M286 (≠ L286), E287 (= E287)
- binding magnesium ion: E273 (= E274), E287 (= E287)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 75% coverage: 1:446/591 of query aligns to 2:444/447 of 2vqdA
- active site: K116 (= K115), K159 (= K157), P196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R336)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K115), I157 (≠ A155), K159 (= K157), G164 (= G162), G166 (= G164), F203 (≠ Y201), L204 (= L202), H209 (= H207), Q233 (= Q231), H236 (= H234), L278 (= L276), E288 (= E287), I437 (≠ T439)
- binding magnesium ion: E276 (= E274), E288 (= E287)
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)
46% identity, 73% coverage: 1:429/591 of query aligns to 4:432/453 of 7kctA
- active site: E276 (= E274), E289 (= E287), N291 (= N289), E297 (= E295), R339 (= R336)
- binding adenosine-5'-diphosphate: K117 (= K115), L157 (≠ A155), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), I169 (≠ L167), E201 (= E199), Y203 (= Y201), I204 (≠ L202), H209 (= H207), Q233 (= Q231), Q237 (= Q235), K238 (= K236), I278 (≠ L276), E289 (= E287), R293 (= R291), Q295 (= Q293), V296 (= V294), E297 (= E295), R339 (= R336)
- binding bicarbonate ion: D116 (≠ N114), R119 (≠ T117)
- binding magnesium ion: E276 (= E274), E289 (= E287)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
42% identity, 82% coverage: 1:482/591 of query aligns to 4:482/1150 of A0A0H3JRU9
- R21 (= R18) mutation to A: Complete loss of catalytic activity.
- K119 (= K115) binding ATP
- K161 (= K157) binding ATP
- H211 (= H207) binding ATP
- E278 (= E274) binding ATP
- K411 (≠ R400) 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.
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
46% identity, 73% coverage: 1:429/591 of query aligns to 2:428/444 of 2vr1A
- active site: K116 (= K115), K159 (= K157), D194 (≠ G194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E287), N288 (= N289), R290 (= R291), E294 (= E295), R336 (= R336)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (= R165), M167 (≠ L167), Y201 (= Y201), L202 (= L202), E274 (= E274), L276 (= L276), E286 (= E287), N288 (= N289)
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)
48% identity, 71% coverage: 4:421/591 of query aligns to 5:425/654 of P9WPQ3
- K322 (≠ P319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
46% identity, 73% coverage: 1:429/591 of query aligns to 2:430/445 of 3jziA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R336)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K115), K159 (= K157), A160 (= A158), G164 (= G162), G165 (= G163), M169 (≠ L167), Y199 (≠ F197), E201 (= E199), K202 (≠ R200), Y203 (= Y201), H209 (= H207), Q233 (= Q231), H236 (= H234), L278 (= L276), I287 (≠ L286), E288 (= E287)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
46% identity, 73% coverage: 1:429/591 of query aligns to 2:430/445 of 2w6oA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R336)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K157), K202 (≠ R200), Y203 (= Y201), L204 (= L202), L278 (= L276)
Sites not aligning to the query:
Query Sequence
>WP_058930563.1 NCBI__GCF_001484605.1:WP_058930563.1
MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAATEAYSLGGNAPSETYL
DIPNLLRVAAESGADAVHPGYGFLSENAGFAQAVLDAGLTWIGPSPEAIRQLGNKITARE
IAVRAGAPLVAGTDGPVDSAAEVREFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESF
DSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE
APAPFLTEEQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITE
ETTGVDLVQEQFRIAAGEPLRFTADPTPRGHSFEFRLNAEDVGRGFLPSPGTIATFSGPT
GPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRRARRALAEMEITGVATVLPFH
RAVVQAPDFTSETALGIHTRWIETDFADSIAADPEFGTSVPDGERRTITVDVDGRRLAVG
LPADLLDGWARSGAAVPAGVSLDGAGLDGAADGGPAAGAADPGELRADMAGTVVKWLVEP
GADVSAGDAVVVLEAMKMETQVTAHRAGMLTGIRAEAGGVVNAGAVLALIG
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