SitesBLAST
Comparing Ac3H11_2275 FitnessBrowser__acidovorax_3H11:Ac3H11_2275 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)
Q5LUF3 Propionyl-CoA carboxylase alpha chain; EC 6.4.1.3 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
59% identity, 100% coverage: 1:682/682 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F348) binding
- W515 (≠ F505) mutation to L: No effect on holoenzyme formation.
- L599 (= L600) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L603) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M604) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K648) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
57% identity, 100% coverage: 2:682/682 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R338), G519 (= G551)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M647), K612 (= K648)
7ybuA Human propionyl-coenzyme a carboxylase
49% identity, 100% coverage: 2:682/682 of query aligns to 5:670/670 of 7ybuA
P05165 Propionyl-CoA carboxylase alpha chain, mitochondrial; PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.3 from Homo sapiens (Human) (see 6 papers)
49% identity, 100% coverage: 2:682/682 of query aligns to 63:728/728 of P05165
- A75 (= A14) to P: in PA-1; dbSNP:rs794727479
- R77 (= R16) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A77) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I103) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ D136) to E: in PA-1
- M229 (≠ L168) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q236) to R: in PA-1
- D368 (= D307) to G: in PA-1
- M373 (= M312) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G318) to V: in PA-1; dbSNP:rs794727087
- C398 (= C337) to R: in PA-1
- R399 (= R338) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P361) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ M479) natural variant: Missing (in PA-1)
- V551 (≠ K500) to F: in dbSNP:rs61749895
- W559 (≠ V508) to L: in PA-1; dbSNP:rs118169528
- G631 (= G585) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G622) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K648) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A666) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
46% identity, 99% coverage: 5:682/682 of query aligns to 1:657/657 of 8sgxX
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
46% identity, 100% coverage: 2:682/682 of query aligns to 1:591/591 of 3n6rA
- active site: K115 (= K175), H138 (= H208), R164 (= R234), T203 (= T273), E205 (= E275), E218 (= E288), N220 (= N290), R222 (= R292), E226 (= E296), R268 (= R338), G464 (= G551)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M647), K557 (= K648)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
42% identity, 99% coverage: 1:678/682 of query aligns to 1:649/654 of P9WPQ3
- K322 (= K320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
50% identity, 66% coverage: 4:454/682 of query aligns to 2:443/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R338)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ L168), F200 (= F202), I201 (≠ V203), E273 (= E275), I275 (≠ V277), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E275), E287 (= E288)
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)
48% identity, 67% coverage: 1:454/682 of query aligns to 3:445/453 of 7kctA
- active site: E276 (= E275), E289 (= E288), N291 (= N290), E297 (= E296), R339 (= R338)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (≠ M156), K159 (= K158), G164 (= G163), G165 (= G164), G166 (= G165), I169 (≠ L168), E201 (= E200), Y203 (≠ F202), I204 (≠ V203), H209 (= H208), Q233 (= Q232), Q237 (= Q236), K238 (= K237), I278 (≠ V277), E289 (= E288), R293 (= R292), Q295 (= Q294), V296 (= V295), E297 (= E296), R339 (= R338)
- binding bicarbonate ion: D116 (= D115), R119 (≠ A118)
- binding magnesium ion: E276 (= E275), E289 (= E288)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
47% identity, 67% coverage: 1:456/682 of query aligns to 1:443/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R338)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (≠ L168), Y201 (≠ F202), L202 (≠ V203), E274 (= E275), L276 (≠ V277), E286 (= E288), N288 (= N290), I435 (≠ T448)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
47% identity, 67% coverage: 1:456/682 of query aligns to 1:442/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (≠ L168), E198 (= E200), Y200 (≠ F202), L201 (≠ V203), H233 (= H235), L275 (≠ V277), E285 (= E288)
- binding magnesium ion: E273 (= E275), E285 (= E288)
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)
47% identity, 67% coverage: 1:456/682 of query aligns to 1:440/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E288), N285 (= N290), R287 (= R292), E291 (= E296), R333 (= R338)
- 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 (≠ M156), K159 (= K158), M164 (≠ L168), E196 (= E200), Y198 (≠ F202), L199 (≠ V203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (≠ V277), E283 (= E288), I432 (≠ T448)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
47% identity, 67% coverage: 1:456/682 of query aligns to 1:439/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E288), N284 (= N290), R286 (= R292), E290 (= E296), R332 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (≠ L168), E195 (= E200), Y197 (≠ F202), L198 (≠ V203), E270 (= E275), L272 (≠ V277), E282 (= E288)
- binding bicarbonate ion: R286 (= R292), Q288 (= Q294), V289 (= V295)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 67% coverage: 1:456/682 of query aligns to 1:445/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (= F202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ V277), E288 (= E288), I437 (≠ T448)
- binding magnesium ion: E276 (= E275), E288 (= E288)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
48% identity, 66% coverage: 5:454/682 of query aligns to 9:446/446 of 3ouuA
- active site: K162 (= K158), G168 (= G164), G169 (= G165), H212 (= H208), K241 (= K237), T277 (= T273), E279 (= E275), E292 (= E288), N294 (= N290), V299 (= V295), E300 (= E296), R341 (= R338)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K116), I160 (≠ M156), K162 (= K158), G167 (= G163), G168 (= G164), G169 (= G165), M172 (≠ L168), E204 (= E200), Y206 (≠ F202), I207 (≠ V203), H212 (= H208), Q236 (= Q232), H239 (= H235), L281 (≠ V277), E292 (= E288), T440 (= T448)
- binding calcium ion: E279 (= E275), E292 (= E288)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
48% identity, 66% coverage: 5:454/682 of query aligns to 8:445/445 of 3ouzA
- active site: K161 (= K158), G167 (= G164), G168 (= G165), H211 (= H208), K240 (= K237), T276 (= T273), E278 (= E275), E291 (= E288), N293 (= N290), V298 (= V295), E299 (= E296), R340 (= R338)
- binding adenosine-5'-diphosphate: K119 (= K116), I159 (≠ M156), K161 (= K158), G166 (= G163), G168 (= G165), M171 (≠ L168), E203 (= E200), Y205 (≠ F202), I206 (≠ V203), H211 (= H208), Q235 (= Q232), L280 (≠ V277), E291 (= E288), T439 (= T448)
- binding magnesium ion: E278 (= E275), E291 (= E288)
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)
48% identity, 67% coverage: 1:456/682 of query aligns to 1:445/448 of P43873
- K116 (= K116) binding
- K159 (= K158) binding
- EKYL 201:204 (≠ EKFV 200:203) binding
- E276 (= E275) binding ; binding
- E288 (= E288) binding ; binding
- N290 (= N290) 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
48% identity, 67% coverage: 1:456/682 of query aligns to 1:445/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding calcium ion: E276 (= E275), E288 (= E288), N290 (= N290)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (≠ L168), E201 (= E200), Y203 (≠ F202), L204 (≠ V203), H236 (= H235), L278 (≠ V277), E288 (= E288), I437 (≠ T448)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
48% identity, 67% coverage: 1:456/682 of query aligns to 1:445/449 of P24182
- R19 (≠ A19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ K23) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K116) binding
- K159 (= K158) binding
- GG 165:166 (= GG 164:165) binding
- EKYL 201:204 (≠ EKFV 200:203) binding
- H209 (= H208) binding
- H236 (= H235) binding
- K238 (= K237) binding
- E276 (= E275) binding ; binding
- E288 (= E288) binding ; binding
- R292 (= R292) active site; binding
- V295 (= V295) binding
- E296 (= E296) mutation to A: Severe reduction in catalytic activity.
- R338 (= R338) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ L374) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R377) mutation to E: Loss of homodimerization. No effect on ATP binding.
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
48% identity, 67% coverage: 1:456/682 of query aligns to 1:445/445 of 3jziA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K158), A160 (= A159), G164 (= G163), G165 (= G164), M169 (≠ L168), Y199 (≠ F198), E201 (= E200), K202 (= K201), Y203 (≠ F202), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ V277), I287 (≠ L287), E288 (= E288)
Query Sequence
>Ac3H11_2275 FitnessBrowser__acidovorax_3H11:Ac3H11_2275
MFTKILIANRGEIACRVIATARKMGIATVAVYSDADKEARHVKLADEAVHIGAAPSRESY
LLADKIIAACKQTGAQAVHPGYGFLSENEAFAKRCEDEGIAFIGPKAHSIAAMGDKIASK
KLANEAKVNTIPGYNDAIAGPEQAVEIAKGIGYPVMIKASAGGGGKGLRVAFNDKEAFEG
FASCQNEARNSFGDDRIFIEKFVQEPRHIEIQVLGDSHGNVIYLNERECSIQRRHQKVIE
EAPSPFISDATRKAMGEQAVQLAKAVKYQSAGTVEFVVGKDQDFYFLEMNTRLQVEHPVT
ECITGLDLVELMIRVAAGEKLPLTQADVKRDGWAIECRINAEDPFRNFLPSTGRLVRFQP
PEETMFQSDTTKKLGVRVDTGVYEGGEIPMYYDSMIAKLIVHGTDRNDAIAKMRAALNGF
VIRGISSNIPFQAALLAHPKFVTGDFNTGFIAENYGKGFHAEDVPHSDPMFLVALAAFMH
RRYRARASGISGQLAGHEVKVGEEFVVVTLGAEGQNQHHAVTVSDFEDKSGSSAIQVGDS
SYQISSNATLGQIRVQGACNGQGFTAQVERGVGKNPLALRIAHNGTQIDTLVLSPLGAKL
HKLMPFKAPPDLSKFLLSPMPGLLVDVAVQPGQKVQAGEKLAVIEAMKMENILFAAQDGV
VGKITAGKGESLAVDQIILEFQ
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