SitesBLAST
Comparing GFF3328 PS417_17030 3-methylcrotonyl-CoA carboxylase 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 96% coverage: 4:620/641 of query aligns to 2:636/654 of P9WPQ3
- K322 (≠ A322) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
42% identity, 99% coverage: 3:638/641 of query aligns to 4:670/670 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)
41% identity, 99% coverage: 3:638/641 of query aligns to 62:728/728 of P05165
- A75 (= A16) to P: in PA-1; dbSNP:rs794727479
- R77 (= R18) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A79) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ L105) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G138) to E: in PA-1
- M229 (= M170) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q238) to R: in PA-1
- D368 (= D309) to G: in PA-1
- M373 (≠ Q314) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G320) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V339) to R: in PA-1
- R399 (= R340) to Q: in PA-1; dbSNP:rs1301904623
- P423 (≠ S363) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L458) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W481) to L: in PA-1; dbSNP:rs118169528
- G631 (= G548) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G578) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K604) modified: N6-biotinyllysine; by HLCS
- C712 (= C622) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
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)
42% identity, 99% coverage: 4:638/641 of query aligns to 2:681/681 of Q5LUF3
- F348 (= F350) binding
- W515 (≠ F470) mutation to L: No effect on holoenzyme formation.
- L599 (≠ G552) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L555) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ F556) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K604) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
41% identity, 99% coverage: 4:638/641 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K118), K157 (= K160), D180 (≠ G197), H193 (= H210), R219 (= R236), T258 (= T275), E260 (= E277), E273 (= E290), N275 (= N292), R277 (= R294), E281 (= E298), R323 (= R340), G519 (≠ Q504)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M603), K612 (= K604)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
40% identity, 99% coverage: 7:638/641 of query aligns to 1:657/657 of 8sgxX
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:428/444 of 2vr1A
- active site: K116 (= K118), K159 (= K160), D194 (≠ G197), H207 (= H210), R233 (= R236), T272 (= T275), E274 (= E277), E286 (= E290), N288 (= N292), R290 (= R294), E294 (= E298), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K160), R165 (≠ K168), M167 (= M170), Y201 (= Y204), L202 (= L205), E274 (= E277), L276 (= L279), E286 (= E290), N288 (= N292)
Sites not aligning to the query:
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
52% identity, 70% coverage: 4:449/641 of query aligns to 2:442/456 of 8hz4A
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/449 of P24182
- R19 (= R21) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ A25) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K118) binding
- K159 (= K160) binding
- GG 165:166 (= GG 166:167) binding
- EKYL 201:204 (= EKYL 202:205) binding
- H209 (= H210) binding
- H236 (= H237) binding
- K238 (= K239) binding
- E276 (= E277) binding ; binding
- E288 (= E290) binding ; binding
- R292 (= R294) active site; binding
- V295 (= V297) binding
- E296 (= E298) mutation to A: Severe reduction in catalytic activity.
- R338 (= R340) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (vs. gap) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R370) mutation to E: Loss of homodimerization. No effect on ATP binding.
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/444 of 3rupA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding adenosine-5'-diphosphate: Y82 (= Y84), G83 (= G85), K116 (= K118), K159 (= K160), G164 (= G165), G164 (= G165), G165 (= G166), G166 (= G167), R167 (≠ K168), M169 (= M170), F193 (= F194), E201 (= E202), K202 (= K203), Y203 (= Y204), L204 (= L205), H209 (= H210), Q233 (= Q234), H236 (= H237), K238 (= K239), L278 (= L279), E288 (= E290), R292 (= R294), V295 (= V297), E296 (= E298), R338 (= R340), D382 (= D386)
- binding calcium ion: E87 (= E89), E276 (= E277), E288 (= E290), E288 (= E290), N290 (= N292)
Sites not aligning to the query:
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/444 of 3g8cA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding adenosine-5'-diphosphate: I157 (≠ L158), K159 (= K160), G164 (= G165), M169 (= M170), E201 (= E202), K202 (= K203), Y203 (= Y204), L204 (= L205), Q233 (= Q234), H236 (= H237), L278 (= L279), E288 (= E290)
- binding bicarbonate ion: K238 (= K239), R292 (= R294), Q294 (= Q296), V295 (= V297), E296 (= E298)
- binding biotin: Y82 (= Y84), F84 (= F86), R292 (= R294), V295 (= V297), R338 (= R340), D382 (= D386)
- binding magnesium ion: E276 (= E277), E288 (= E290)
Sites not aligning to the query:
6oi9A Crystal structure of e. Coli biotin carboxylase complexed with 7-[3- (aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3- d]pyrimidin-2-amine (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 6oi9A
- active site: E276 (= E277), E288 (= E290), N290 (= N292), E296 (= E298), R338 (= R340)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K160), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (= L205), H209 (= H210), Q233 (= Q234), H236 (= H237), E276 (= E277), L278 (= L279), E288 (= E290)
Sites not aligning to the query:
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2w71A
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K160), Y203 (= Y204), L204 (= L205), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2w70A
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ L158), K159 (= K160), G166 (= G167), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (= L205), L278 (= L279)
2w6zA Crystal structure of biotin carboxylase from e. Coli in complex with the 3-(3-methyl-but-2-enyl)-3h-purin-6-ylamine fragment (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2w6zA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K160), Y203 (= Y204), L204 (= L205), L278 (= L279)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2w6qA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (≠ L158), K159 (= K160), E201 (= E202), K202 (= K203), Y203 (= Y204), L204 (= L205), H236 (= H237), L278 (= L279)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2w6pA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K160), Y203 (= Y204), L204 (= L205), Q233 (= Q234), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2w6mA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (≠ L158), K159 (= K160), M169 (= M170), E201 (= E202), K202 (= K203), Y203 (= Y204), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
2v5aA Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 3 (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2v5aA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine: I157 (≠ L158), K159 (= K160), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (= L205), Q233 (= Q234), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
2v58A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 1 (see paper)
52% identity, 67% coverage: 4:434/641 of query aligns to 2:430/446 of 2v58A
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: I157 (≠ L158), K159 (= K160), E201 (= E202), Y203 (= Y204), L204 (= L205), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
Query Sequence
>GFF3328 PS417_17030 3-methylcrotonyl-CoA carboxylase
MSTLTTLLVANRGEIACRVMRTAKAMGLTTVAVHSAIDRDARHSREADIRVDLGGSKATD
SYLQIDKLIAAAQASGAQAIHPGYGFLSENAGFARAIEAAGLIFLGPPASAIDAMGSKSA
AKALMETAGVPLVPGYHGEAQDLETFRAACERIGYPVLLKATAGGGGKGMKVVEDVSQLA
EALASAQREALSSFGNGQMLVEKYLLKPRHVEIQVFADQHGHCLYLNERDCSIQRRHQKV
VEEAPAPGLSGEQRKAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHP
VTEAITGLDLVAWQIRVAQGEALPITQEQVPLTGHAIEVRLYAEDPTNDFLPATGRLALY
RESAPGPGRRVDSGVEQGDSVSPFYDPMLGKLIAWGEDREQAQLRLLAMLDEFAIGGLKT
NLGFLRRIIGHPAFAAAELDTGFIPRYQEELLPAPGDLSDEFWQAAGSAFIQSLPPEDGP
WGDKRGFRAGLPAEVSLHLSCTGQDRLVTLAADAPPLRGEQLLIERQGVRRSHLAVRSEG
SVFLRWDGEMHGVTLFDPIAAVEANQSHQGGLTAPMNGSIVRVLVEVGQHVDAGTQLVVL
EAMKMEHSIRAPQAGVVKALFCQEGEMVAEGCALVELEPAG
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