SitesBLAST
Comparing WP_011383117.1 AMB_RS03465 acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha 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)
3u9sA Crystal structure of p. Aeruginosa 3-methylcrotonyl-coa carboxylase (mcc) 750 kd holoenzyme, coa complex (see paper)
53% identity, 99% coverage: 2:662/665 of query aligns to 4:621/621 of 3u9sA
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
47% identity, 98% coverage: 1:652/665 of query aligns to 1:643/654 of P9WPQ3
- K322 (= K319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
45% identity, 100% coverage: 1:662/665 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F347) binding
- W515 (= W495) mutation to L: No effect on holoenzyme formation.
- L599 (≠ A587) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (vs. gap) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (vs. gap) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K628) modified: N6-biotinyllysine
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)
43% identity, 99% coverage: 2:662/665 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 (= G136) to E: in PA-1
- M229 (= M168) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q236) to R: in PA-1
- D368 (= D306) to G: in PA-1
- M373 (≠ Q311) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G317) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A336) to R: in PA-1
- R399 (= R337) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P360) to L: in PA-1; dbSNP:rs1443858896
- L532 (vs. gap) natural variant: Missing (in PA-1)
- V551 (≠ A480) to F: in dbSNP:rs61749895
- W559 (= W495) to L: in PA-1; dbSNP:rs118169528
- G631 (= G572) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G602) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K628) modified: N6-biotinyllysine; by HLCS
- C712 (≠ F646) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
44% identity, 99% coverage: 2:662/665 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 (= E287), N275 (= N289), R277 (= R291), E281 (= E295), R323 (= R337), G519 (≠ S535)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M627), K612 (= K628)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
52% identity, 67% coverage: 1:443/665 of query aligns to 1:439/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: I157 (≠ L156), K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), K199 (≠ T201), Y200 (= Y202), L201 (= L203), H233 (= H235), L275 (= L277), E285 (= E287)
- binding magnesium ion: E273 (= E275), E285 (= E287), N287 (= N289)
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)
51% identity, 67% coverage: 1:443/665 of query aligns to 1:437/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E287), N285 (= N289), R287 (= R291), E291 (= E295), R333 (= R337)
- 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 (≠ L156), K159 (= K158), M164 (= M168), E196 (= E200), K197 (≠ T201), Y198 (= Y202), L199 (= L203), H204 (= H208), Q228 (= Q232), H231 (= H235), E271 (= E275), L273 (= L277), E283 (= E287), I432 (≠ T438), H433 (≠ G439)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
51% identity, 67% coverage: 1:443/665 of query aligns to 1:436/439 of 4mv3A