SitesBLAST
Comparing Ac3H11_3016 FitnessBrowser__acidovorax_3H11:Ac3H11_3016 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)
49% identity, 99% coverage: 2:669/675 of query aligns to 4:620/621 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)
45% identity, 98% coverage: 1:660/675 of query aligns to 1:643/654 of P9WPQ3
- K322 (≠ P328) 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)
43% identity, 98% coverage: 1:660/675 of query aligns to 1:671/681 of Q5LUF3
- F348 (= F356) binding
- W515 (≠ G503) mutation to L: No effect on holoenzyme formation.
- L599 (vs. gap) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ I585) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ T586) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K636) modified: N6-biotinyllysine
7ybuA Propionyl-CoA carboxylase beta chain, mitochondrial
42% identity, 99% coverage: 2:669/675 of query aligns to 5:669/670 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)
42% identity, 99% coverage: 2:669/675 of query aligns to 63:727/728 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 (= D315) to G: in PA-1
- M373 (≠ Q320) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G326) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A345) to R: in PA-1
- R399 (= R346) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P369) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ A475) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (vs. gap) to L: in PA-1; dbSNP:rs118169528
- G631 (= G560) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G610) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K636) modified: N6-biotinyllysine; by HLCS
- C712 (≠ Y654) 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)
42% identity, 98% coverage: 2:660/675 of query aligns to 1:636/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E296), N275 (= N298), R277 (= R300), E281 (= E304), R323 (= R346), G519 (= G543)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M635), K612 (= K636)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
41% identity, 99% coverage: 5:669/675 of query aligns to 1:656/657 of 8sgxX