SitesBLAST
Comparing WP_027457190.1 NCBI__GCF_000519045.1:WP_027457190.1 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)
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)
57% identity, 100% coverage: 1:667/667 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F349) binding biotin
- W515 (= W498) mutation to L: No effect on holoenzyme formation.
- L599 (= L585) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L588) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M589) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K633) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
56% identity, 100% coverage: 2:667/667 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 (= E289), N275 (= N291), R277 (= R293), E281 (= E297), R323 (= R339), G519 (= G540)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M632), K612 (= K633)
7ybuA Human propionyl-coenzyme a carboxylase (see paper)
50% identity, 100% coverage: 2:667/667 of query aligns to 5:670/670 of 7ybuA
8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
50% identity, 100% coverage: 2:667/667 of query aligns to 3:668/668 of 8xl5A
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)
50% identity, 100% coverage: 2:667/667 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; dbSNP:rs2063109875
- D368 (= D308) to G: in PA-1
- M373 (= M313) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G319) to V: in PA-1; dbSNP:rs794727087
- C398 (= C338) to R: in PA-1
- R399 (= R339) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P362) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ V472) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (≠ Q497) to L: in PA-1; dbSNP:rs118169528
- G631 (= G570) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G607) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K633) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A651) 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)
47% identity, 99% coverage: 5:667/667 of query aligns to 1:657/657 of 8sgxX
8xl6A Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
42% identity, 100% coverage: 4:667/667 of query aligns to 3:660/660 of 8xl6A
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
54% identity, 70% coverage: 203:667/667 of query aligns to 133:591/591 of 3n6rA