SitesBLAST
Comparing WP_090274990.1 NCBI__GCF_900105005.1:WP_090274990.1 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)
8xl6A Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
46% identity, 98% coverage: 5:634/640 of query aligns to 1:660/660 of 8xl6A
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
43% identity, 99% coverage: 5:635/640 of query aligns to 4:650/651 of 8j78I
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
44% identity, 98% coverage: 8:631/640 of query aligns to 5:659/666 of 8rthA
8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
43% identity, 98% coverage: 5:634/640 of query aligns to 3:668/668 of 8xl5A
7ybuA Human propionyl-coenzyme a carboxylase (see paper)
43% identity, 98% coverage: 5:634/640 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)
43% identity, 98% coverage: 5:634/640 of query aligns to 63:728/728 of P05165
- A75 (= A17) to P: in PA-1; dbSNP:rs794727479
- R77 (= R19) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A80) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ L106) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G139) to E: in PA-1
- M229 (= M171) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q239) to R: in PA-1; dbSNP:rs2063109875
- D368 (= D310) to G: in PA-1
- M373 (≠ Q315) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G321) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V340) to R: in PA-1
- R399 (= R341) to Q: in PA-1; dbSNP:rs1301904623
- P423 (≠ A364) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L459) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W464) to L: in PA-1; dbSNP:rs118169528
- G631 (≠ D536) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G574) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K600) modified: N6-biotinyllysine; by HLCS
- C712 (= C618) 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)
41% identity, 98% coverage: 8:634/640 of query aligns to 1:657/657 of 8sgxX
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
54% identity, 71% coverage: 5:456/640 of query aligns to 2:455/654 of P9WPQ3
- K322 (≠ P323) 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)
51% identity, 69% coverage: 5:445/640 of query aligns to 2:461/681 of Q5LUF3
- F348 (= F351) binding biotin
Sites not aligning to the query:
- 515 W→L: No effect on holoenzyme formation.
- 599 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 602 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 603 M→A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- 647 modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
50% identity, 69% coverage: 5:445/640 of query aligns to 1:426/646 of 3n6rG
- active site: K115 (= K119), K157 (= K161), D180 (≠ E190), H193 (= H211), R219 (= R237), T258 (= T276), E260 (= E278), E273 (= E291), N275 (= N293), R277 (= R295), E281 (= E299), R323 (= R341)
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:440/444 of 2vr1A
- active site: K116 (= K119), K159 (= K161), D194 (≠ A198), H207 (= H211), R233 (= R237), T272 (= T276), E274 (= E278), E286 (= E291), N288 (= N293), R290 (= R295), E294 (= E299), R336 (= R341)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K161), R165 (≠ K169), M167 (= M171), Y201 (= Y205), L202 (≠ V206), E274 (= E278), L276 (= L280), E286 (= E291), N288 (= N293), I435 (≠ T442)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
50% identity, 70% coverage: 2:447/640 of query aligns to 1:444/447 of 3jzfB
- active site: K118 (= K119), K161 (= K161), D198 (≠ A198), H211 (= H211), R237 (= R237), T276 (= T276), E278 (= E278), E290 (= E291), N292 (= N293), R294 (= R295), E298 (= E299), R340 (= R341)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K119), K161 (= K161), A162 (= A162), G166 (= G166), G168 (= G168), R169 (≠ K169), G170 (= G170), M171 (= M171), Y201 (≠ L201), E203 (= E203), K204 (= K204), Y205 (= Y205), H211 (= H211), H238 (= H238), L280 (= L280), I289 (≠ M290), E290 (= E291)
1dv2A The structure of biotin carboxylase, mutant e288k, complexed with atp (see paper)
50% identity, 70% coverage: 3:447/640 of query aligns to 3:445/450 of 1dv2A
- active site: K119 (= K119), K162 (= K161), D199 (≠ A198), H212 (= H211), R238 (= R237), T277 (= T276), E279 (= E278), K291 (≠ E291), N293 (= N293), R295 (= R295), E299 (= E299), R341 (= R341)
- binding adenosine-5'-triphosphate: K119 (= K119), K162 (= K161), G166 (= G165), G168 (= G167), M172 (= M171), E204 (= E203), K205 (= K204), Y206 (= Y205), L207 (≠ V206), H239 (= H238), L281 (= L280), K291 (≠ E291)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/444 of 3rupA
- active site: K116 (= K119), K159 (= K161), D196 (≠ A198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding adenosine-5'-diphosphate: Y82 (= Y85), G83 (= G86), K116 (= K119), K159 (= K161), G164 (= G166), G164 (= G166), G165 (= G167), G166 (= G168), R167 (≠ K169), M169 (= M171), F193 (= F195), E201 (= E203), K202 (= K204), Y203 (= Y205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (= H238), K238 (= K240), L278 (= L280), E288 (= E291), R292 (= R295), V295 (= V298), E296 (= E299), R338 (= R341), D382 (= D387), I437 (≠ T442)
- binding calcium ion: E87 (= E90), E276 (= E278), E288 (= E291), E288 (= E291), N290 (= N293)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/444 of 3g8cA
- active site: K116 (= K119), K159 (= K161), D196 (≠ A198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding adenosine-5'-diphosphate: I157 (≠ L159), K159 (= K161), G164 (= G166), M169 (= M171), E201 (= E203), K202 (= K204), Y203 (= Y205), L204 (≠ V206), Q233 (= Q235), H236 (= H238), L278 (= L280), E288 (= E291), I437 (≠ T442)
- binding bicarbonate ion: K238 (= K240), R292 (= R295), Q294 (= Q297), V295 (= V298), E296 (= E299)
- binding biotin: Y82 (= Y85), F84 (= F87), R292 (= R295), V295 (= V298), R338 (= R341), D382 (= D387)
- binding magnesium ion: E276 (= E278), E288 (= E291)
8uz2C E. Coli acetyl-coa carboxylase, narrow helical local reconstruction, 3.18 angstrom
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/446 of 8uz2C
- binding adenosine-5'-diphosphate: K116 (= K119), K159 (= K161), G164 (= G166), G165 (= G167), G166 (= G168), M169 (= M171), H209 (= H211), Q233 (= Q235), H236 (= H238), L278 (= L280), E288 (= E291), I437 (≠ T442)
- binding magnesium ion: E276 (= E278), E288 (= E291)
- binding : R356 (≠ L360), I410 (≠ A415)
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)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/446 of 6oi9A
- active site: E276 (= E278), E288 (= E291), N290 (= N293), E296 (= E299), R338 (= R341)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K161), M169 (= M171), E201 (= E203), Y203 (= Y205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (= H238), E276 (= E278), L278 (= L280), E288 (= E291), I437 (≠ T442)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/446 of 2w71A
- active site: K116 (= K119), K159 (= K161), D196 (≠ A198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K161), Y203 (= Y205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (= H238), L278 (= L280), I437 (≠ T442)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/446 of 2w70A
- active site: K116 (= K119), K159 (= K161), D196 (≠ A198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ L159), K159 (= K161), G166 (= G168), M169 (= M171), E201 (= E203), Y203 (= Y205), L204 (≠ V206), L278 (= L280)
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)
50% identity, 69% coverage: 5:447/640 of query aligns to 2:442/446 of 2w6zA
- active site: K116 (= K119), K159 (= K161), D196 (≠ A198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K161), Y203 (= Y205), L204 (≠ V206), L278 (= L280)
Query Sequence
>WP_090274990.1 NCBI__GCF_900105005.1:WP_090274990.1
MKHYIDTLLVANRGEIACRVMSTAKSMGLTTVAVHSAVDANARHAREADIRIDLGGAKPA
DSYLQIDKLIAAAKSSGAQAIHPGYGFLSENAGFARAIEAAGLIFLGPPAAAIDAMGSKS
AAKALMEEAGVPLVPGYHGEAQDLETFRAAAELIGYPVLLKATAGGGGKGMKVVEREEDL
AEALASAQREAQSSFGDARMLVEKYVLKPRHVEIQIFADQQGNCLYLNERDCSIQRRHQK
VVEEAPAPGLSAELRRAMGEAAVTAARAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEH
PVTEAITGLDLVAWQIRVARGEPLPITQEQVPLIGHAIEVRLYAEDPDNDFLPSTGTLAL
YREAATGAGRRVDSGVAEGDSVSPFYDPMLGKLIAWGENREEARLRLLAMLDETAIGGVR
TNLAFLRRVVGHPAFADAELDTDFIPRHETDLLRPASKLSDTFWQQAAEAFVSTTPVVAR
SDDAHSPWSRYDGLRLGMPAQITLHLQCNGESRRVQLTTSQPSSSEPLPRAIRQNDTLYL
QHSGEWLAVTAFDPITEAQDSLQQQGGLTAPMNGSIVRVLVEAGQHVAAGTALIVLEAMK
MEHSIRSAQDGVVKSLFCNEGDMVSEGTVLLELEEVQEDT
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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