SitesBLAST
Comparing WP_012592398.1 NCBI__GCF_000021745.1:WP_012592398.1 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)
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
44% identity, 96% coverage: 2:599/626 of query aligns to 2:641/666 of 8rthA
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
42% identity, 97% coverage: 4:611/626 of query aligns to 6:638/651 of 8j78I
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, 99% coverage: 1:618/626 of query aligns to 1:649/654 of P9WPQ3
- K322 (≠ P329) 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)
48% identity, 72% coverage: 1:448/626 of query aligns to 1:461/681 of Q5LUF3
- F348 (= F357) 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)
48% identity, 71% coverage: 2:448/626 of query aligns to 1:426/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E297), N275 (= N299), R277 (= R301), E281 (= E305), R323 (= R347)
Sites not aligning to the query:
7ybuA Human propionyl-coenzyme a carboxylase
49% identity, 71% coverage: 2:448/626 of query aligns to 5:446/670 of 7ybuA
Sites not aligning to the query:
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)
49% identity, 71% coverage: 2:448/626 of query aligns to 63:504/728 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 (= D316) to G: in PA-1
- M373 (≠ Q321) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G327) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A346) to R: in PA-1
- R399 (= R347) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P370) to L: in PA-1; dbSNP:rs1443858896
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 532 natural variant: Missing (in PA-1)
- 551 V → F: in dbSNP:rs61749895
- 559 W → L: in PA-1; dbSNP:rs118169528
- 631 G → R: in PA-1; loss of function; dbSNP:rs796052018
- 668 G → R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- 694 modified: N6-biotinyllysine; by HLCS
- 712 natural variant: Missing (in PA-1; loss of biotinylation)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
47% identity, 72% coverage: 1:450/626 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 (= E297), N287 (= N299), R289 (= R301), E293 (= E305), R335 (= R347)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (= Y202), L201 (≠ V203), H233 (= H235), L275 (≠ I277), E285 (= E297)
- binding magnesium ion: E273 (= E275), E285 (= E297)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
46% identity, 72% coverage: 1:450/626 of query aligns to 1:436/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E297), N284 (= N299), R286 (= R301), E290 (= E305), R332 (= R347)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (= Y202), L198 (≠ V203), E270 (= E275), L272 (≠ I277), E282 (= E297)
- binding bicarbonate ion: R286 (= R301), Q288 (= Q303), V289 (= V304)
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)
46% identity, 72% coverage: 1:450/626 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 (= E297), N285 (= N299), R287 (= R301), E291 (= E305), R333 (= R347)
- 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), Y198 (= Y202), L199 (≠ V203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (≠ I277), E283 (= E297), I432 (≠ T445)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
46% identity, 72% coverage: 3:451/626 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E297), N289 (= N299), R291 (= R301), E295 (= E305), R337 (= R347)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ L156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (≠ Y202), I201 (≠ V203), E273 (= E275), I275 (= I277), M286 (= M296), E287 (= E297)
- binding magnesium ion: E273 (= E275), E287 (= E297)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
47% identity, 72% coverage: 1:450/626 of query aligns to 1:440/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E297), N288 (= N299), R290 (= R301), E294 (= E305), R336 (= R347)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (= Y202), L202 (≠ V203), E274 (= E275), L276 (≠ I277), E286 (= E297), N288 (= N299), I435 (≠ T445)
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
47% identity, 72% coverage: 1:450/626 of query aligns to 1:442/448 of P43873
- K116 (= K116) binding ATP
- K159 (= K158) binding ATP
- EKYL 201:204 (≠ EKYV 200:203) binding ATP
- E276 (= E275) binding ATP; binding Mg(2+)
- E288 (= E297) binding ATP; binding Mg(2+)
- N290 (= N299) binding Mg(2+)
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
47% identity, 72% coverage: 1:450/626 of query aligns to 1:442/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding calcium ion: E276 (= E275), E288 (= E297), N290 (= N299)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), H236 (= H235), L278 (≠ I277), E288 (= E297), I437 (≠ T445)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 72% coverage: 1:450/626 of query aligns to 1:442/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ L156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (≠ Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ I277), E288 (= E297), I437 (≠ T445)
- binding magnesium ion: E276 (= E275), E288 (= E297)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
46% identity, 72% coverage: 1:450/626 of query aligns to 1:428/430 of 4mv1A
- active site: K116 (= K116), K159 (= K158), D182 (= D195), H195 (= H208), R221 (= R234), T260 (= T273), E262 (= E275), E274 (= E297), N276 (= N299), R278 (= R301), E282 (= E305), R324 (= R347)
- binding adenosine-5'-diphosphate: K159 (= K158), E187 (= E200), K188 (= K201), Y189 (= Y202), L190 (≠ V203), L264 (≠ I277)
- binding phosphate ion: K224 (= K237), R278 (= R301), Q280 (= Q303), V281 (= V304), E282 (= E305)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
47% identity, 72% coverage: 1:450/626 of query aligns to 1:442/445 of 3jziA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K158), A160 (= A159), G164 (= G163), G165 (= G164), M169 (= M168), Y199 (≠ L198), E201 (= E200), K202 (= K201), Y203 (= Y202), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ I277), I287 (≠ M296), E288 (= E297)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
47% identity, 72% coverage: 1:450/626 of query aligns to 1:442/445 of 2w6oA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K158), K202 (= K201), Y203 (= Y202), L204 (≠ V203), L278 (≠ I277), I437 (≠ T445)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
47% identity, 72% coverage: 1:450/626 of query aligns to 1:442/445 of 2w6nA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ L156), K159 (= K158), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (= Y202), L278 (≠ I277)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
47% identity, 72% coverage: 1:450/626 of query aligns to 1:442/445 of 2v59A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ I277), I437 (≠ T445)
Query Sequence
>WP_012592398.1 NCBI__GCF_000021745.1:WP_012592398.1
MFEKILIANRGEIARRIIRTAKRLGVRTVAVHSDVDAAMPFVAEADEAVGIGGASARESY
LAPDKILSAARTTGAEAIHPGYGFLSENADFAKAVAGAGLVWIGAPPAAIRAMGLKDAAK
RLMQKAGVPVTPGYLGDNQSLTRLQTEADAIGYPVLIKAVAGGGGKGMRKVEAAGSFAQA
LESCRREAAAAFGDDRVLLEKYVLNPRHIEVQIFGDSHGGVVHLFERDCSLQRRHQKVIE
EAPAPGMDDETRAAVCAAAVRAAKAVNYVGAGTIEFIAQSDADARGAVRADRIWFMEMNT
RLQVEHPVTEAITGQDLVEWQLRVACGEPLPLKQEALAINGWAMEARLYAENPATGFLPS
TGPLDWLRFPDNVRVDSGVERYGEVTPHYDPMIAKLIVHAPTRAMAAQRLAKAAGSVEAW
PVKTNAAFLARAASDADFVAGRVDTGFIDRHGDRLLPPKDPSHAVLQAAARAMLSADAVD
PWRALAGFRANAAPDRRIIVEVAGVSHVVAVEGPPPSARFAEVGGQRIVFFHGEAWPFGA
PTANRSGGEVVSTGVIVAPMPGRIVAVEISDGEKVSRGQKLLVLEAMKMEHAMTAPFDGV
IAHLKTKVGAQVSDGDVLLSVVKGED
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