SitesBLAST
Comparing CCNA_02250 FitnessBrowser__Caulo:CCNA_02250 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
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, 99% coverage: 1:650/654 of query aligns to 1:653/654 of P9WPQ3
- K322 (≠ P325) 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)
49% identity, 68% coverage: 1:445/654 of query aligns to 1:461/681 of Q5LUF3
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
7ybuA Human propionyl-coenzyme a carboxylase
40% identity, 99% coverage: 2:650/654 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)
40% identity, 99% coverage: 2:650/654 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 (= D312) to G: in PA-1
- M373 (≠ Q317) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G323) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A342) to R: in PA-1
- R399 (= R343) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P366) to L: in PA-1; dbSNP:rs1443858896
- L532 (vs. gap) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W483) to L: in PA-1; dbSNP:rs118169528
- G631 (≠ P546) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G590) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K616) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A634) 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)
50% identity, 68% coverage: 2:445/654 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 (= E293), N275 (= N295), R277 (= R297), E281 (= E301), R323 (= R343)
Sites not aligning to the query:
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
38% identity, 99% coverage: 5:650/654 of query aligns to 1:657/657 of 8sgxX
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
48% identity, 69% coverage: 1:449/654 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E293), N287 (= N295), R289 (= R297), E293 (= E301), R335 (= R343)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (= Y202), L201 (≠ V203), H233 (= H235), L275 (≠ I277), E285 (= E293)
- binding magnesium ion: E273 (= E275), E285 (= E293)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
50% identity, 69% coverage: 1:449/654 of query aligns to 1:444/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- 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 (= E293), I437 (≠ T442)
- binding magnesium ion: E276 (= E275), E288 (= E293)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
49% identity, 68% coverage: 3:446/654 of query aligns to 1:441/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E293), N289 (= N295), R291 (= R297), E295 (= E301), R337 (= R343)
- 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 (= M292), E287 (= E293)
- binding magnesium ion: E273 (= E275), E287 (= E293)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E293), N288 (= N295), R290 (= R297), E294 (= E301), R336 (= R343)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (= Y202), L202 (≠ V203), E274 (= E275), L276 (≠ I277), E286 (= E293), N288 (= N295), I435 (≠ T442)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
48% identity, 69% coverage: 1:449/654 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E293), N284 (= N295), R286 (= R297), E290 (= E301), R332 (= R343)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (= Y202), L198 (≠ V203), E270 (= E275), L272 (≠ I277), E282 (= E293)
- binding bicarbonate ion: R286 (= R297), Q288 (= Q299), V289 (= V300)
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)
48% identity, 69% coverage: 1:449/654 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E293), N285 (= N295), R287 (= R297), E291 (= E301), R333 (= R343)
- 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 (= E293), I432 (≠ T442)
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)
49% identity, 69% coverage: 1:449/654 of query aligns to 1:444/448 of P43873
- K116 (= K116) binding
- K159 (= K158) binding
- EKYL 201:204 (≠ EKYV 200:203) binding
- E276 (= E275) binding ; binding
- E288 (= E293) binding ; binding
- N290 (= N295) binding
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
49% identity, 69% coverage: 1:449/654 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding calcium ion: E276 (= E275), E288 (= E293), N290 (= N295)
- 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 (= E293), I437 (≠ T442)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:444/449 of P24182
- R19 (= R19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (= E23) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K116) binding
- K159 (= K158) binding
- GG 165:166 (= GG 164:165) binding
- EKYL 201:204 (≠ EKYV 200:203) binding
- H209 (= H208) binding
- H236 (= H235) binding
- K238 (= K237) binding
- E276 (= E275) binding ; binding
- E288 (= E293) binding ; binding
- R292 (= R297) active site; binding
- V295 (= V300) binding
- E296 (= E301) mutation to A: Severe reduction in catalytic activity.
- R338 (= R343) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (vs. gap) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R371) mutation to E: Loss of homodimerization. No effect on ATP binding.
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)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:444/446 of 6oi9A
- active site: E276 (= E275), E288 (= E293), N290 (= N295), E296 (= E301), R338 (= R343)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), E276 (= E275), L278 (≠ I277), E288 (= E293), I437 (≠ T442)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:444/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ I277), I437 (≠ T442)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:444/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ L156), K159 (= K158), G166 (= G165), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), L278 (≠ I277)
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)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:444/446 of 2w6zA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), L278 (≠ I277)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
47% identity, 69% coverage: 1:449/654 of query aligns to 1:444/446 of 2w6qA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (≠ L156), K159 (= K158), E201 (= E200), K202 (= K201), Y203 (= Y202), L204 (≠ V203), H236 (= H235), L278 (≠ I277)
Query Sequence
>CCNA_02250 FitnessBrowser__Caulo:CCNA_02250
MLSSVLIANRGEIARRIIRTARELGVRTIAVYSEADANAPFVMEADAAILIGPAPAKESY
LDPRKILAAARQMGAEAIHPGYGFLSENAEFAQSVIDAGLVWIGPPPSAIRAMGLKDAAK
AVMIKAGVPTTPGYLGEDQSVERLTVEAAKIGYPVLIKAVAGGGGKGMRKVERAEDFEAA
LGSCRREASAAFGDDRVLLEKYVTRPRHIEVQVFGDSHGNVVHLFERDCSLQRRHQKVIE
EAPAPGMDEATREAVCAAAVKAAQAVNYVGAGTVEFIADASEGLRADRIWFMEMNTRLQV
EHPVTEMVTGQDLVEWQLRVASGEPLPLEQDEITLDGWAMEARLYAENPATGFLPSTGKL
KHFRLPEGDVRVDSAVEEGGEVTPFYDPMIAKLIAHGADREDAAQRLAEACALVEVWPVK
TNAAFLAKCASHPDFVDGAVDTGFIEARLDELTERAFSDEPAMAAIGWRLDSFLEAEARR
DPWEGAPSKLLGFRMNAPRASMHLPMSTDGKATPLRVALIGGGTEDWSWDIRHADGSTFD
EVTRLPTTYGKGPIQVFEGGDVQEFDFVAKIGGAGEGGASDGAILSPMPGKIVSVSVSAG
QTVSKGQTLLTLEAMKMEHAMAAPFDGVVAELSAVAGGQVSEGVVLARLEPAVA
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