SitesBLAST
Comparing CA265_RS02215 FitnessBrowser__Pedo557:CA265_RS02215 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)
7ybuA Human propionyl-coenzyme a carboxylase
51% identity, 93% coverage: 13:478/503 of query aligns to 7:475/670 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)
51% identity, 93% coverage: 13:478/503 of query aligns to 65:533/728 of P05165
- A75 (= A23) to P: in PA-1; dbSNP:rs794727479
- R77 (= R25) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A86) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V112) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ E145) to E: in PA-1
- M229 (= M177) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q245) 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 (≠ L346) to R: in PA-1
- R399 (= R347) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P370) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L477) natural variant: Missing (in PA-1)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
51% identity, 86% coverage: 14:447/503 of query aligns to 5:440/654 of P9WPQ3
- K322 (= K329) 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, 89% coverage: 12:460/503 of query aligns to 3:470/681 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
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
51% identity, 88% coverage: 11:452/503 of query aligns to 2:439/442 of 4mv4A
- active site: K116 (= K125), K159 (= K167), D193 (≠ G204), H206 (= H217), R232 (= R243), T271 (= T282), E273 (= E284), E285 (= E297), N287 (= N299), R289 (= R301), E293 (= E305), R335 (= R347)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K167), G164 (= G172), M166 (= M177), E198 (= E209), Y200 (= Y211), L201 (≠ V212), H233 (= H244), L275 (= L287), E285 (= E297)
- binding magnesium ion: E273 (= E284), E285 (= E297)
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)
51% identity, 88% coverage: 11:452/503 of query aligns to 2:437/440 of 6oi8A
- active site: K116 (= K125), K159 (= K167), D191 (≠ G204), H204 (= H217), R230 (= R243), T269 (= T282), E271 (= E284), 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 (≠ L165), K159 (= K167), M164 (= M177), E196 (= E209), Y198 (= Y211), L199 (≠ V212), H204 (= H217), Q228 (= Q241), E271 (= E284), L273 (= L287), E283 (= E297), I432 (≠ T447)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
51% identity, 88% coverage: 11:452/503 of query aligns to 2:436/439 of 4mv3A
- active site: K116 (= K125), K159 (= K167), D190 (≠ G204), H203 (= H217), R229 (= R243), T268 (= T282), E270 (= E284), E282 (= E297), N284 (= N299), R286 (= R301), E290 (= E305), R332 (= R347)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K167), M163 (= M177), E195 (= E209), Y197 (= Y211), L198 (≠ V212), E270 (= E284), L272 (= L287), E282 (= E297)
- binding bicarbonate ion: R286 (= R301), Q288 (= Q303), V289 (= V304)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
50% identity, 89% coverage: 12:460/503 of query aligns to 2:435/646 of 3n6rG
- active site: K115 (= K125), K157 (= K167), D180 (≠ E196), H193 (= H217), R219 (= R243), T258 (= T282), E260 (= E284), E273 (= E297), N275 (= N299), R277 (= R301), E281 (= E305), R323 (= R347)
Sites not aligning to the query:
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
52% identity, 87% coverage: 14:453/503 of query aligns to 5:440/456 of 8hz4A
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
49% identity, 87% coverage: 13:450/503 of query aligns to 2:440/448 of 2vpqB
- active site: V116 (≠ S127), K156 (= K167), H206 (= H217), R232 (= R243), T271 (= T282), E273 (= E284), E287 (= E297), N289 (= N299), R291 (= R301), E295 (= E305), R337 (= R347)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K125), I154 (≠ L165), K156 (= K167), G161 (= G172), G163 (= G174), I166 (≠ M177), F200 (≠ Y211), I201 (≠ V212), E273 (= E284), I275 (= I286), M286 (≠ L296), E287 (= E297)
- binding magnesium ion: E273 (= E284), E287 (= E297)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:440/444 of 2vr1A
- active site: K116 (= K125), K159 (= K167), D194 (≠ G204), H207 (= H217), R233 (= R243), T272 (= T282), E274 (= E284), E286 (= E297), N288 (= N299), R290 (= R301), E294 (= E305), R336 (= R347)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K167), R165 (≠ K175), M167 (= M177), Y201 (= Y211), L202 (≠ V212), E274 (= E284), L276 (≠ I286), E286 (= E297), N288 (= N299), I435 (≠ T447)
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)
52% identity, 88% coverage: 11:452/503 of query aligns to 2:442/448 of P43873
- K116 (= K125) binding
- K159 (= K167) binding
- EKYL 201:204 (≠ ERYV 209:212) binding
- E276 (= E284) binding ; binding
- E288 (= E297) binding ; binding
- N290 (= N299) 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
52% identity, 88% coverage: 11:452/503 of query aligns to 2:442/445 of 6ojhA
- active site: K116 (= K125), K159 (= K167), D196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding calcium ion: E276 (= E284), E288 (= E297), N290 (= N299)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K167), M169 (= M177), E201 (= E209), Y203 (= Y211), L204 (≠ V212), H236 (= H244), L278 (= L287), E288 (= E297), I437 (≠ T447)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
51% identity, 88% coverage: 11:452/503 of query aligns to 2:442/447 of 2vqdA
- active site: K116 (= K125), K159 (= K167), P196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K125), I157 (≠ L165), K159 (= K167), G164 (= G172), G166 (= G174), F203 (≠ Y211), L204 (≠ V212), H209 (= H217), Q233 (= Q241), H236 (= H244), L278 (= L287), E288 (= E297), I437 (≠ T447)
- binding magnesium ion: E276 (= E284), E288 (= E297)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:428/430 of 4mv1A
- active site: K116 (= K125), K159 (= K167), D182 (≠ E196), H195 (= H217), R221 (= R243), T260 (= T282), E262 (= E284), E274 (= E297), N276 (= N299), R278 (= R301), E282 (= E305), R324 (= R347)
- binding adenosine-5'-diphosphate: K159 (= K167), E187 (= E209), K188 (≠ R210), Y189 (= Y211), L190 (≠ V212), L264 (= L287)
- binding phosphate ion: K224 (= K246), R278 (= R301), Q280 (= Q303), V281 (= V304), E282 (= E305)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:442/444 of 3rupA
- active site: K116 (= K125), K159 (= K167), D196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding adenosine-5'-diphosphate: Y82 (= Y91), G83 (= G92), K116 (= K125), K159 (= K167), G164 (= G172), G164 (= G172), G165 (= G173), G166 (= G174), R167 (≠ K175), M169 (= M177), F193 (= F201), E201 (= E209), K202 (≠ R210), Y203 (= Y211), L204 (≠ V212), H209 (= H217), Q233 (= Q241), H236 (= H244), K238 (= K246), L278 (≠ I286), E288 (= E297), R292 (= R301), V295 (= V304), E296 (= E305), R338 (= R347), D382 (= D392), I437 (≠ T447)
- binding calcium ion: E87 (= E96), E276 (= E284), E288 (= E297), E288 (= E297), N290 (= N299)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:442/444 of 3g8cA
- active site: K116 (= K125), K159 (= K167), D196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding adenosine-5'-diphosphate: I157 (≠ L165), K159 (= K167), G164 (= G172), M169 (= M177), E201 (= E209), K202 (≠ R210), Y203 (= Y211), L204 (≠ V212), Q233 (= Q241), H236 (= H244), L278 (≠ I286), E288 (= E297), I437 (≠ T447)
- binding bicarbonate ion: K238 (= K246), R292 (= R301), Q294 (= Q303), V295 (= V304), E296 (= E305)
- binding biotin: Y82 (= Y91), F84 (= F93), R292 (= R301), V295 (= V304), R338 (= R347), D382 (= D392)
- binding magnesium ion: E276 (= E284), E288 (= E297)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:442/445 of 3jziA
- active site: K116 (= K125), K159 (= K167), D196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), 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 (= K125), K159 (= K167), A160 (= A168), G164 (= G172), G165 (= G173), M169 (= M177), Y199 (≠ F207), E201 (= E209), K202 (≠ R210), Y203 (= Y211), H209 (= H217), Q233 (= Q241), H236 (= H244), L278 (≠ I286), I287 (≠ L296), 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)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:442/445 of 2w6oA
- active site: K116 (= K125), K159 (= K167), D196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K167), K202 (≠ R210), Y203 (= Y211), L204 (≠ V212), L278 (≠ I286), I437 (≠ T447)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
50% identity, 88% coverage: 11:452/503 of query aligns to 2:442/445 of 2w6nA
- active site: K116 (= K125), K159 (= K167), D196 (≠ G204), H209 (= H217), R235 (= R243), T274 (= T282), E276 (= E284), E288 (= E297), N290 (= N299), R292 (= R301), E296 (= E305), R338 (= R347)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ L165), K159 (= K167), M169 (= M177), E201 (= E209), K202 (≠ R210), Y203 (= Y211), L278 (≠ I286)
Query Sequence
>CA265_RS02215 FitnessBrowser__Pedo557:CA265_RS02215
MPENSKAQTPISKLLVANRGEIALRIMRSAKEMGIKTVAVFSEADRNALHVRYADEAVCI
GPAPSNQSYLVGEKIIGACKLTGAEAIHPGYGFLSENAGFAQMVADAGLILVGPSPQAME
TMGNKLSAKAAALKYNIPMVPGTEEAIQDVNEAKQRAIEVGFPILIKAAAGGGGKGMRIV
ERAEDFEEQMQLAVSEATSAFGDGAVFIERYVTSPRHIEIQVLGDNHGNIVHLFERECSV
QRRHQKVIEEAPSSVLTEEIRQRMGKCAVDVARSVNYTGAGTVEFILDENLDFFFLEMNT
RLQVEHPVTELITGIDLVKEQLKIASGEKLSFSQEDLKISGHAVELRVYAEDPANNFLPD
IGTLQTYNTPKGNGVRVDDGFEQGMEIPIYYDPMIAKLITYGKDREEAIERMVRAIEEYD
ITGIETTLGFGKFVMQHEAFKTGNFDTHFVGKYFKPESLKVQDETEALIAAVIAAKLFDK
KEVKLGDAAIKNSSDWRKNRLKY
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