SitesBLAST
Comparing 201056 FitnessBrowser__MR1:201056 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)
40% identity, 97% coverage: 11:686/694 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F358) binding
- W515 (≠ R507) mutation to L: No effect on holoenzyme formation.
- L599 (≠ F591) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ F594) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ L595) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K652) modified: N6-biotinyllysine
7ybuA Human propionyl-coenzyme a carboxylase
41% identity, 97% coverage: 12:686/694 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)
41% identity, 97% coverage: 12:686/694 of query aligns to 63:728/728 of P05165
- A75 (= A24) to P: in PA-1; dbSNP:rs794727479
- R77 (= R26) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A87) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V113) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G146) to E: in PA-1
- M229 (= M178) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q246) to R: in PA-1
- D368 (= D317) to G: in PA-1
- M373 (≠ Q322) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G328) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V347) to R: in PA-1
- R399 (= R348) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P371) to L: in PA-1; dbSNP:rs1443858896
- L532 (vs. gap) natural variant: Missing (in PA-1)
- V551 (≠ A490) to F: in dbSNP:rs61749895
- W559 (≠ F506) to L: in PA-1; dbSNP:rs118169528
- G631 (≠ S597) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G626) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K652) modified: N6-biotinyllysine; by HLCS
- C712 (≠ F670) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 94% coverage: 11:665/694 of query aligns to 1:633/654 of P9WPQ3
- K322 (≠ P330) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
40% identity, 97% coverage: 12:686/694 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K126), K157 (= K168), D180 (= D205), H193 (= H218), R219 (= R244), T258 (= T283), E260 (= E285), E273 (= E298), N275 (= N300), R277 (= R302), E281 (= E306), R323 (= R348), G519 (≠ Q546)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M651), K612 (= K652)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
47% identity, 63% coverage: 15:452/694 of query aligns to 1:437/657 of 8sgxX
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:440/444 of 2vr1A
- active site: K116 (= K126), K159 (= K168), D194 (= D205), H207 (= H218), R233 (= R244), T272 (= T283), E274 (= E285), E286 (= E298), N288 (= N300), R290 (= R302), E294 (= E306), R336 (= R348)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K168), R165 (≠ K176), M167 (= M178), Y201 (= Y212), L202 (= L213), E274 (= E285), L276 (= L287), E286 (= E298), N288 (= N300), I435 (≠ T449)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:439/442 of 4mv4A
- active site: K116 (= K126), K159 (= K168), D193 (= D205), H206 (= H218), R232 (= R244), T271 (= T283), E273 (= E285), E285 (= E298), N287 (= N300), R289 (= R302), E293 (= E306), R335 (= R348)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K168), G164 (≠ K176), M166 (= M178), E198 (= E210), Y200 (= Y212), L201 (= L213), H233 (= H245), L275 (= L287), E285 (= E298)
- binding magnesium ion: E273 (= E285), E285 (= E298)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
48% identity, 64% coverage: 11:454/694 of query aligns to 1:436/439 of 4mv3A
- active site: K116 (= K126), K159 (= K168), D190 (= D205), H203 (= H218), R229 (= R244), T268 (= T283), E270 (= E285), E282 (= E298), N284 (= N300), R286 (= R302), E290 (= E306), R332 (= R348)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K168), M163 (= M178), E195 (= E210), Y197 (= Y212), L198 (= L213), E270 (= E285), L272 (= L287), E282 (= E298)
- binding bicarbonate ion: R286 (= R302), Q288 (= Q304), V289 (= V305)
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, 64% coverage: 11:454/694 of query aligns to 1:437/440 of 6oi8A
- active site: K116 (= K126), K159 (= K168), D191 (= D205), H204 (= H218), R230 (= R244), T269 (= T283), E271 (= E285), E283 (= E298), N285 (= N300), R287 (= R302), E291 (= E306), R333 (= R348)
- 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 (≠ L166), K159 (= K168), M164 (= M178), E196 (= E210), Y198 (= Y212), L199 (= L213), H204 (= H218), Q228 (= Q242), E271 (= E285), L273 (= L287), E283 (= E298), I432 (≠ T449)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
48% identity, 63% coverage: 14:452/694 of query aligns to 2:440/448 of 2vpqB
- active site: V116 (≠ A128), K156 (= K168), H206 (= H218), R232 (= R244), T271 (= T283), E273 (= E285), E287 (= E298), N289 (= N300), R291 (= R302), E295 (= E306), R337 (= R348)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K126), I154 (≠ L166), K156 (= K168), G161 (= G173), G163 (= G175), I166 (≠ M178), F200 (≠ Y212), I201 (≠ L213), E273 (= E285), I275 (≠ L287), M286 (= M297), E287 (= E298)
- binding magnesium ion: E273 (= E285), E287 (= E298)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
48% identity, 66% coverage: 11:470/694 of query aligns to 1:455/456 of 8hz4A
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, 64% coverage: 11:454/694 of query aligns to 1:442/445 of 6ojhA
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding calcium ion: E276 (= E285), E288 (= E298), N290 (= N300)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K168), M169 (= M178), E201 (= E210), Y203 (= Y212), L204 (= L213), H236 (= H245), L278 (= L287), E288 (= E298), I437 (≠ T449)
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, 64% coverage: 11:454/694 of query aligns to 1:442/448 of P43873
- K116 (= K126) binding
- K159 (= K168) binding
- EKYL 201:204 (≠ ERYL 210:213) binding
- E276 (= E285) binding ; binding
- E288 (= E298) binding ; binding
- N290 (= N300) binding
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:442/444 of 3rupA
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding adenosine-5'-diphosphate: Y82 (= Y92), G83 (= G93), K116 (= K126), K159 (= K168), G164 (= G173), G164 (= G173), G165 (= G174), G166 (= G175), R167 (≠ K176), M169 (= M178), F193 (= F202), E201 (= E210), K202 (≠ R211), Y203 (= Y212), L204 (= L213), H209 (= H218), Q233 (= Q242), H236 (= H245), K238 (= K247), L278 (= L287), E288 (= E298), R292 (= R302), V295 (= V305), E296 (= E306), R338 (= R348), D382 (= D394), I437 (≠ T449)
- binding calcium ion: E87 (= E97), E276 (= E285), E288 (= E298), E288 (= E298), N290 (= N300)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:442/444 of 3g8cA
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding adenosine-5'-diphosphate: I157 (≠ L166), K159 (= K168), G164 (= G173), M169 (= M178), E201 (= E210), K202 (≠ R211), Y203 (= Y212), L204 (= L213), Q233 (= Q242), H236 (= H245), L278 (= L287), E288 (= E298), I437 (≠ T449)
- binding bicarbonate ion: K238 (= K247), R292 (= R302), Q294 (= Q304), V295 (= V305), E296 (= E306)
- binding biotin: Y82 (= Y92), F84 (= F94), R292 (= R302), V295 (= V305), R338 (= R348), D382 (= D394)
- binding magnesium ion: E276 (= E285), E288 (= E298)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:442/445 of 3jziA
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K126), K159 (= K168), A160 (= A169), G164 (= G173), G165 (= G174), M169 (= M178), Y199 (≠ L208), E201 (= E210), K202 (≠ R211), Y203 (= Y212), H209 (= H218), Q233 (= Q242), H236 (= H245), L278 (= L287), I287 (≠ M297), E288 (= E298)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:442/445 of 2w6oA
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K168), K202 (≠ R211), Y203 (= Y212), L204 (= L213), L278 (= L287), I437 (≠ T449)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:442/445 of 2w6nA
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ L166), K159 (= K168), M169 (= M178), E201 (= E210), K202 (≠ R211), Y203 (= Y212), L278 (= L287)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
49% identity, 64% coverage: 11:454/694 of query aligns to 1:442/445 of 2v59A
- active site: K116 (= K126), K159 (= K168), D196 (= D205), H209 (= H218), R235 (= R244), T274 (= T283), E276 (= E285), E288 (= E298), N290 (= N300), R292 (= R302), E296 (= E306), R338 (= R348)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K168), Y203 (= Y212), L204 (= L213), H209 (= H218), Q233 (= Q242), H236 (= H245), L278 (= L287), I437 (≠ T449)
Query Sequence
>201056 FitnessBrowser__MR1:201056
MLTKQMLTNSMFTKLLIANRGEIACRIIKTAQAMGVRTVALYSDADKNARHVAMADESFY
LGGSAPADSYLKGDLIIAIAKKAQAQAIHPGYGFLSENADFARKCEAAGIVFVGPGSDAI
DAMGSKSAAKAIMTAAQVPLVPGYHGDDQTDATLKAEALKIGFPMLIKAAYGGGGKGMRI
VEHEGEIMDAINSARREAASSFGNDKLLMERYLRQPRHVEVQVFADTFGNAIYLSDRDCS
IQRRHQKVVEEAPAPGLSDELRAQMGEAAVAAAKAIDYVGAGTIEFLLDTDNSFYFMEMN
TRLQVEHPVTEMVTGQDLVKWQLMVASGQPLPLKQDEVRIHGHAFEVRIYAEDPQNEFLP
ASGKLNFLREPEQSKYVRIDSGIRENDVISNFYDPMIAKLIVWDESRPRALQRLVHALES
YQISGLKHNIEFLANIAEHPAFAKADFSTDFINRYGDALIGSASSEADTALAFAALYQVL
ARKEAAKAQAINSADPDSPWGQVSGFRLNSVSQHSIALLDDAHELQQLVLLDFGDHYQLS
HNRSSQHQLSQSAADGQVSKSLSGELKQDLLLAEINGHKSKVPVSAQGDDFTLFLPSGSY
HFRAVKTQVVEAESSNEDKLKAPMNGTVVTHLVDVGAEVKAGQGLLVMEAMKMEYTIEAP
FDGIVTEFYFKAGELVSDGAVLLHVEPKAQSEEA
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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