SitesBLAST
Comparing AZOBR_RS22285 FitnessBrowser__azobra:AZOBR_RS22285 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)
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)
44% identity, 99% coverage: 1:663/667 of query aligns to 1:679/681 of Q5LUF3
- F348 (= F347) binding
- W515 (= W486) mutation to L: No effect on holoenzyme formation.
- L599 (≠ T584) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ A587) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ A588) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K629) modified: N6-biotinyllysine
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, 98% coverage: 1:654/667 of query aligns to 1:644/654 of P9WPQ3
- K322 (≠ V319) 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)
44% identity, 99% coverage: 2:663/667 of query aligns to 1:644/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E287), N275 (= N289), R277 (= R291), E281 (= E295), R323 (= R337), G519 (≠ A534)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M628), K612 (= K629)
7ybuA Human propionyl-coenzyme a carboxylase
45% identity, 99% coverage: 2:661/667 of query aligns to 5:667/670 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)
45% identity, 99% coverage: 2:661/667 of query aligns to 63:725/728 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 (= D306) to G: in PA-1
- M373 (≠ Q311) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G317) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A336) to R: in PA-1
- R399 (= R337) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P360) to L: in PA-1; dbSNP:rs1443858896
- L532 (vs. gap) natural variant: Missing (in PA-1)
- V551 (≠ A482) to F: in dbSNP:rs61749895
- W559 (= W495) to L: in PA-1; dbSNP:rs118169528
- G631 (= G573) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G603) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K629) modified: N6-biotinyllysine; by HLCS
- C712 (≠ F647) 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, 99% coverage: 5:663/667 of query aligns to 1:657/657 of 8sgxX
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
52% identity, 66% coverage: 1:443/667 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 (= E287), N288 (= N289), R290 (= R291), E294 (= E295), R336 (= R337)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (= Y202), L202 (= L203), E274 (= E275), L276 (= L277), E286 (= E287), N288 (= N289), I435 (≠ T438)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
51% identity, 66% coverage: 1:443/667 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 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (= Y202), L201 (= L203), H233 (= H235), L275 (= L277), E285 (= E287)
- binding magnesium ion: E273 (= E275), E285 (= E287)
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, 66% coverage: 1:443/667 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 (= E287), N285 (= N289), R287 (= R291), E291 (= E295), R333 (= R337)
- 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 (= L203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (= L277), E283 (= E287), I432 (≠ T438)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
51% identity, 66% coverage: 1:443/667 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 (= E287), N284 (= N289), R286 (= R291), E290 (= E295), R332 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (= Y202), L198 (= L203), E270 (= E275), L272 (= L277), E282 (= E287)
- binding bicarbonate ion: R286 (= R291), Q288 (= Q293), V289 (= V294)
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)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 6oi9A
- active site: E276 (= E275), E288 (= E287), N290 (= N289), E296 (= E295), R338 (= R337)
- 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 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), E276 (= E275), L278 (= L277), E288 (= E287), I437 (≠ T438)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (= Y202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T438)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- 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 (= L203), L278 (= L277)
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)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2w6zA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K158), Y203 (= Y202), L204 (= L203), L278 (= L277)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2w6qA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (≠ L156), K159 (= K158), E201 (= E200), K202 (= K201), Y203 (= Y202), L204 (= L203), H236 (= H235), L278 (= L277)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2w6pA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K158), Y203 (= Y202), L204 (= L203), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T438)
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2w6mA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (≠ L156), K159 (= K158), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (= Y202), H236 (= H235), L278 (= L277), I437 (≠ T438)
2v5aA Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 3 (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2v5aA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine: I157 (≠ L156), K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (= L203), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T438)
2v58A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 1 (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/446 of 2v58A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: I157 (≠ L156), K159 (= K158), E201 (= E200), Y203 (= Y202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T438)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
52% identity, 66% coverage: 1:443/667 of query aligns to 1:442/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K158), G164 (= G163), G164 (= G163), G165 (= G164), G166 (= G165), R167 (≠ K166), M169 (= M168), F193 (= F192), E201 (= E200), K202 (= K201), Y203 (= Y202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), K238 (= K237), L278 (= L277), E288 (= E287), R292 (= R291), V295 (= V294), E296 (= E295), R338 (= R337), D382 (= D383), I437 (≠ T438)
- binding calcium ion: E87 (= E87), E276 (= E275), E288 (= E287), E288 (= E287), N290 (= N289)
Query Sequence
>AZOBR_RS22285 FitnessBrowser__azobra:AZOBR_RS22285
MFDKILIANRGEIACRVIRTARRMGIRTVAVYSEADARAMHVEMADEAVCIGPAPVGESY
LRGDAILEVAKRTGAQAIHPGYGFLSENAGFAAACAEAGVVFIGPPIEAIRVMGSKAESK
RVMSQADVPLVPGFHGEAQDLETLSAEAERIGYPVLVKASAGGGGKGMRVVRAAGEFADA
VAGAKREAKAAFGDDSVLLEKYLGRPRHVEIQVFCDTHGNGVYLFERDCSIQRRHQKVIE
EAPAPALPDDLRRRMGEAAVAAAKAVNYVGAGTVEFLYEDGGFYFIEMNTRLQVEHPVTE
KITGQDLVEWQLRVAAGGVLPLMQDQLTRRGHAFEARLYAEDPQREFLPAIGKLVRLRPP
AENEHVRVDTGVREGDEVTMFYDPMIAKLIVWDEDRDAALRRLRVALAAYEVVGVTTNVA
FLGAIAGHPAFRAVEIDTGFIERHRADLLPPPAPVPDRGLAIAALSVLLRRNADTRKARR
AASDPWSPWLSASGWRLNDDNHHDLRLMDGDTPRALTLHFRPDGYEIEVEGRPAIRAERV
TLDGETLTATIDAVRTRATVVCQGLDLTILSDGAVWRLHLDDPTARAAEQEGGSGRLTAP
MPGTVVRVLVEPGQTVEAGAPLMLLEAMKMEHTIKAPAAGTVSAVNFAAGDQVSEGVDLL
VLDVAEG
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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