SitesBLAST
Comparing Pf6N2E2_2781 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2781 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)
3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
42% identity, 83% coverage: 202:1223/1226 of query aligns to 133:1129/1130 of 3va7A
- active site: H138 (= H207), E205 (= E274), E219 (= E288), N221 (= N290), V226 (= V295), E227 (= E296), R269 (= R340), A550 (≠ S620), I648 (≠ L713), L730 (= L816), D760 (= D845), N762 (≠ V847), F895 (≠ Y981)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y698), T641 (= T706), P653 (= P718), G656 (= G721), F658 (= F723), P943 (= P1028), G944 (= G1029), K1096 (= K1190)
- binding urea: D893 (= D979), Y937 (= Y1023), G944 (= G1029), G945 (= G1030), Y946 (= Y1031)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
44% identity, 36% coverage: 3:446/1226 of query aligns to 1:441/448 of 2vpqB
- active site: V116 (≠ T118), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ Y201), I201 (= I202), E273 (= E274), I275 (≠ V276), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E274), E287 (= E288)
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)
46% identity, 36% coverage: 1:442/1226 of query aligns to 1:458/681 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
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
43% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/447 of 2vqdA
- active site: K116 (= K116), K159 (= K157), P196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M155), K159 (= K157), G164 (= G162), G166 (= G164), F203 (≠ Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), E288 (= E288), I437 (≠ T442)
- binding magnesium ion: E276 (= E274), E288 (= E288)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
45% identity, 36% coverage: 2:442/1226 of query aligns to 1:423/646 of 3n6rG
- active site: K115 (= K116), K157 (= K157), D180 (≠ A194), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R340)
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
45% identity, 36% coverage: 1:446/1226 of query aligns to 1:439/444 of 2vr1A
- active site: K116 (= K116), K159 (= K157), D194 (≠ A194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (≠ I165), M167 (= M167), Y201 (= Y201), L202 (≠ I202), E274 (= E274), L276 (≠ V276), E286 (= E288), N288 (= N290), I435 (≠ T442)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
44% identity, 36% coverage: 1:446/1226 of query aligns to 1:438/442 of 4mv4A
- active site: K116 (= K116), K159 (= K157), D193 (≠ A194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (= M167), E198 (= E199), Y200 (= Y201), L201 (≠ I202), H233 (≠ N234), L275 (≠ V276), E285 (= E288)
- binding magnesium ion: E273 (= E274), E285 (= E288)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
43% identity, 36% coverage: 2:446/1226 of query aligns to 3:454/1129 of 3tw6B
- active site: K124 (= K116), K162 (= K157), H212 (= H207), R238 (= R233), T277 (= T272), E279 (= E274), E293 (= E288), N295 (= N290), R297 (= R292), E301 (= E296), R349 (= R340)
- binding adenosine-5'-diphosphate: K124 (= K116), K162 (= K157), G167 (= G162), G169 (= G164), M172 (= M167), E204 (= E199), L206 (≠ Y201), V207 (≠ I202), H212 (= H207), Q236 (= Q231), N239 (= N234), L281 (≠ V276), E293 (= E288), T450 (= T442)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R340), D395 (= D387)
- binding magnesium ion: E279 (= E274), E293 (= E288)
Sites not aligning to the query:
- active site: 544, 650, 713, 742, 744, 877
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 1102
- binding magnesium ion: 529, 530, 532, 763
- binding zinc ion: 544, 713, 742, 744
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
43% identity, 36% coverage: 1:446/1226 of query aligns to 1:444/654 of P9WPQ3
- K322 (≠ P322) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
43% identity, 36% coverage: 1:446/1226 of query aligns to 1:436/440 of 6oi8A
- active site: K116 (= K116), K159 (= K157), D191 (≠ A194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E288), N285 (= N290), R287 (= R292), E291 (= E296), R333 (= R340)
- 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 (≠ M155), K159 (= K157), M164 (= M167), E196 (= E199), Y198 (= Y201), L199 (≠ I202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (≠ V276), E283 (= E288), I432 (≠ T442)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
43% identity, 36% coverage: 1:446/1226 of query aligns to 1:435/439 of 4mv3A
- active site: K116 (= K116), K159 (= K157), D190 (≠ A194), H203 (= H207), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E288), N284 (= N290), R286 (= R292), E290 (= E296), R332 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (= M167), E195 (= E199), Y197 (= Y201), L198 (≠ I202), E270 (= E274), L272 (≠ V276), E282 (= E288)
- binding bicarbonate ion: R286 (= R292), Q288 (= Q294), V289 (= V295)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
43% identity, 36% coverage: 1:446/1226 of query aligns to 1:427/430 of 4mv1A
- active site: K116 (= K116), K159 (= K157), D182 (= D193), H195 (= H207), R221 (= R233), T260 (= T272), E262 (= E274), E274 (= E288), N276 (= N290), R278 (= R292), E282 (= E296), R324 (= R340)
- binding adenosine-5'-diphosphate: K159 (= K157), E187 (= E199), K188 (= K200), Y189 (= Y201), L190 (≠ I202), L264 (≠ V276)
- binding phosphate ion: K224 (= K236), R278 (= R292), Q280 (= Q294), V281 (= V295), E282 (= E296)
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)
44% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/448 of P43873
- K116 (= K116) binding
- K159 (= K157) binding
- EKYL 201:204 (≠ EKYI 199:202) binding
- E276 (= E274) binding ; binding
- E288 (= E288) binding ; binding
- N290 (= N290) 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
44% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/445 of 6ojhA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding calcium ion: E276 (= E274), E288 (= E288), N290 (= N290)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K157), M169 (= M167), E201 (= E199), Y203 (= Y201), L204 (≠ I202), H236 (≠ N234), L278 (≠ V276), E288 (= E288), I437 (≠ T442)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
45% identity, 36% coverage: 1:446/1226 of query aligns to 3:443/447 of 3jzfB
- active site: K118 (= K116), K161 (= K157), D198 (≠ A194), H211 (= H207), R237 (= R233), T276 (= T272), E278 (= E274), E290 (= E288), N292 (= N290), R294 (= R292), E298 (= E296), R340 (= R340)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K157), A162 (≠ S158), G166 (= G162), G168 (= G164), R169 (≠ I165), G170 (= G166), M171 (= M167), Y201 (≠ F197), E203 (= E199), K204 (= K200), Y205 (= Y201), H211 (= H207), H238 (≠ N234), L280 (≠ V276), I289 (≠ L287), E290 (= E288)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
45% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/445 of 3jziA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K157), A160 (≠ S158), G164 (= G162), G165 (= G163), M169 (= M167), Y199 (≠ F197), E201 (= E199), K202 (= K200), Y203 (= Y201), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), I287 (≠ L287), E288 (= E288)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
45% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/445 of 2w6oA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K157), K202 (= K200), Y203 (= Y201), L204 (≠ I202), L278 (≠ V276), I437 (≠ T442)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
45% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/445 of 2w6nA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M155), K159 (= K157), M169 (= M167), E201 (= E199), K202 (= K200), Y203 (= Y201), L278 (≠ V276)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
45% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/445 of 2v59A
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K157), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), 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)
45% identity, 36% coverage: 1:446/1226 of query aligns to 1:441/449 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 (= K157) binding
- GG 165:166 (= GG 163:164) binding
- EKYL 201:204 (≠ EKYI 199:202) binding
- H209 (= H207) binding
- H236 (≠ N234) binding
- K238 (= K236) binding
- E276 (= E274) binding ; binding
- E288 (= E288) binding ; binding
- R292 (= R292) active site; binding
- V295 (= V295) binding
- E296 (= E296) mutation to A: Severe reduction in catalytic activity.
- R338 (= R340) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ K368) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R371) mutation to E: Loss of homodimerization. No effect on ATP binding.
Query Sequence
>Pf6N2E2_2781 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2781
MFEKILIANRGAIACRILRTLRELKVQGVAVYSQADAASLHILQADEAHCLGEGAAAGTY
LAVDKLLAIAKGSGATAIHPGYGFLSENAAFAEACEAAGIAFIGPTPEQLRVFGLKHTAR
DLARQHGVPLLEGTELLDSLDAALLAATRIGYPVMLKSTAGGGGIGMRVCRSAAELSESF
EAVKRLGQNNFSDAGVFIEKYIERARHLEVQVFGDGQGQVIALGVRDCSVQRRNQKVLEE
TPAPNLPEGMADELCAAAIQLAQAVNYRSAGTVEFVFDSDAGRFYFLEVNTRLQVEHGVT
EQVWGVDLVRWMVQLAAGDLPPLNELGQGLKAEGHAIQARLYAEDPGRDFQPSPGLLTAV
KFPQADGKALRIDTWVEAGCQIPPYFDPMIAKVIRWAPTREQARLGLYQALDESLLYGVE
TNRQYLQQILLDTPFASGQPWTRCLEALVYRANTVEVLSPGTQTSVQDYPGRLGYWAVGV
PPSGPMDSRSLRLGNRLLGNEEGAAALEITMNGPLLRFNCAARVTVTGAVIALTLDGEAV
PMNTPLSIAAGATLAIGNISGAGARSYLCLQGGVQVPDYLGSKSTFTLGQFGGHGGRALC
TGDVLHLTPLDEHTTLPPTSAPILELPSVRQIRVIYGPHGAPEYFTERYIQTFFDTAWEV
HFNSSRTGVRLIGPKPEWVRADGGEAGLHPSNIHDNPYAIGAVDFTGDMPVILGPDGPSL
GGFVCPVTVIEADLWQLGQLKAGDKVRFVPVDISTARSLATHIPCGEGACSRSNAQHSPD
NGPTDKELGPLRDPARASSLATGSGCTQKWGSPVVLDIGQDDTRLVARLSGDTHLLLEIG
APELDLVLRFRAHALMQALEHKHLPGVIDLTPGIRSLQVHYQPEQLPLADLLSIVAGEWD
AVCAAQDLQVPSRIVHLPLSWDDPACQLAIEKYMTTVRKDAPWCPSNLEFIRRINDLPNL
DEVQRTVFDASYLVMGLGDVYLGAPVATPLDPRHRLVTTKYNPARTWTAENSVGIGGAYM
CVYGMEGPGGYQFVGRTLQMWNRYRDVAAFDGKPWLLRFFDQIRFYPVSADELLRIRRDF
PLGRFDLAIEHSQLNLAEYQRFLAQEADSIAAFRHQQQRAFEAERERWIASGQAHFDSEE
PAIAPSEDSPLTDGQLSVDSHIAGNLWQVQVEVGARVAAGDVLVILESMKMEIPVLAPVA
GVVREVRVQPGSAVRAGQRVVVLERD
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