SitesBLAST
Comparing CCNA_01905 FitnessBrowser__Caulo:CCNA_01905 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)
3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
46% identity, 83% coverage: 202:1199/1207 of query aligns to 133:1129/1130 of 3va7A
- active site: H138 (= H207), E205 (= E274), E219 (= E288), N221 (= N290), V226 (= V295), E227 (= E296), R269 (= R338), A550 (= A611), I648 (≠ L707), L730 (= L787), D760 (= D816), N762 (≠ E818), F895 (≠ Y952)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y692), T641 (= T700), P653 (= P712), G656 (= G715), F658 (= F717), P943 (= P999), G944 (= G1000), K1096 (= K1166)
- binding urea: D893 (= D950), Y937 (= Y994), G944 (= G1000), G945 (= G1001), Y946 (= Y1002)
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, 36% coverage: 1:436/1207 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
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
48% identity, 40% coverage: 1:478/1207 of query aligns to 1:485/654 of P9WPQ3
- K322 (≠ F320) 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)
49% identity, 36% coverage: 2:436/1207 of query aligns to 1:423/646 of 3n6rG
- active site: K115 (= K116), K157 (= K157), D180 (≠ G194), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R338)
Sites not aligning to the query:
7ybuA Human propionyl-coenzyme a carboxylase
46% identity, 37% coverage: 2:442/1207 of query aligns to 5:449/670 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)
46% identity, 37% coverage: 2:442/1207 of query aligns to 63:507/728 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 (vs. gap) to E: in PA-1
- M229 (= M167) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1
- D368 (= D307) to G: in PA-1
- M373 (= M312) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G318) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V337) to R: in PA-1
- R399 (= R338) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P361) to L: in PA-1; dbSNP:rs1443858896
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 532 natural variant: Missing (in PA-1)
- 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)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
43% identity, 37% coverage: 4:447/1207 of query aligns to 2:448/448 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 (= R338)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (= I155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ Y201), I201 (≠ V202), E273 (= E274), I275 (≠ L276), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E274), E287 (= E288)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
45% identity, 36% coverage: 1:440/1207 of query aligns to 1:438/442 of 4mv4A
- active site: K116 (= K116), K159 (= K157), D193 (≠ G194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (= M167), E198 (= E199), Y200 (= Y201), L201 (≠ V202), H233 (≠ N234), L275 (= L276), E285 (= E288)
- binding magnesium ion: E273 (= E274), E285 (= E288)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
45% identity, 36% coverage: 1:440/1207 of query aligns to 1:441/447 of 2vqdA
- active site: K116 (= K116), K159 (= K157), P196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (= I155), K159 (= K157), G164 (= G162), G166 (= G164), F203 (≠ Y201), L204 (≠ V202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (= L276), E288 (= E288), I437 (≠ T436)
- binding magnesium ion: E276 (= E274), E288 (= E288)
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)
45% identity, 36% coverage: 1:440/1207 of query aligns to 1:436/440 of 6oi8A
- active site: K116 (= K116), K159 (= K157), D191 (≠ G194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E288), N285 (= N290), R287 (= R292), E291 (= E296), R333 (= R338)
- 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 (= I155), K159 (= K157), M164 (= M167), E196 (= E199), Y198 (= Y201), L199 (≠ V202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (= L276), E283 (= E288), I432 (≠ T436)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
45% identity, 36% coverage: 1:440/1207 of query aligns to 1:435/439 of 4mv3A
- active site: K116 (= K116), K159 (= K157), D190 (≠ G194), H203 (= H207), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E288), N284 (= N290), R286 (= R292), E290 (= E296), R332 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (= M167), E195 (= E199), Y197 (= Y201), L198 (≠ V202), E270 (= E274), L272 (= L276), E282 (= E288)
- binding bicarbonate ion: R286 (= R292), Q288 (= Q294), V289 (= V295)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
44% identity, 36% coverage: 1:440/1207 of query aligns to 1:439/444 of 2vr1A
- active site: K116 (= K116), K159 (= K157), D194 (≠ G194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R338)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (≠ I165), M167 (= M167), Y201 (= Y201), L202 (≠ V202), E274 (= E274), L276 (= L276), E286 (= E288), N288 (= N290), I435 (≠ T436)
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)
46% identity, 36% coverage: 1:440/1207 of query aligns to 1:441/448 of P43873
- K116 (= K116) binding
- K159 (= K157) binding
- EKYL 201:204 (≠ ERYV 199:202) binding
- E276 (= E274) binding ; binding
- E288 (= E288) binding ; binding
- N290 (= N290) binding
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
43% identity, 36% coverage: 5:440/1207 of query aligns to 1:438/657 of 8sgxX
Sites not aligning to the query:
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
46% identity, 36% coverage: 1:440/1207 of query aligns to 1:441/445 of 6ojhA
- active site: K116 (= K116), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- 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 (≠ V202), H236 (≠ N234), L278 (= L276), E288 (= E288), I437 (≠ T436)
7kctA Crystal structure of the hydrogenobacter thermophilus 2-oxoglutarate carboxylase (ogc) biotin carboxylase (bc) domain dimer in complex with adenosine 5'-diphosphate magnesium salt (mgadp), adenosine 5'- diphosphate (adp, and bicarbonate anion (hydrogen carbonate/hco3-) (see paper)
42% identity, 36% coverage: 1:440/1207 of query aligns to 3:443/453 of 7kctA
- active site: E276 (= E274), E289 (= E288), N291 (= N290), E297 (= E296), R339 (= R338)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (≠ I155), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), I169 (≠ M167), E201 (= E199), Y203 (= Y201), I204 (≠ V202), H209 (= H207), Q233 (= Q231), Q237 (= Q235), K238 (= K236), I278 (≠ L276), E289 (= E288), R293 (= R292), Q295 (= Q294), V296 (= V295), E297 (= E296), R339 (= R338)
- binding bicarbonate ion: D116 (≠ L115), R119 (≠ T118)
- binding magnesium ion: E276 (= E274), E289 (= E288)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 36% coverage: 1:440/1207 of query aligns to 1:441/449 of P24182
- R19 (= R19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ A23) 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 (≠ ERYV 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 (= R338) 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 (= R365) mutation to E: Loss of homodimerization. No effect on ATP binding.
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
44% identity, 36% coverage: 1:440/1207 of query aligns to 1:441/444 of 3rupA
- active site: K116 (= K116), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K157), G164 (= G162), G164 (= G162), G165 (= G163), G166 (= G164), R167 (≠ I165), M169 (= M167), F193 (= F191), E201 (= E199), K202 (≠ R200), Y203 (= Y201), L204 (≠ V202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), K238 (= K236), L278 (= L276), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R338), D382 (= D381), I437 (≠ T436)
- binding calcium ion: E87 (= E87), E276 (= E274), E288 (= E288), E288 (= E288), N290 (= N290)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
44% identity, 36% coverage: 1:440/1207 of query aligns to 1:441/444 of 3g8cA
- active site: K116 (= K116), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: I157 (= I155), K159 (= K157), G164 (= G162), M169 (= M167), E201 (= E199), K202 (≠ R200), Y203 (= Y201), L204 (≠ V202), Q233 (= Q231), H236 (≠ N234), L278 (= L276), E288 (= E288), I437 (≠ T436)
- binding bicarbonate ion: K238 (= K236), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R338), D382 (= D381)
- binding magnesium ion: E276 (= E274), E288 (= E288)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
44% identity, 36% coverage: 1:440/1207 of query aligns to 3:443/447 of 3jzfB
- active site: K118 (= K116), K161 (= K157), D198 (≠ G194), H211 (= H207), R237 (= R233), T276 (= T272), E278 (= E274), E290 (= E288), N292 (= N290), R294 (= R292), E298 (= E296), R340 (= R338)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K157), A162 (= A158), G166 (= G162), G168 (= G164), R169 (≠ I165), G170 (= G166), M171 (= M167), Y201 (≠ F197), E203 (= E199), K204 (≠ R200), Y205 (= Y201), H211 (= H207), H238 (≠ N234), L280 (= L276), I289 (≠ L287), E290 (= E288)
Query Sequence
>CCNA_01905 FitnessBrowser__Caulo:CCNA_01905
MFDKVLIANRGAIACRIIRTLRAMGVKSVAVFSDADAGSLHVSMADEAVRLGPAPAAESY
LRADLVLAAAQATGAQAIHPGYGFLSESAAFAQACEDAGVTFIGPSADNIRAFGLKHTAR
DLAQAHGVPLAPGTDLLTDPAAALAAAQRIGFPVILKATAGGGGIGMRVCESAEAVEEAF
AAVRRLATGNFSDGGVFLERYVHKARHIEVQVFGDGAGRVAALGERDCSLQRRNQKVVEE
TPAPGLPAATRTALLDAAVRLAKAANYRSAGTVEFLYDADRDDFFFLEVNTRLQVEHGVT
EQVTGVDLVEWMVRGAAGDFSFLDTPPPAPRGAAIQVRLYAEDPAQDYRPSAGVLTEVAF
PEGVRADGWVVDGTEVSAFYDPMLAKLIVIAEHRPAAVAALQAALDATRLAGIETNLDWL
RTVTRSQPFVSGEVSTRALETIAWAPDTIQVLSGGPATTVQDWPGRRGYWDVGVPPSGPM
DALAFRLGNRLLANPDDAAGLEITALGPTLKFNRPATLCLTGARFDARLDGVAVEPYTPF
DVRPGQTLKIGRVVEAGLRGYLLLRGGLDVPTYLGSRSTFTLGGFGGHAGRNLTAGDVLR
LLPAPEAPPGALDEPLRPALTKTWTIRVLPGPHGAPDFFTPADVAMIGGTDWKVHYNSNR
TGVRLVGPKPEWARRDGGEAGLHPSNIHDNAYAIGAIDFTGDMPIILGPDGPSLGGFVCP
FVIIEADLWKAGQLAPGDTVRFAVVDDPTAAAALETQEALIAQLGAAPPRPAPAVIDVEA
SPILRELPQDGHRPRVLYRRQGDQHLLVEYGPIVLDLELRLRIHALLLDLQAQALEGVID
LTPGIRSLQVHYDSRRLSQARLLDILVAAEDRLGGLDDFEIPSRVVHLPLSWKDPAIYQT
IDKYMQAVRDDAPWCPDNIEFIRRVNGLNGIDDVQKIVFDARYLVMGLGDVYLGAPVATP
VDPRHRLVTTKYNPARTWTPPNVVGIGGAYMCIYGMEGPGGYQLFGRTIQVWNTWRQTDA
FTDGKPWLLRFFDQIRFFPVSAEELVEWRRDFPLGRRAIRIEEETFRLSDYRRLLAENAE
SIAAFQSRRQAAFDAERADWEAKGEFARVEALSGVAEADDAVAAVEVPAGADLVEAPLGG
NVWKVLVEPGQAVEAGAVIAIIEAMKAECDVATPTAGVVSAVYAQPGQPIAAGAPVIAVT
PVAEAAA
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