SitesBLAST
Comparing 8500054 FitnessBrowser__Miya:8500054 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)
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)
36% identity, 99% coverage: 7:472/472 of query aligns to 6:437/453 of 7kctA
- active site: E276 (= E300), E289 (= E313), N291 (= N315), E297 (= E321), R339 (= R369)
- binding adenosine-5'-diphosphate: K117 (= K121), L157 (= L171), K159 (= K173), G164 (= G178), G165 (= G179), G166 (= G180), I169 (= I183), E201 (= E215), Y203 (≠ R217), I204 (= I218), H209 (= H223), Q233 (= Q248), Q237 (= Q253), K238 (= K254), I278 (= I302), E289 (= E313), R293 (= R317), Q295 (= Q319), V296 (= V320), E297 (= E321), R339 (= R369)
- binding bicarbonate ion: D116 (= D120), R119 (≠ N123)
- binding magnesium ion: E276 (= E300), E289 (= E313)
7ybuA Human propionyl-coenzyme a carboxylase
35% identity, 97% coverage: 7:463/472 of query aligns to 7:438/670 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)
35% identity, 97% coverage: 7:463/472 of query aligns to 65:496/728 of P05165
- A75 (= A17) to P: in PA-1; dbSNP:rs794727479
- R77 (= R19) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A80) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I108) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ R141) to E: in PA-1
- M229 (≠ I183) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q253) to R: in PA-1
- D368 (= D338) to G: in PA-1
- M373 (≠ Q343) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G349) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ Y368) to R: in PA-1
- R399 (= R369) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P392) 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)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
36% identity, 96% coverage: 7:460/472 of query aligns to 4:426/447 of 2vqdA
- active site: K116 (= K121), K159 (= K173), P196 (≠ E210), H209 (= H223), R235 (≠ T250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K121), I157 (≠ L171), K159 (= K173), G164 (= G178), G166 (= G180), F203 (≠ R217), L204 (≠ I218), H209 (= H223), Q233 (= Q248), H236 (≠ G251), L278 (≠ I302), E288 (= E313)
- binding magnesium ion: E276 (= E300), E288 (= E313)
Sites not aligning to the query:
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
34% identity, 99% coverage: 7:472/472 of query aligns to 2:435/448 of 2vpqB
- active site: V116 (≠ N123), K156 (= K173), H206 (= H223), R232 (≠ T250), T271 (= T298), E273 (= E300), E287 (= E313), N289 (= N315), R291 (= R317), E295 (= E321), R337 (= R369)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K121), I154 (≠ L171), K156 (= K173), G161 (= G178), G163 (= G180), I166 (= I183), F200 (≠ R217), I201 (= I218), E273 (= E300), I275 (= I302), M286 (= M312), E287 (= E313)
- binding magnesium ion: E273 (= E300), E287 (= E313)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:411/444 of 2vr1A
- active site: K116 (= K121), K159 (= K173), D194 (≠ E210), H207 (= H223), R233 (≠ T250), T272 (= T298), E274 (= E300), E286 (= E313), N288 (= N315), R290 (= R317), E294 (= E321), R336 (= R369)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K173), R165 (≠ G179), M167 (= M181), Y201 (≠ R217), L202 (≠ I218), E274 (= E300), L276 (≠ I302), E286 (= E313), N288 (= N315)
Sites not aligning to the query:
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
34% identity, 97% coverage: 8:464/472 of query aligns to 1:420/657 of 8sgxX
Sites not aligning to the query:
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
34% identity, 93% coverage: 7:447/472 of query aligns to 4:410/442 of 4mv4A
- active site: K116 (= K121), K159 (= K173), D193 (≠ E210), H206 (= H223), R232 (≠ T250), T271 (= T298), E273 (= E300), E285 (= E313), N287 (= N315), R289 (= R317), E293 (= E321), R335 (= R369)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K173), G164 (= G179), M166 (= M181), E198 (= E215), Y200 (≠ R217), L201 (≠ I218), H233 (≠ G251), L275 (≠ I302), E285 (= E313)
- binding magnesium ion: E273 (= E300), E285 (= E313)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
36% identity, 92% coverage: 7:438/472 of query aligns to 39:456/1178 of Q05920
- K39 (= K7) modified: N6-acetyllysine
- K79 (≠ I47) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ E117) modified: N6-acetyllysine
- K152 (= K121) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ D220) modified: N6-acetyllysine
- K434 (= K427) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
- 589 modified: N6-acetyllysine
- 717 modified: N6-acetyllysine
- 748 modified: N6-acetyllysine; K→Q: Reduced pyruvate carboxylase activity.
- 892 modified: N6-acetyllysine
- 969 modified: N6-acetyllysine
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
36% identity, 92% coverage: 7:438/472 of query aligns to 39:456/1178 of P11498
- V145 (= V114) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (≠ K125) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (≠ T250) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y293) to C: in PC deficiency
- R451 (= R433) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
Sites not aligning to the query:
- 572 binding
- 583 R → L: in PC deficiency; dbSNP:rs119103242
- 610 A → T: in PC deficiency; mild; dbSNP:rs28940589
- 631 R → Q: in PC deficiency; dbSNP:rs113994145
- 741 binding via carbamate group; modified: N6-carboxylysine
- 743 M → I: in PC deficiency; mild; dbSNP:rs28940590
- 771 binding
- 773 binding
- 1077 mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- 1131:1133 natural variant: Missing (in PC deficiency)
- 1144 modified: N6-biotinyllysine
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
36% identity, 92% coverage: 7:438/472 of query aligns to 7:424/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K173), G167 (= G178), G168 (= G179), F206 (≠ R217), Q236 (= Q248), H239 (≠ G251), E292 (= E313)
- binding coenzyme a: F21 (≠ V21), R22 (≠ Q22), T25 (≠ R25), R45 (≠ V45), Q46 (≠ R46), K47 (≠ I47), A48 (= A48), D49 (≠ R49), E50 (= E50), R366 (= R394), R413 (vs. gap), A416 (= A430), R419 (= R433)
Sites not aligning to the query:
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
36% identity, 92% coverage: 7:438/472 of query aligns to 8:425/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ V21), T26 (≠ R25), R46 (≠ V45), Q47 (≠ R46), K48 (≠ I47), A49 (= A48), D50 (≠ R49), R367 (= R394), R414 (vs. gap), E418 (= E431), R420 (= R433), R422 (= R435)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K173), G168 (= G178), G169 (= G179), M173 (≠ I183), F207 (≠ R217), I208 (= I218), P211 (≠ F221), H240 (≠ G251)
Sites not aligning to the query:
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)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:408/440 of 6oi8A
- active site: K116 (= K121), K159 (= K173), D191 (≠ E210), H204 (= H223), R230 (≠ T250), T269 (= T298), E271 (= E300), E283 (= E313), N285 (= N315), R287 (= R317), E291 (= E321), R333 (= R369)
- 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 (≠ L171), K159 (= K173), M164 (= M181), E196 (= E215), Y198 (≠ R217), L199 (≠ I218), H204 (= H223), Q228 (= Q248), E271 (= E300), L273 (≠ I302), E283 (= E313)
Sites not aligning to the query:
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:413/449 of P24182
- R19 (≠ Q22) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ K26) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K121) binding
- K159 (≠ V172) binding
- GG 165:166 (= GG 178:179) binding
- EKYL 201:204 (≠ EQRI 215:218) binding
- H209 (= H223) binding
- H236 (≠ G251) binding
- K238 (= K254) binding
- E276 (= E300) binding ; binding
- E288 (= E313) binding ; binding
- R292 (= R317) active site; binding
- V295 (= V320) binding
- E296 (= E321) mutation to A: Severe reduction in catalytic activity.
- R338 (= R369) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ P395) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (≠ A398) 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)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:413/444 of 3rupA
- active site: K116 (= K121), K159 (≠ V172), D196 (≠ E210), H209 (= H223), R235 (≠ T250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding adenosine-5'-diphosphate: Y82 (= Y85), G83 (= G86), K116 (= K121), K159 (≠ V172), G164 (= G177), G164 (= G177), G165 (= G178), G166 (= G179), R167 (≠ G180), M169 (≠ G182), F193 (= F207), E201 (= E215), K202 (≠ Q216), Y203 (≠ R217), L204 (≠ I218), H209 (= H223), Q233 (= Q248), H236 (≠ G251), K238 (= K254), L278 (≠ I302), E288 (= E313), R292 (= R317), V295 (= V320), E296 (= E321), R338 (= R369), D382 (= D416)
- binding calcium ion: E87 (= E90), E276 (= E300), E288 (= E313), E288 (= E313), N290 (= N315)
Sites not aligning to the query:
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:413/444 of 3g8cA
- active site: K116 (= K121), K159 (≠ V172), D196 (≠ E210), H209 (= H223), R235 (≠ T250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding adenosine-5'-diphosphate: I157 (≠ V170), K159 (≠ V172), G164 (= G177), M169 (≠ G182), E201 (= E215), K202 (≠ Q216), Y203 (≠ R217), L204 (≠ I218), Q233 (= Q248), H236 (≠ G251), L278 (≠ I302), E288 (= E313)
- binding bicarbonate ion: K238 (= K254), R292 (= R317), Q294 (= Q319), V295 (= V320), E296 (= E321)
- binding biotin: Y82 (= Y85), F84 (= F87), R292 (= R317), V295 (= V320), R338 (= R369), D382 (= D416)
- binding magnesium ion: E276 (= E300), E288 (= E313)
Sites not aligning to the query:
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
33% identity, 93% coverage: 7:447/472 of query aligns to 6:415/447 of 3jzfB
- active site: K118 (= K121), K161 (≠ V172), D198 (≠ E210), H211 (= H223), R237 (≠ T250), T276 (= T298), E278 (= E300), E290 (= E313), N292 (= N315), R294 (= R317), E298 (= E321), R340 (= R369)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K121), K161 (≠ V172), A162 (≠ K173), G166 (= G177), G168 (= G179), R169 (≠ G180), G170 (≠ M181), M171 (≠ G182), Y201 (≠ L213), E203 (= E215), K204 (≠ Q216), Y205 (≠ R217), H211 (= H223), H238 (≠ G251), L280 (≠ I302), I289 (≠ M312), E290 (= E313)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:413/445 of 3jziA
- active site: K116 (= K121), K159 (≠ V172), D196 (≠ E210), H209 (= H223), R235 (≠ T250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K121), K159 (≠ V172), A160 (≠ K173), G164 (= G177), G165 (= G178), M169 (≠ G182), Y199 (≠ L213), E201 (= E215), K202 (≠ Q216), Y203 (≠ R217), H209 (= H223), Q233 (= Q248), H236 (≠ G251), L278 (≠ I302), I287 (≠ M312), E288 (= E313)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:413/445 of 2w6oA
- active site: K116 (= K121), K159 (≠ V172), D196 (≠ E210), H209 (= H223), R235 (≠ T250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (≠ V172), K202 (≠ Q216), Y203 (≠ R217), L204 (≠ I218), L278 (≠ I302)
Sites not aligning to the query:
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
33% identity, 93% coverage: 7:447/472 of query aligns to 4:413/445 of 2w6nA
- active site: K116 (= K121), K159 (≠ V172), D196 (≠ E210), H209 (= H223), R235 (≠ T250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ V170), K159 (≠ V172), M169 (≠ G182), E201 (= E215), K202 (≠ Q216), Y203 (≠ R217), L278 (≠ I302)
Query Sequence
>8500054 FitnessBrowser__Miya:8500054
MQTKDHKVLVANRGEIAIRIVQACRKLGLAFTCVYTAEDAASGHVRIARELGGDKSLCRV
SSYHDANELMAVADDAGATAVHPGYGFFAEDYRFARRVSQRDRKLIFIGPSWRVIRELGD
KINTKRLARSLGVPTVPGSDRPIYDEMEAEKVAQSLFEFQEQQGIRKPLVLVKASAGGGG
MGIEEVYDIDLFRSVYRRIRNYALRQFKDEGVLIEQRIRDFNHLEVQVVSDRSGRNPVHF
GTRNCSIQSTGLQKRIEIAPGFDPSSIEYGFDAAQVLRDITQHSLAMARKVGYDNVGTWE
WIVTRDGRPFLMEVNTRIQVENGVSATIARVRGQKGVDLIAEQIRIGLGEPLGYGQEDVT
FEGVGIEYRLIAEDPDNRFTPWVGRVDGFGWPERPWLAMHTHVPSDDPYDIPTEFDPNLA
LAIIWGKDLAEARERGVEFLDTLVLEGANNAGEPLRSNVRFLRDNTGRILKF
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