SitesBLAST
Comparing 350977 FitnessBrowser__Btheta:350977 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)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
54% identity, 87% coverage: 3:441/503 of query aligns to 1:441/448 of 2vpqB
- active site: V116 (≠ E117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E287), N289 (= N289), R291 (= R291), E295 (= E295), R337 (= R337)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ Y201), I201 (= I202), E273 (= E274), I275 (≠ M276), M286 (≠ L286), E287 (= E287)
- binding magnesium ion: E273 (= E274), E287 (= E287)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
51% identity, 88% coverage: 1:444/503 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K115), K159 (= K157), D193 (= D194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (≠ K165), M166 (= M167), E198 (= E199), Y200 (= Y201), L201 (≠ I202), H233 (≠ N234), L275 (≠ M276), E285 (= E287)
- binding magnesium ion: E273 (= E274), E285 (= E287)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
50% identity, 88% coverage: 1:444/503 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K115), K159 (= K157), D190 (= D194), H203 (= H207), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E287), N284 (= N289), R286 (= R291), E290 (= E295), R332 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (= M167), E195 (= E199), Y197 (= Y201), L198 (≠ I202), E270 (= E274), L272 (≠ M276), E282 (= E287)
- binding bicarbonate ion: R286 (= R291), Q288 (= Q293), V289 (= V294)
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)
50% identity, 88% coverage: 1:444/503 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K115), K159 (= K157), D191 (= D194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), 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 (≠ M155), K159 (= K157), M164 (= M167), E196 (= E199), Y198 (= Y201), L199 (≠ I202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (≠ M276), E283 (= E287), I432 (≠ T437)
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)
51% identity, 88% coverage: 1:441/503 of query aligns to 3:443/453 of 7kctA
- active site: E276 (= E274), E289 (= E287), N291 (= N289), E297 (= E295), R339 (= R337)
- binding adenosine-5'-diphosphate: K117 (= K115), L157 (≠ M155), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), I169 (≠ M167), E201 (= E199), Y203 (= Y201), I204 (= I202), H209 (= H207), Q233 (= Q231), Q237 (= Q235), K238 (= K236), I278 (≠ M276), E289 (= E287), R293 (= R291), Q295 (= Q293), V296 (= V294), E297 (= E295), R339 (= R337)
- binding bicarbonate ion: D116 (≠ I114), R119 (≠ E117)
- binding magnesium ion: E276 (= E274), E289 (= E287)
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)
50% identity, 87% coverage: 1:440/503 of query aligns to 1:461/681 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
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)
51% identity, 88% coverage: 1:444/503 of query aligns to 1:444/448 of P43873
- K116 (= K115) binding
- K159 (= K157) binding
- EKYL 201:204 (≠ EKYI 199:202) binding
- E276 (= E274) binding ; binding
- E288 (= E287) binding ; binding
- N290 (= N289) 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
51% identity, 88% coverage: 1:444/503 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K115), K159 (= K157), D196 (= D194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding calcium ion: E276 (= E274), E288 (= E287), N290 (= N289)
- 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 (≠ M276), E288 (= E287), I437 (≠ T437)
7ybuA Human propionyl-coenzyme a carboxylase
46% identity, 98% coverage: 4:497/503 of query aligns to 7:508/670 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, 98% coverage: 4:497/503 of query aligns to 65:566/728 of P05165
- A75 (= A14) to P: in PA-1; dbSNP:rs794727479
- R77 (= R16) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A76) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I102) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ T135) to E: in PA-1
- M229 (= M167) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1
- D368 (= D306) to G: in PA-1
- M373 (= M311) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G317) to V: in PA-1; dbSNP:rs794727087
- C398 (= C336) to R: in PA-1
- R399 (= R337) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P360) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ A465) natural variant: Missing (in PA-1)
- V551 (= V484) to F: in dbSNP:rs61749895
- W559 (= W490) to L: in PA-1; dbSNP:rs118169528
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 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)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
49% identity, 88% coverage: 1:444/503 of query aligns to 1:430/430 of 4mv1A
- active site: K116 (= K115), K159 (= K157), D182 (= D194), H195 (= H207), R221 (= R233), T260 (= T272), E262 (= E274), E274 (= E287), N276 (= N289), R278 (= R291), E282 (= E295), R324 (= R337)
- binding adenosine-5'-diphosphate: K159 (= K157), E187 (= E199), K188 (= K200), Y189 (= Y201), L190 (≠ I202), L264 (≠ M276)
- binding phosphate ion: K224 (= K236), R278 (= R291), Q280 (= Q293), V281 (= V294), E282 (= E295)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
48% identity, 88% coverage: 1:444/503 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K115), K159 (= K157), D194 (= D194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E287), N288 (= N289), R290 (= R291), E294 (= E295), R336 (= R337)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (≠ K165), M167 (= M167), Y201 (= Y201), L202 (≠ I202), E274 (= E274), L276 (≠ M276), E286 (= E287), N288 (= N289), I435 (≠ T437)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
49% identity, 87% coverage: 3:440/503 of query aligns to 2:426/646 of 3n6rG
- active site: K115 (= K115), K157 (= K157), D180 (= D194), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E287), N275 (= N289), R277 (= R291), E281 (= E295), R323 (= R337)
Sites not aligning to the query:
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
47% identity, 88% coverage: 1:444/503 of query aligns to 1:444/447 of 2vqdA
- active site: K116 (= K115), K159 (= K157), P196 (≠ D194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K115), I157 (≠ M155), K159 (= K157), G164 (= G162), G166 (= G164), F203 (≠ Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ M276), E288 (= E287), I437 (≠ T437)
- binding magnesium ion: E276 (= E274), E288 (= E287)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
48% identity, 90% coverage: 2:454/503 of query aligns to 37:495/1178 of Q05920
- K39 (= K4) modified: N6-acetyllysine
- K79 (≠ Y44) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (= K111) modified: N6-acetyllysine
- K152 (= K115) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N204) modified: N6-acetyllysine
- K434 (≠ R393) 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
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
51% identity, 87% coverage: 1:440/503 of query aligns to 1:437/456 of 8hz4A
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
47% identity, 90% coverage: 2:454/503 of query aligns to 37:495/1178 of P11498
- V145 (≠ I108) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R119) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R233) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y267) to C: in PC deficiency
- R451 (≠ K410) 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)
47% identity, 90% coverage: 2:454/503 of query aligns to 5:463/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K157), G167 (= G162), G168 (= G163), F206 (≠ Y201), Q236 (= Q231), H239 (≠ N234), E292 (= E287)
- binding coenzyme a: F21 (= F18), R22 (= R19), T25 (≠ R22), R45 (≠ V42), Q46 (≠ R43), K47 (≠ Y44), A48 (= A45), D49 (≠ E46), E50 (= E47), R366 (≠ E358), R413 (= R404), A416 (≠ R407), R419 (≠ K410), Q462 (= Q453)
Sites not aligning to the query:
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
47% identity, 90% coverage: 2:454/503 of query aligns to 6:464/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (= F18), T26 (≠ R22), R46 (≠ V42), Q47 (≠ R43), K48 (≠ Y44), A49 (= A45), D50 (≠ E46), R367 (≠ E358), R414 (= R404), E418 (= E408), R420 (≠ K410), R422 (≠ L412), A462 (≠ R452), Q463 (= Q453)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K157), G168 (= G162), G169 (= G163), M173 (= M167), F207 (≠ Y201), I208 (= I202), P211 (= P205), H240 (≠ N234)
Sites not aligning to the query:
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
48% identity, 87% coverage: 2:440/503 of query aligns to 5:442/445 of 3ouzA
- active site: K161 (= K157), G167 (= G163), G168 (= G164), H211 (= H207), K240 (= K236), T276 (= T272), E278 (= E274), E291 (= E287), N293 (= N289), V298 (= V294), E299 (= E295), R340 (= R337)
- binding adenosine-5'-diphosphate: K119 (= K115), I159 (≠ M155), K161 (= K157), G166 (= G162), G168 (= G164), M171 (= M167), E203 (= E199), Y205 (= Y201), I206 (= I202), H211 (= H207), Q235 (= Q231), L280 (≠ M276), E291 (= E287), T439 (= T437)
- binding magnesium ion: E278 (= E274), E291 (= E287)
Query Sequence
>350977 FitnessBrowser__Btheta:350977
MIKKILVANRGEIAMRIFRTCRVMDISTVAVYTHVDRGALHVRYAEEAYCISNSPEDTSY
LKPELILAIAKKTGAAIHPGYGFLSENADFARRCEEEGVIFIGPGADIIAKMGIKTEARK
IMREAGLPIVPGTETPVQGIEEVKKVAKEVGYPIMLKALAGGGGKGMRLVRSEEEAETAL
RLSQSEAGTSFGNDAVYIEKYIENPHHIEVQIMGDKYGNVVHLGERECSIQRRNQKVIEE
SPSPFVKDETRKKMLKVAVEACKRIGYYSAGTLEFMMDKDQNFYFLEMNTRLQVEHPVTE
ECTGVDLVRDMITVAAGNPLPYKQEDIKFSGAAIECRIYAEDPENNFMPSPGVITVREAP
EGRNLRLDSAAYAGFEVSLHYDPMIAKLCCWGRTRESAISNMARALREYKILGIKTTIPF
HQRVLKNAAFLEGKYDTTFIDTRFDKEDLKRRQNTDPTVAVIAAAVRHYEREKEAASRAT
TLPVVGESLWKYYGKLQMTANNY
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