SitesBLAST
Comparing H281DRAFT_03840 FitnessBrowser__Burk376:H281DRAFT_03840 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: 202:1196/1199 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 (= A617), I648 (≠ L712), L730 (vs. gap), D760 (= D818), N762 (≠ V820), F895 (≠ Y954)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y697), T641 (= T705), P653 (= P717), G656 (= G720), F658 (= F722), P943 (= P1001), G944 (= G1002), K1096 (= K1163)
- binding urea: D893 (= D952), Y937 (= Y996), G944 (= G1002), G945 (= G1003), Y946 (= Y1004)
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)
41% identity, 45% coverage: 1:535/1199 of query aligns to 1:528/681 of Q5LUF3
- F348 (= F350) binding
- W515 (≠ A522) mutation to L: No effect on holoenzyme formation.
Sites not aligning to the query:
- 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
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
40% identity, 45% coverage: 2:535/1199 of query aligns to 1:493/646 of 3n6rG
- active site: K115 (= K116), K157 (= K157), D180 (≠ S194), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R340)
Sites not aligning to the query:
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
42% identity, 37% coverage: 3:446/1199 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
44% identity, 37% coverage: 1:446/1199 of query aligns to 1:444/654 of P9WPQ3
- K322 (≠ P322) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
42% identity, 37% coverage: 2:445/1199 of query aligns to 5:446/670 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)
42% identity, 37% coverage: 2:445/1199 of query aligns to 63:504/728 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 (= G135) 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 (≠ A339) to R: in PA-1
- R399 (= R340) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P363) 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)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
42% identity, 37% coverage: 1:446/1199 of query aligns to 1:438/442 of 4mv4A
- active site: K116 (= K116), K159 (= K157), D193 (≠ S194), 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)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
42% identity, 37% coverage: 1:446/1199 of query aligns to 1:439/444 of 2vr1A
- active site: K116 (= K116), K159 (= K157), D194 (≠ S194), 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)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
42% identity, 37% coverage: 1:438/1199 of query aligns to 1:433/447 of 2vqdA
- active site: K116 (= K116), K159 (= K157), P196 (≠ S194), 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)
- binding magnesium ion: E276 (= E274), E288 (= E288)
Sites not aligning to the query:
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
40% identity, 37% coverage: 3:446/1199 of query aligns to 5:451/1150 of A0A0H3JRU9
- R21 (= R19) mutation to A: Complete loss of catalytic activity.
- K119 (= K116) binding
- K161 (= K157) binding
- H211 (= H207) binding
- E278 (= E274) binding
- K411 (≠ A406) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding
- 542 binding
- 580 A→T: Complete loss of catalytic activity.
- 614 R→A: Complete loss of catalytic activity.
- 621 Y→A: Complete loss of catalytic activity.
- 712 binding
- 741 binding
- 743 binding
- 838 Q→A: About 2.5-fold loss of catalytic activity.
- 876 T→A: Complete loss of catalytic activity.
- 879 S→A: About 2-fold loss of catalytic activity.
- 880 K→T: Complete loss of catalytic activity.
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)
41% identity, 37% coverage: 1:446/1199 of query aligns to 1:436/440 of 6oi8A
- active site: K116 (= K116), K159 (= K157), D191 (≠ S194), 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)
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)
41% identity, 37% coverage: 1:446/1199 of query aligns to 3:443/453 of 7kctA
- active site: E276 (= E274), E289 (= E288), N291 (= N290), E297 (= E296), R339 (= R340)
- binding adenosine-5'-diphosphate: K117 (= K116), 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 (≠ V276), E289 (= E288), R293 (= R292), Q295 (= Q294), V296 (= V295), E297 (= E296), R339 (= R340)
- binding bicarbonate ion: D116 (≠ L115), R119 (≠ T118)
- binding magnesium ion: E276 (= E274), E289 (= E288)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
41% identity, 37% coverage: 1:446/1199 of query aligns to 1:435/439 of 4mv3A
- active site: K116 (= K116), K159 (= K157), D190 (≠ S194), 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)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
41% identity, 37% coverage: 4:446/1199 of query aligns to 5:454/1129 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
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
42% identity, 37% coverage: 1:446/1199 of query aligns to 1:441/445 of 6ojhA
- active site: K116 (= K116), K159 (= K157), D196 (≠ S194), 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)
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)
42% identity, 37% coverage: 1:446/1199 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
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
41% identity, 37% coverage: 1:446/1199 of query aligns to 1:427/430 of 4mv1A
- active site: K116 (= K116), K159 (= K157), D182 (≠ S194), 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)
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)
42% identity, 37% coverage: 1:446/1199 of query aligns to 1:441/446 of 6oi9A
- active site: E276 (= E274), E288 (= E288), N290 (= N290), E296 (= E296), R338 (= R340)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K157), M169 (= M167), E201 (= E199), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), E276 (= E274), L278 (≠ V276), E288 (= E288), I437 (≠ T442)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
42% identity, 37% coverage: 1:446/1199 of query aligns to 1:441/446 of 2w71A
- active site: K116 (= K116), K159 (= K157), D196 (≠ S194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K157), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), I437 (≠ T442)
Query Sequence
>H281DRAFT_03840 FitnessBrowser__Burk376:H281DRAFT_03840
MFEKILIANRGAIACRILRTLRELNVTGVSVFSEADRASRHVSEAPIAHELGDGPAAMTY
LDSTKILEIARCEGVQAIHPGYGFLSENAAFGEACEAAGIAFIGPTPAQLRAFGLKHTAR
EIAGEQGVPMLNGTGLLEDLPAALNAAESIGYPVMLKSTAGGGGIGMRVCWHADELSAHF
DAVKRLGENNFSDSGVFLEKYIERARHLEVQVFGDGKGDAIALGVRDCSVQRRNQKVLEE
TPAPCLPEGIAQALCDAAVKLAKAVDYRSAGTVEFVYDSTAQQFYFLEVNTRLQVEHGVT
EQVWGVDLVRWMIELAAGTLAPLNELAASLTPRGHAIQARLYAEDPGRDFIPSPGLLTHV
AFPQADGSALRIDTWIESGCEVPPYFDPMLAKIIAWSPTREEARHALNDALQNTRIFGVE
TNRDYLRQILDDEPFASGEPWTRCLEGLKYRASTIEVVSGGTQTTVQDFPGRQGFWAVGI
PPSGPMDDRAMRLGNRLLGNAPEAAALEITMSGPTLRFNTDAVIAITGAEIPVLLDDVTQ
PLNTSVYVRAGSVLALGTIRGAGARAYLCVRGGLDVALYLGSRSTFTLGQFGGHGGRAVR
AGDVLHLYPLQDTQAGAALSNVPTLESVRTIRVIYGPHGAPEYFSARYIEQFLDTEWEIH
FNSSRTGVRLIGPKPEWAREDGGEAGLHPSNIHDNPYAVGAVDFTGDMPVILGPDGPSLG
GFVCPVTIIEADLWHIGQLKAGDKVRFVPVEIGHAREAARERIRELESLAITQCAPVERR
SSLTSPIVLDSGAADERLVARLSGDTHLLLEIGPPELDLVSRFRGHALMQALEAKALPGV
IDLTPGIRSLQIHYRPEDLSLAQLLGIVGEAWEQVLLMKDLRVPSRVVHIPLSWDDPACQ
LAIEKYMTTVRKDAPWCPSNLEFIRRINDLESIDAVRRIVFDANYLVMGLGDVYLGAPVA
TPLDPRHRLVTTKYNPARTWTAENSVGIGGAYLCVYGMEGPGGYQFVGRTLQMWNRYRKV
ADFAGQPYLLRFFDQIRFYEVSSEELLRIRADFPLGRYPLRIEESELSLPDYQAFLASES
ASIEEFRSRQQAAFEAERERWREAGTSEEAIEAPVAEDAQLAPLEDGEVSVDSEIAGSLW
QVKVKPGDVVAADDILLIIESMKMEISVCAPCAGTVGEIYVGPGSPVRAGQRIAVIERH
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