SitesBLAST
Comparing GFF2304 FitnessBrowser__psRCH2:GFF2304 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)
43% 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 (= A621), I648 (≠ L714), L730 (≠ I791), D760 (= D818), N762 (≠ V820), F895 (≠ Y954)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y699), T641 (= T707), P653 (= P719), G656 (= G722), F658 (= F724), 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)
47% identity, 37% coverage: 1:438/1199 of query aligns to 1:454/681 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
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
47% identity, 36% coverage: 2:438/1199 of query aligns to 1:419/646 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:
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
44% identity, 37% coverage: 4:446/1199 of query aligns to 2:441/448 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)
45% identity, 36% coverage: 1:430/1199 of query aligns to 1:428/654 of P9WPQ3
- K322 (≠ L320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
43% identity, 37% coverage: 1:446/1199 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)
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:
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
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 (≠ V103) 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 (≠ 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)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
43% identity, 37% coverage: 1:438/1199 of query aligns to 1:433/447 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)
- binding magnesium ion: E276 (= E274), E288 (= E288)
Sites not aligning to the query:
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)
43% 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)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
42% identity, 37% coverage: 5:446/1199 of query aligns to 1:438/657 of 8sgxX
Sites not aligning to the query:
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
42% identity, 37% coverage: 4:446/1199 of query aligns to 39:482/1178 of Q05920
- K39 (= K4) modified: N6-acetyllysine
- K79 (≠ Q44) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ M112) modified: N6-acetyllysine
- K152 (= K116) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ R204) modified: N6-acetyllysine
- K434 (≠ P398) 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)
42% identity, 37% coverage: 4:446/1199 of query aligns to 39:482/1178 of P11498
- V145 (≠ Q109) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R120) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R233) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y267) to C: in PC deficiency
- R451 (≠ L415) 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
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
42% identity, 37% coverage: 4:446/1199 of query aligns to 8:451/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ L18), T26 (≠ R22), R46 (≠ I42), Q47 (= Q43), K48 (≠ Q44), A49 (= A45), D50 (= D46), R367 (≠ P363), R414 (≠ T409), E418 (= E413), R420 (≠ L415), R422 (≠ Y417)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K157), G168 (= G162), G169 (= G163), M173 (= M167), F207 (≠ Y201), I208 (= I202), P211 (≠ A205), H240 (≠ N234)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
42% identity, 37% coverage: 4:446/1199 of query aligns to 7:450/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K157), G167 (= G162), G168 (= G163), F206 (≠ Y201), Q236 (= Q231), H239 (≠ N234), E292 (= E288)
- binding coenzyme a: F21 (≠ L18), R22 (= R19), T25 (≠ R22), R45 (≠ I42), Q46 (= Q43), K47 (≠ Q44), A48 (= A45), D49 (= D46), E50 (= E47), R366 (≠ P363), R413 (≠ T409), A416 (≠ D412), R419 (≠ L415)
Sites not aligning to the query:
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
43% identity, 37% coverage: 1:446/1199 of query aligns to 1:441/444 of 3rupA
- 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 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 (= K200), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), K238 (= K236), L278 (≠ V276), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R340), D382 (= D387), I437 (≠ T442)
- 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)
43% identity, 37% coverage: 1:446/1199 of query aligns to 1:441/444 of 3g8cA
- 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 adenosine-5'-diphosphate: I157 (≠ M155), K159 (= K157), G164 (= G162), M169 (= M167), E201 (= E199), K202 (= K200), Y203 (= Y201), L204 (≠ I202), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), E288 (= E288), I437 (≠ T442)
- binding bicarbonate ion: K238 (= K236), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R340), D382 (= D387)
- binding magnesium ion: E276 (= E274), E288 (= E288)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
43% identity, 37% coverage: 1:446/1199 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)
43% identity, 37% coverage: 1:446/1199 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)
Query Sequence
>GFF2304 FitnessBrowser__psRCH2:GFF2304
MFDKLLIANRGAIACRILRTLRGLDVKSVAVYSEADAASLHIQQADEAHSLGEGPAAQTY
LVVEKILRIARETGASAIHPGYGFLSENAAFAEACEAAGIAFVGPTPEQLRMFGLKHTAR
ALAKQRGVPMLEGTELLDSLADALGAAEQVGYPVMLKSTAGGGGIGMRVCRSAAELAEAF
DAVKRLGQNNFSDAGVFIEKYIQRARHLEVQVFGDGRGEVIALGVRDCSVQRRNQKVLEE
TPAPNLPAGMAEALCEAAVKLAKAVSYRSAGTVEFVYDAEAEQFYFLEVNTRLQVEHGVT
EQVWGVDLVRWMIELAAGDLPPLVELARALKSSGHSIQARLYAEDPGRDFQPSPGLLTVV
DFPKGDGKALRIDTWVEAGCEIPPYFDPMVAKLITWAPDRESARAALDTALDETLLYGVE
SNRAYLRQILGYAPFAEGRPWTRCLEGLTYRATTFEVISAGTQTTVQDFPGRLGYWAVGV
PPSGPMDNRALRLGNALLGNPEDAAGLEITMSGPILRFNTDAVVAITGAEIPVKLDDAPQ
PMCTAILVKAGSTLAIGTIVGAGARSYLAVRGGLQVPDYLGSKSTFTLGQFGGHAGRALR
AGDVLHLAPLTDSACGASLPAALCSALPAVRELRVIYGPHGAPEYFTEGYIQTFFATDWE
VHFNSSRTGVRLIGPKPEWVRESGGEAGLHPSNIHDNPYAIGAVDFTGDMPVILGPDGPS
LGGFVCPVTIIEADLWQLGQLKAGDRVRFVPVDVASARQLAQAANIECARLAAAPVPCVP
VALQSPIVLDIGEADTRLVARLSGDTHLLLEIGAPELDLVLRFRGHALMQALEAKQLDGV
IDLTPGIRSLQVHYQPETLALQTLLDIVAGEWDAVCAAQDLKVPSRIVHLPLSWDDPACT
LAIEKYMTTVRKDAPWCPSNLEFIRRINDLPDLDEVYRTVFEASYLVMGLGDVYLGAPVA
TPLDPRHRLVTTKYNPARTWTAENSVGIGGAYMCVYGMEGPGGYQFVGRTLQMWNRYRAV
EAFGGLPWLLRFFDQIRFYPVSAEQLLKIRRDFPLGRYPLKIEQTELRLSDYQDFLAAEA
EGIDAFRRQQRAAFDAERQRWIASGQAHFESEEVAADLGEDAPLGSGLHGIESHIAGNLW
QVSVAEGARVEAGDVLVILESMKMEIPLTAPVAGVVKEVRAQPGSPVRAGQRVVVIEEA
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