SitesBLAST
Comparing WP_038218466.1 NCBI__GCF_000745855.1:WP_038218466.1 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)
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)
58% identity, 100% coverage: 1:683/684 of query aligns to 1:680/681 of Q5LUF3
- F348 (= F348) binding biotin
- W515 (≠ F507) mutation to L: No effect on holoenzyme formation.
- L599 (= L602) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L605) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M606) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K650) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
56% identity, 100% coverage: 2:683/684 of query aligns to 1:645/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R338), G519 (≠ I546)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M649), K612 (= K650)
7ybuA Human propionyl-coenzyme a carboxylase
49% identity, 100% coverage: 2:683/684 of query aligns to 5:669/670 of 7ybuA
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)
49% identity, 100% coverage: 2:683/684 of query aligns to 63:727/728 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 (≠ D136) to E: in PA-1
- M229 (≠ L168) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q236) 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 (= C337) to R: in PA-1
- R399 (= R338) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P361) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ V481) natural variant: Missing (in PA-1)
- V551 (≠ G500) to F: in dbSNP:rs61749895
- W559 (≠ Q506) to L: in PA-1; dbSNP:rs118169528
- G631 (= G587) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G624) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K650) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A668) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
47% identity, 99% coverage: 5:683/684 of query aligns to 1:656/657 of 8sgxX
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
49% identity, 100% coverage: 2:683/684 of query aligns to 1:590/591 of 3n6rA
- active site: K115 (= K116), H138 (≠ A144), R164 (= R189), T203 (= T273), E205 (= E275), E218 (= E288), N220 (= N290), R222 (= R292), E226 (= E296), R268 (= R338), G464 (≠ I546)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M649), K557 (= K650)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
43% identity, 99% coverage: 1:680/684 of query aligns to 1:649/654 of P9WPQ3
- K322 (= K320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
39% identity, 99% coverage: 4:683/684 of query aligns to 6:648/651 of 8j78I
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
50% identity, 66% coverage: 3:456/684 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R338)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ L168), F200 (= F202), I201 (≠ V203), E273 (= E275), I275 (≠ V277), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E275), E287 (= E288)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:438/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R338)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (≠ L168), Y201 (≠ F202), L202 (≠ V203), E274 (= E275), L276 (≠ V277), E286 (= E288), N288 (= N290), I435 (≠ T450)
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)
49% identity, 67% coverage: 1:456/684 of query aligns to 3:445/453 of 7kctA
- active site: E276 (= E275), E289 (= E288), N291 (= N290), E297 (= E296), R339 (= R338)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (≠ M156), K159 (= K158), G164 (= G163), G165 (= G164), G166 (= G165), I169 (≠ L168), E201 (= E200), Y203 (≠ F202), I204 (≠ V203), H209 (= H208), Q233 (= Q232), Q237 (= Q236), K238 (= K237), I278 (≠ V277), E289 (= E288), R293 (= R292), Q295 (= Q294), V296 (= V295), E297 (= E296), R339 (= R338)
- binding bicarbonate ion: D116 (= D115), R119 (≠ A118)
- binding magnesium ion: E276 (= E275), E289 (= E288)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K158), G164 (= G163), G164 (= G163), G165 (= G164), G166 (= G165), R167 (≠ K166), M169 (≠ L168), F193 (= F192), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), K238 (= K237), L278 (≠ V277), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R338), D382 (= D395), I437 (≠ T450)
- binding calcium ion: E87 (= E87), E276 (= E275), E288 (= E288), E288 (= E288), N290 (= N290)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/444 of 3g8cA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: I157 (≠ M156), K159 (= K158), G164 (= G163), M169 (≠ L168), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (≠ V203), Q233 (= Q232), H236 (= H235), L278 (≠ V277), E288 (= E288), I437 (≠ T450)
- binding bicarbonate ion: K238 (= K237), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R338), D382 (= D395)
- binding magnesium ion: E276 (= E275), E288 (= E288)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/445 of 3jziA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K158), A160 (= A159), G164 (= G163), G165 (= G164), M169 (≠ L168), Y199 (≠ F198), E201 (= E200), K202 (= K201), Y203 (≠ F202), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ V277), 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)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/445 of 2w6oA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K158), K202 (= K201), Y203 (≠ F202), L204 (≠ V203), L278 (≠ V277), I437 (≠ T450)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/445 of 2w6nA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M156), K159 (= K158), M169 (≠ L168), E201 (= E200), K202 (= K201), Y203 (≠ F202), L278 (≠ V277)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/445 of 2v59A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K158), Y203 (≠ F202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ V277), I437 (≠ T450)
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)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/446 of 6oi9A
- active site: E276 (= E275), E288 (= E288), N290 (= N290), E296 (= E296), R338 (= R338)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (≠ L168), E201 (= E200), Y203 (≠ F202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), E276 (= E275), L278 (≠ V277), E288 (= E288), I437 (≠ T450)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (≠ F202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ V277), I437 (≠ T450)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
49% identity, 66% coverage: 1:453/684 of query aligns to 1:440/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ M156), K159 (= K158), G166 (= G165), M169 (≠ L168), E201 (= E200), Y203 (≠ F202), L204 (≠ V203), L278 (≠ V277)
Query Sequence
>WP_038218466.1 NCBI__GCF_000745855.1:WP_038218466.1
MFKKILIANRGEIACRVIKTARKLGIRTVAVYSDADKDARHVELADEAVHIGAAPSRESY
LLADRIIEACKKTGAEAVHPGYGFLSENEGFAKRVEEEGIVFIGPKHYSIAAMGDKIASK
KLAGEAKVNTIPGYNDAIDTAEQAVEIAKGIGYPVMIKASAGGGGKGLRVAFNDKEALEG
FTSCRNEARNSFGDDRVFIEKFVEEPRHIEIQVLGDAHGNVIYLNERECSIQRRHQKVIE
EAPSPFISEATRKAMGEQAVALAKAVKYQSAGTVEFVVGKDQSFYFLEMNTRLQVEHPVT
ECITGLDLVELMIRVAAGEKLPLAQKDVQRNGWAIECRINAEDPFRNFLPSTGRLVRFQP
PAEQLAAAEPTPADAYGVRVDTGVYEGGEIPMYYDSMIAKLIVHGRDRNHAIALMREALN
GFVIRGIHSNIPFQAALLAHPKFVSGEFNTGFIAEHYAHGFRAEDVPHADPDFLVALAAY
VHRRYRARASGISGQLEGHGVKVGEQFVVVTLAADGQHVHTPVSVTDFQGKTGSSAVQVG
ANSYRIDSLSPLGSIRVEGRVNGQPFTAQVERGAGKNPLALRVQHNGTQIEAMVLSPLGA
RLLALMPYKAPPDMSKFLLSPMPGLLVDVAVQEGQQVQAGEKLAVIEAMKMENVLFAAQD
GVVGKIAAAKGESLAVDQVIMEFA
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