SitesBLAST
Comparing RR42_RS29420 FitnessBrowser__Cup4G11:RR42_RS29420 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)
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, 97% coverage: 7:653/666 of query aligns to 2:653/654 of P9WPQ3
- K322 (≠ P325) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
40% identity, 97% coverage: 7:653/666 of query aligns to 5:670/670 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)
40% identity, 97% coverage: 7:653/666 of query aligns to 63:728/728 of P05165
- A75 (= A19) to P: in PA-1; dbSNP:rs794727479
- R77 (= R21) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A82) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I108) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G141) to E: in PA-1
- M229 (= M173) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q241) to R: in PA-1
- D368 (= D312) to G: in PA-1
- M373 (≠ Q317) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G323) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V342) to R: in PA-1
- R399 (= R343) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P366) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L469) natural variant: Missing (in PA-1)
- V551 (≠ P488) to F: in dbSNP:rs61749895
- W559 (≠ Y496) to L: in PA-1; dbSNP:rs118169528
- G631 (= G562) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G593) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K619) modified: N6-biotinyllysine; by HLCS
- C712 (≠ V637) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
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)
40% identity, 97% coverage: 7:653/666 of query aligns to 2:681/681 of Q5LUF3
- F348 (= F353) binding
- W515 (≠ Y496) mutation to L: No effect on holoenzyme formation.
- L599 (≠ A581) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (vs. gap) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (vs. gap) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K619) modified: N6-biotinyllysine
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
50% identity, 66% coverage: 8:447/666 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ G123), K156 (= K163), H206 (= H213), R232 (= R239), T271 (= T278), E273 (= E280), E287 (= E293), N289 (= N295), R291 (= R297), E295 (= E301), R337 (= R343)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K121), I154 (≠ M161), K156 (= K163), G161 (= G168), G163 (= G170), I166 (≠ M173), F200 (≠ A207), I201 (≠ V208), E273 (= E280), I275 (≠ L282), M286 (= M292), E287 (= E293)
- binding magnesium ion: E273 (= E280), E287 (= E293)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:438/444 of 2vr1A
- active site: K116 (= K121), K159 (= K163), D194 (≠ P200), H207 (= H213), R233 (= R239), T272 (= T278), E274 (= E280), E286 (= E293), N288 (= N295), R290 (= R297), E294 (= E301), R336 (= R343)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K163), R165 (= R171), M167 (= M173), Y201 (≠ A207), L202 (≠ V208), E274 (= E280), L276 (= L282), E286 (= E293), N288 (= N295), I435 (≠ T441)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
39% identity, 97% coverage: 7:653/666 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K121), K157 (= K163), D180 (≠ E192), H193 (= H213), R219 (= R239), T258 (= T278), E260 (= E280), E273 (= E293), N275 (= N295), R277 (= R297), E281 (= E301), R323 (= R343), G519 (= G532)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M618), K612 (= K619)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
53% identity, 67% coverage: 7:449/666 of query aligns to 2:442/456 of 8hz4A
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
50% identity, 62% coverage: 7:421/666 of query aligns to 2:414/442 of 4mv4A
- active site: K116 (= K121), K159 (= K163), D193 (≠ P200), H206 (= H213), R232 (= R239), T271 (= T278), E273 (= E280), E285 (= E293), N287 (= N295), R289 (= R297), E293 (= E301), R335 (= R343)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K163), G164 (= G168), M166 (= M173), E198 (= E205), Y200 (≠ A207), L201 (≠ V208), H233 (= H240), L275 (= L282), E285 (= E293)
- binding magnesium ion: E273 (= E280), E285 (= E293)
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, 62% coverage: 7:421/666 of query aligns to 2:412/440 of 6oi8A
- active site: K116 (= K121), K159 (= K163), D191 (≠ P200), H204 (= H213), R230 (= R239), T269 (= T278), E271 (= E280), E283 (= E293), N285 (= N295), R287 (= R297), E291 (= E301), R333 (= R343)
- 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 (≠ M161), K159 (= K163), M164 (= M173), E196 (= E205), Y198 (≠ A207), L199 (≠ V208), H204 (= H213), Q228 (= Q237), E271 (= E280), L273 (= L282), E283 (= E293)
Sites not aligning to the query:
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
50% identity, 62% coverage: 7:421/666 of query aligns to 2:411/439 of 4mv3A
- active site: K116 (= K121), K159 (= K163), D190 (≠ P200), H203 (= H213), R229 (= R239), T268 (= T278), E270 (= E280), E282 (= E293), N284 (= N295), R286 (= R297), E290 (= E301), R332 (= R343)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K163), M163 (= M173), E195 (= E205), Y197 (≠ A207), L198 (≠ V208), E270 (= E280), L272 (= L282), E282 (= E293)
- binding bicarbonate ion: R286 (= R297), Q288 (= Q299), V289 (= V300)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
37% identity, 97% coverage: 10:653/666 of query aligns to 1:657/657 of 8sgxX
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/447 of 2vqdA
- active site: K116 (= K121), K159 (= K163), P196 (= P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K121), I157 (≠ M161), K159 (= K163), G164 (= G168), G166 (= G170), F203 (≠ A207), L204 (≠ V208), H209 (= H213), Q233 (= Q237), H236 (= H240), L278 (= L282), E288 (= E293), I437 (≠ T441)
- binding magnesium ion: E276 (= E280), E288 (= E293)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/444 of 3rupA
- active site: K116 (= K121), K159 (= K163), D196 (≠ P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding adenosine-5'-diphosphate: Y82 (= Y87), G83 (= G88), K116 (= K121), K159 (= K163), G164 (= G168), G164 (= G168), G165 (= G169), G166 (= G170), R167 (= R171), M169 (= M173), F193 (= F197), E201 (= E205), K202 (≠ R206), Y203 (≠ A207), L204 (≠ V208), H209 (= H213), Q233 (= Q237), H236 (= H240), K238 (= K242), L278 (= L282), E288 (= E293), R292 (= R297), V295 (= V300), E296 (= E301), R338 (= R343), D382 (= D386), I437 (≠ T441)
- binding calcium ion: E87 (= E92), E276 (= E280), E288 (= E293), E288 (= E293), N290 (= N295)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/444 of 3g8cA
- active site: K116 (= K121), K159 (= K163), D196 (≠ P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding adenosine-5'-diphosphate: I157 (≠ M161), K159 (= K163), G164 (= G168), M169 (= M173), E201 (= E205), K202 (≠ R206), Y203 (≠ A207), L204 (≠ V208), Q233 (= Q237), H236 (= H240), L278 (= L282), E288 (= E293), I437 (≠ T441)
- binding bicarbonate ion: K238 (= K242), R292 (= R297), Q294 (= Q299), V295 (= V300), E296 (= E301)
- binding biotin: Y82 (= Y87), F84 (= F89), R292 (= R297), V295 (= V300), R338 (= R343), D382 (= D386)
- binding magnesium ion: E276 (= E280), E288 (= E293)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/445 of 3jziA
- active site: K116 (= K121), K159 (= K163), D196 (≠ P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K121), K159 (= K163), A160 (= A164), G164 (= G168), G165 (= G169), M169 (= M173), Y199 (≠ I203), E201 (= E205), K202 (≠ R206), Y203 (≠ A207), H209 (= H213), Q233 (= Q237), H236 (= H240), L278 (= L282), I287 (≠ M292), E288 (= E293)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/445 of 2w6oA
- active site: K116 (= K121), K159 (= K163), D196 (≠ P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K163), K202 (≠ R206), Y203 (≠ A207), L204 (≠ V208), L278 (= L282), I437 (≠ T441)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/445 of 2w6nA
- active site: K116 (= K121), K159 (= K163), D196 (≠ P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M161), K159 (= K163), M169 (= M173), E201 (= E205), K202 (≠ R206), Y203 (≠ A207), L278 (= L282)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/445 of 2v59A
- active site: K116 (= K121), K159 (= K163), D196 (≠ P200), H209 (= H213), R235 (= R239), T274 (= T278), E276 (= E280), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K163), Y203 (≠ A207), L204 (≠ V208), H209 (= H213), Q233 (= Q237), H236 (= H240), L278 (= L282), I437 (≠ T441)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
50% identity, 66% coverage: 7:444/666 of query aligns to 2:440/449 of P24182
- R19 (= R24) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ A28) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K121) binding
- K159 (= K163) binding
- GG 165:166 (= GG 169:170) binding
- EKYL 201:204 (≠ ERAV 205:208) binding
- H209 (= H213) binding
- H236 (= H240) binding
- K238 (= K242) binding
- E276 (= E280) binding ; binding
- E288 (= E293) binding ; binding
- R292 (= R297) active site; binding
- V295 (= V300) binding
- E296 (= E301) mutation to A: Severe reduction in catalytic activity.
- R338 (= R343) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (vs. gap) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R370) mutation to E: Loss of homodimerization. No effect on ATP binding.
Query Sequence
>RR42_RS29420 FitnessBrowser__Cup4G11:RR42_RS29420
MKQPTPFQKILIANRGEIALRVMRSATALGYRTVAVYSSADAGARHVEEAGQAVYIGQAQ
PAQSYLRIDAIIEAARRSGADAVHPGYGFLAENAAFARACREAGLVFIGPSAESIVAMGN
KAGAKRLMMAADVPCIPGYQGEDQDEARLCAEAERIGFPVMIKATAGGGGRGMRLVPHAR
AFPELLRSARSEAQGAFGDPEVILERAVVEPRHIEIQILADRYGNAIHLGERDCSVQRRH
QKLIEEAPSPAVSAELRARMGATAVAAVKAIGYEGAGTLEFLLDRDGNYYFMEMNTRLQV
EHPVTEAITGLDLVALQLRIAAGEPLPLRQEDVRFSGHAIEVRLCAEDADQGFMPQSGEI
ALWQAPPALRVEHALGSGAAIPPYYDSMIAKLISYGGTRDEARRKLSQGLEDLVALGVTT
NQVFLGRCLAHPAFAAGEATTAFIGQHQDALLQPDAALRQRAAALAALLLYETSPERQPG
APAASLAPTLPIGLRYRVNGAEHQASLAYGAGNRFAVAMGESRFAFETIALGAHSVRFSC
DGLVESATFHRDASTLLLHYQGTPLRIEDHTRAAAARAGEAAGDGKLRASMNGRVVNVMV
AAGDQVEAGQPMVTLEAMKMEHIHVAPAAGRVGAVHVQVGDQAAAMRVIAEIEFEAPPAE
PVKAAA
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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