SitesBLAST
Comparing 5210129 Shew_2573 carbamoyl-phosphate synthase L chain, ATP-binding (RefSeq) 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 96% coverage: 1:651/677 of query aligns to 1:633/654 of P9WPQ3
- K322 (≠ E325) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
42% identity, 99% coverage: 2:671/677 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)
42% identity, 99% coverage: 2:671/677 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 (≠ V103) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G136) to E: in PA-1
- M229 (= M168) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q236) 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 (≠ Y477) natural variant: Missing (in PA-1)
- V551 (≠ Y497) to F: in dbSNP:rs61749895
- W559 (≠ F506) to L: in PA-1; dbSNP:rs118169528
- G631 (≠ S583) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G612) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K638) modified: N6-biotinyllysine; by HLCS
- C712 (≠ F656) 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)
50% identity, 68% coverage: 1:459/677 of query aligns to 1:474/681 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)
49% identity, 68% coverage: 2:459/677 of query aligns to 1:439/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E293), N275 (= N295), R277 (= R297), E281 (= E301), R323 (= R343)
Sites not aligning to the query:
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
39% identity, 99% coverage: 5:671/677 of query aligns to 1:656/657 of 8sgxX
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 66% coverage: 1:449/677 of query aligns to 1:439/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E293), N287 (= N295), R289 (= R297), E293 (= E301), R335 (= R343)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (≠ K166), M166 (= M168), E198 (= E200), Y200 (= Y202), L201 (= L203), H233 (= H235), L275 (= L277), E285 (= E293)
- binding magnesium ion: E273 (= E275), E285 (= E293)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:440/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E293), N288 (= N295), R290 (= R297), E294 (= E301), R336 (= R343)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (= Y202), L202 (= L203), E274 (= E275), L276 (= L277), E286 (= E293), N288 (= N295), I435 (≠ T444)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:436/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E293), N284 (= N295), R286 (= R297), E290 (= E301), R332 (= R343)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (= Y202), L198 (= L203), E270 (= E275), L272 (= L277), E282 (= E293)
- binding bicarbonate ion: R286 (= R297), Q288 (= Q299), V289 (= V300)
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)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:437/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), 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 (≠ L156), K159 (= K158), M164 (= M168), E196 (= E200), Y198 (= Y202), L199 (= L203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (= L277), E283 (= E293), I432 (≠ T444)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
48% identity, 66% coverage: 4:449/677 of query aligns to 2:442/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E293), N289 (= N295), R291 (= R297), E295 (= E301), R337 (= R343)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ L156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (≠ Y202), I201 (≠ L203), E273 (= E275), I275 (≠ L277), M286 (= M292), E287 (= E293)
- binding magnesium ion: E273 (= E275), E287 (= E293)
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
49% identity, 66% coverage: 1:449/677 of query aligns to 1:442/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding calcium ion: E276 (= E275), E288 (= E293), N290 (= N295)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (= L203), H236 (= H235), L278 (= L277), E288 (= E293), I437 (≠ T444)
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)
49% identity, 66% coverage: 1:449/677 of query aligns to 1:442/448 of P43873
- K116 (= K116) binding
- K159 (= K158) binding
- EKYL 201:204 (≠ ERYL 200:203) binding
- E276 (= E275) binding ; binding
- E288 (= E293) binding ; binding
- N290 (= N295) binding
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:442/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ L156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (≠ Y202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), E288 (= E293), I437 (≠ T444)
- binding magnesium ion: E276 (= E275), E288 (= E293)
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)
47% identity, 66% coverage: 1:450/677 of query aligns to 3:445/453 of 7kctA
- active site: E276 (= E275), E289 (= E293), N291 (= N295), E297 (= E301), R339 (= R343)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (= L156), K159 (= K158), G164 (= G163), G165 (= G164), G166 (= G165), I169 (≠ M168), E201 (= E200), Y203 (= Y202), I204 (≠ L203), H209 (= H208), Q233 (= Q232), Q237 (= Q236), K238 (= K237), I278 (≠ L277), E289 (= E293), R293 (= R297), Q295 (= Q299), V296 (= V300), E297 (= E301), R339 (= R343)
- binding bicarbonate ion: D116 (≠ S115), R119 (≠ A118)
- binding magnesium ion: E276 (= E275), E289 (= E293)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:428/430 of 4mv1A
- active site: K116 (= K116), K159 (= K158), D182 (= D195), H195 (= H208), R221 (= R234), T260 (= T273), E262 (= E275), E274 (= E293), N276 (= N295), R278 (= R297), E282 (= E301), R324 (= R343)
- binding adenosine-5'-diphosphate: K159 (= K158), E187 (= E200), K188 (≠ R201), Y189 (= Y202), L190 (= L203), L264 (= L277)
- binding phosphate ion: K224 (= K237), R278 (= R297), Q280 (= Q299), V281 (= V300), E282 (= E301)
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)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:442/446 of 6oi9A
- active site: E276 (= E275), E288 (= E293), N290 (= N295), E296 (= E301), R338 (= R343)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), E276 (= E275), L278 (= L277), E288 (= E293), I437 (≠ T444)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:442/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (= Y202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T444)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:442/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ L156), K159 (= K158), G166 (= G165), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (= L203), L278 (= L277)
2w6zA Crystal structure of biotin carboxylase from e. Coli in complex with the 3-(3-methyl-but-2-enyl)-3h-purin-6-ylamine fragment (see paper)
48% identity, 66% coverage: 1:449/677 of query aligns to 1:442/446 of 2w6zA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E293), N290 (= N295), R292 (= R297), E296 (= E301), R338 (= R343)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K158), Y203 (= Y202), L204 (= L203), L278 (= L277)
Query Sequence
>5210129 Shew_2573 carbamoyl-phosphate synthase L chain, ATP-binding (RefSeq)
MFTKLLIANRGEIACRIIKTAQVMGIKTVALYSDADKDARHVAMADESFYLGGSAPSESY
LKGELILEIAKRSGAQAIHPGYGFLSENADFARQCEQAGIAFVGPSADAIDAMGSKSAAK
IIMEQANVPLVPGYHGDDQSDEVLLKASKEIGFPQLIKAAYGGGGKGMRIVESESEALEA
INSARREAASSFGNDKLLIERYLRQPRHVEVQVFADTQGNCIYLSDRDCSIQRRHQKVVE
EAPAPGLSDSLRRAMGEAAVAAAKAIDYVGAGTVEFLLDTHATEESNSFYFMEMNTRLQV
EHPVTEMVTGQDLVKWQLMVASGSELPLSQEDVRIHGHSFEVRIYAEDPQNEFLPASGKL
NFLREPEQNRYVRIDSGIRENDVISNFYDPMIAKLIVWDESRPRALQRLVHALESYQISG
LKHNIEFLANIAEHKAFSQADFSTDFIERYGDTLIGANLDGDNSHEQNGALAFAALYHLC
AQKEQAKLTATNSQDPYSPWGQVSGFRLNRSGMHQLSLLDDEHEVQHLTLSQIGDCYYLN
LNDQQLTLSGELKQDLLHAEINGHKSKIPVSREGDDFTLFLPSGSYHFRALQTEVVEEQA
NSEDKLKAPMNGTIVTHLVEVGDEVEAGQGLMVMEAMKMEYTIEAPFDGTVAAFFFQPGE
LVSDGALLLEVTAKEDA
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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