SitesBLAST
Comparing SM_b20756 SM_b20756 propionyl-CoA carboxylase subunit alpha 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)
68% identity, 100% coverage: 4:670/670 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F351) binding
- W515 (= W504) mutation to L: No effect on holoenzyme formation.
- L599 (= L588) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L591) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M592) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K636) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
67% identity, 99% coverage: 5:670/670 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K119), K157 (= K161), D180 (= D198), H193 (= H211), R219 (= R237), T258 (= T276), E260 (= E278), E273 (= E291), N275 (= N293), R277 (= R295), E281 (= E299), R323 (= R341), G519 (= G543)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M635), K612 (= K636)
7ybuA Human propionyl-coenzyme a carboxylase
52% identity, 99% coverage: 5:670/670 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)
52% identity, 99% coverage: 5:670/670 of query aligns to 63:728/728 of P05165
- A75 (= A17) to P: in PA-1; dbSNP:rs794727479
- R77 (= R19) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A80) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I106) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G139) to E: in PA-1
- M229 (= M171) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q239) to R: in PA-1
- D368 (= D310) to G: in PA-1
- M373 (= M315) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G321) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ S340) to R: in PA-1
- R399 (= R341) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P364) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ V478) natural variant: Missing (in PA-1)
- V551 (= V500) to F: in dbSNP:rs61749895
- W559 (= W504) to L: in PA-1; dbSNP:rs118169528
- G631 (= G573) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G610) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K636) modified: N6-biotinyllysine; by HLCS
- C712 (≠ I654) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
66% identity, 69% coverage: 206:670/670 of query aligns to 133:591/591 of 3n6rA
- active site: H138 (= H211), R164 (= R237), T203 (= T276), E205 (= E278), E218 (= E291), N220 (= N293), R222 (= R295), E226 (= E299), R268 (= R341), G464 (= G543)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M635), K557 (= K636)
Sites not aligning to the query:
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
45% identity, 99% coverage: 8:670/670 of query aligns to 1:657/657 of 8sgxX
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: 4:666/670 of query aligns to 1:649/654 of P9WPQ3
- K322 (= K323) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
51% identity, 67% coverage: 3:452/670 of query aligns to 2:444/453 of 7kctA
- active site: E276 (= E278), E289 (= E291), N291 (= N293), E297 (= E299), R339 (= R341)
- binding adenosine-5'-diphosphate: K117 (= K119), L157 (≠ M159), K159 (= K161), G164 (= G166), G165 (= G167), G166 (= G168), I169 (≠ M171), E201 (= E203), Y203 (≠ F205), I204 (≠ V206), H209 (= H211), Q233 (= Q235), Q237 (= Q239), K238 (= K240), I278 (= I280), E289 (= E291), R293 (= R295), Q295 (= Q297), V296 (= V298), E297 (= E299), R339 (= R341)
- binding bicarbonate ion: D116 (= D118), R119 (≠ T121)
- binding magnesium ion: E276 (= E278), E289 (= E291)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
50% identity, 67% coverage: 6:452/670 of query aligns to 1:442/448 of 2vpqB
- active site: V116 (≠ T121), K156 (= K161), H206 (= H211), R232 (= R237), T271 (= T276), E273 (= E278), E287 (= E291), N289 (= N293), R291 (= R295), E295 (= E299), R337 (= R341)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K119), I154 (≠ M159), K156 (= K161), G161 (= G166), G163 (= G168), I166 (≠ M171), F200 (= F205), I201 (≠ V206), E273 (= E278), I275 (= I280), M286 (≠ L290), E287 (= E291)
- binding magnesium ion: E273 (= E278), E287 (= E291)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
48% identity, 67% coverage: 4:454/670 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K119), K159 (= K161), D193 (= D198), H206 (= H211), R232 (= R237), T271 (= T276), E273 (= E278), E285 (= E291), N287 (= N293), R289 (= R295), E293 (= E299), R335 (= R341)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K161), G164 (= G166), M166 (= M171), E198 (= E203), Y200 (≠ F205), L201 (≠ V206), H233 (≠ N238), L275 (≠ I280), E285 (= E291)
- binding magnesium ion: E273 (= E278), E285 (= E291)
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, 67% coverage: 4:454/670 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K119), K159 (= K161), D191 (= D198), H204 (= H211), R230 (= R237), T269 (= T276), E271 (= E278), E283 (= E291), N285 (= N293), R287 (= R295), E291 (= E299), R333 (= R341)
- 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 (≠ M159), K159 (= K161), M164 (= M171), E196 (= E203), Y198 (≠ F205), L199 (≠ V206), H204 (= H211), Q228 (= Q235), E271 (= E278), L273 (≠ I280), E283 (= E291), I432 (≠ T447)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
48% identity, 67% coverage: 4:454/670 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K119), K159 (= K161), D190 (= D198), H203 (= H211), R229 (= R237), T268 (= T276), E270 (= E278), E282 (= E291), N284 (= N293), R286 (= R295), E290 (= E299), R332 (= R341)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K161), M163 (= M171), E195 (= E203), Y197 (≠ F205), L198 (≠ V206), E270 (= E278), L272 (≠ I280), E282 (= E291)
- binding bicarbonate ion: R286 (= R295), Q288 (= Q297), V289 (= V298)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
48% identity, 67% coverage: 4:454/670 of query aligns to 1:444/447 of 2vqdA
- active site: K116 (= K119), K159 (= K161), P196 (≠ D198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K119), I157 (≠ M159), K159 (= K161), G164 (= G166), G166 (= G168), F203 (= F205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (≠ N238), L278 (≠ I280), E288 (= E291), I437 (≠ T447)
- binding magnesium ion: E276 (= E278), E288 (= E291)
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
48% identity, 67% coverage: 4:454/670 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K119), K159 (= K161), D196 (= D198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding calcium ion: E276 (= E278), E288 (= E291), N290 (= N293)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K161), M169 (= M171), E201 (= E203), Y203 (≠ F205), L204 (≠ V206), H236 (≠ N238), L278 (≠ I280), E288 (= E291), I437 (≠ T447)
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)
48% identity, 67% coverage: 4:454/670 of query aligns to 1:444/448 of P43873
- K116 (= K119) binding
- K159 (= K161) binding
- EKYL 201:204 (≠ EKFV 203:206) binding
- E276 (= E278) binding ; binding
- E288 (= E291) binding ; binding
- N290 (= N293) binding
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
47% identity, 67% coverage: 4:454/670 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K119), K159 (= K161), D194 (= D198), H207 (= H211), R233 (= R237), T272 (= T276), E274 (= E278), E286 (= E291), N288 (= N293), R290 (= R295), E294 (= E299), R336 (= R341)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K161), R165 (≠ K169), M167 (= M171), Y201 (≠ F205), L202 (≠ V206), E274 (= E278), L276 (≠ I280), E286 (= E291), N288 (= N293), I435 (≠ T447)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
47% identity, 67% coverage: 4:454/670 of query aligns to 1:430/430 of 4mv1A
- active site: K116 (= K119), K159 (= K161), D182 (= D198), H195 (= H211), R221 (= R237), T260 (= T276), E262 (= E278), E274 (= E291), N276 (= N293), R278 (= R295), E282 (= E299), R324 (= R341)
- binding adenosine-5'-diphosphate: K159 (= K161), E187 (= E203), K188 (= K204), Y189 (≠ F205), L190 (≠ V206), L264 (≠ I280)
- binding phosphate ion: K224 (= K240), R278 (= R295), Q280 (= Q297), V281 (= V298), E282 (= E299)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
48% identity, 67% coverage: 3:454/670 of query aligns to 2:446/447 of 3jzfB
- active site: K118 (= K119), K161 (= K161), D198 (= D198), H211 (= H211), R237 (= R237), T276 (= T276), E278 (= E278), E290 (= E291), N292 (= N293), R294 (= R295), E298 (= E299), R340 (= R341)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K119), K161 (= K161), A162 (= A162), G166 (= G166), G168 (= G168), R169 (≠ K169), G170 (= G170), M171 (= M171), Y201 (≠ F201), E203 (= E203), K204 (= K204), Y205 (≠ F205), H211 (= H211), H238 (≠ N238), L280 (≠ I280), I289 (≠ L290), E290 (= E291)
1dv2A The structure of biotin carboxylase, mutant e288k, complexed with atp (see paper)
47% identity, 67% coverage: 3:454/670 of query aligns to 3:447/450 of 1dv2A
- active site: K119 (= K119), K162 (= K161), D199 (= D198), H212 (= H211), R238 (= R237), T277 (= T276), E279 (= E278), K291 (≠ E291), N293 (= N293), R295 (= R295), E299 (= E299), R341 (= R341)
- binding adenosine-5'-triphosphate: K119 (= K119), K162 (= K161), G166 (= G165), G168 (= G167), M172 (= M171), E204 (= E203), K205 (= K204), Y206 (≠ F205), L207 (≠ V206), H239 (≠ N238), L281 (≠ I280), K291 (≠ E291)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
48% identity, 67% coverage: 4:454/670 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K119), K159 (= K161), D196 (= D198), H209 (= H211), R235 (= R237), T274 (= T276), E276 (= E278), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding adenosine-5'-diphosphate: Y82 (= Y85), G83 (= G86), K116 (= K119), K159 (= K161), G164 (= G166), G164 (= G166), G165 (= G167), G166 (= G168), R167 (≠ K169), M169 (= M171), F193 (= F195), E201 (= E203), K202 (= K204), Y203 (≠ F205), L204 (≠ V206), H209 (= H211), Q233 (= Q235), H236 (≠ N238), K238 (= K240), L278 (≠ I280), E288 (= E291), R292 (= R295), V295 (= V298), E296 (= E299), R338 (= R341), D382 (= D392), I437 (≠ T447)
- binding calcium ion: E87 (= E90), E276 (= E278), E288 (= E291), E288 (= E291), N290 (= N293)
Query Sequence
>SM_b20756 SM_b20756 propionyl-CoA carboxylase subunit alpha
MGHMFKKILIANRGEIACRVIRTTKALGIPTVAVYSDADRDAMHVRMADEAVHIGPSPSS
QSYIVIENILAAIRRTGADAVHPGYGFLSENAAFAEALEKDGVTFIGPPVRAIEAMGDKI
TSKKLAAEAGVFTVPGHMGLIEDADEAARIAAEIGFPVMIKASAGGGGKGMRIAWNEREA
REGFQSSRNEAKSSFGDDRIFIEKFVTEPRHIEIQVLGDKHGNILYLGERECSIQRRNQK
VIEEAPSPFLDEKTRRAMGEQAVALAKAVGYHSAGTVEFIVDAGRNFYFLEMNTRLQVEH
PVTELVTGLDLVEQMIRVAAGAKLAFAQKDVKLDGWAIESRLYAEDPYRTFLPSIGRLTR
YRPPEEGTQADGTVIRNDTGVFEGGEISMYYDPMIAKLCTWGPDRLTAVRAMADALDAFE
VEGIGHNLPFLAAVMQQERFHEGRLTTAYIAEEFAGGFHGVALDDASARKLAAVAATVNQ
TLQERASRISGTIGNHRRVVGHEWVTSLDGHEIQVTCEVSADGTYVRFADGTSVSVATDW
APGRTRAAFNIDNQPMSVKVELAGPGIRLRWRGIDVVARVRSPRIAELARLMPKKLPPDT
SKMLLCPMPGVVTSITVKAGETVEAGQAIAVVEAMKMENILRAEKRAIVKRVAIEAGASL
AVDELIMEFE
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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