SitesBLAST
Comparing WP_058929521.1 NCBI__GCF_001484605.1:WP_058929521.1 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
54% identity, 93% coverage: 17:706/740 of query aligns to 1:652/654 of P9WPQ3
- K322 (≠ E343) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
41% identity, 92% coverage: 18:697/740 of query aligns to 5:660/670 of 7ybuA
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, 93% coverage: 17:703/740 of query aligns to 1:677/681 of Q5LUF3
- F348 (= F371) binding biotin
- W515 (= W513) mutation to L: No effect on holoenzyme formation.
- L599 (= L624) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ V627) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ L628) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K674) modified: N6-biotinyllysine
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
39% identity, 93% coverage: 18:706/740 of query aligns to 2:662/666 of 8rthA
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)
41% identity, 92% coverage: 18:697/740 of query aligns to 63:718/728 of P05165
- A75 (= A30) to P: in PA-1; dbSNP:rs794727479
- R77 (= R32) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A93) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I119) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ E152) to E: in PA-1
- M229 (= M184) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q252) to R: in PA-1
- D368 (= D330) to G: in PA-1
- M373 (≠ Q335) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G341) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A360) to R: in PA-1
- R399 (= R361) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P385) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ A491) natural variant: Missing (in PA-1)
- V551 (≠ P504) to F: in dbSNP:rs61749895
- W559 (= W513) to L: in PA-1; dbSNP:rs118169528
- G631 (= G607) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G648) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K674) modified: N6-biotinyllysine; by HLCS
- C712 (≠ I691) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
38% identity, 90% coverage: 19:687/740 of query aligns to 5:628/651 of 8j78I
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
40% identity, 93% coverage: 18:703/740 of query aligns to 1:642/646 of 3n6rG
- active site: K115 (= K132), K157 (= K174), D180 (= D211), H193 (= H224), R219 (= R250), T258 (= T294), E260 (= E296), E273 (= E311), N275 (= N313), R277 (= R315), E281 (= E319), R323 (= R361), G519 (= G564)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M673), K612 (= K674)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
48% identity, 63% coverage: 21:489/740 of query aligns to 1:455/657 of 8sgxX
Sites not aligning to the query:
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
44% identity, 61% coverage: 17:471/740 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K132), K159 (= K174), D193 (= D211), H206 (= H224), R232 (= R250), T271 (= T294), E273 (= E296), E285 (= E311), N287 (= N313), R289 (= R315), E293 (= E319), R335 (= R361)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K174), G164 (= G179), M166 (= M184), E198 (= E216), Y200 (≠ L218), L201 (≠ V219), H233 (= H251), L275 (= L298), E285 (= E311)
- binding magnesium ion: E273 (= E296), E285 (= E311)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
45% identity, 61% coverage: 21:469/740 of query aligns to 3:442/448 of 2vpqB
- active site: V116 (≠ R134), K156 (= K174), H206 (= H224), R232 (= R250), T271 (= T294), E273 (= E296), E287 (= E311), N289 (= N313), R291 (= R315), E295 (= E319), R337 (= R361)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K132), I154 (≠ L172), K156 (= K174), G161 (= G179), G163 (= G181), I166 (≠ M184), F200 (≠ L218), I201 (≠ V219), E273 (= E296), I275 (≠ V299), M286 (= M310), E287 (= E311)
- binding magnesium ion: E273 (= E296), E287 (= E311)
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)
44% identity, 61% coverage: 17:471/740 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K132), K159 (= K174), D191 (= D211), H204 (= H224), R230 (= R250), T269 (= T294), E271 (= E296), E283 (= E311), N285 (= N313), R287 (= R315), E291 (= E319), R333 (= R361)
- 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 (≠ L172), K159 (= K174), M164 (= M184), E196 (= E216), Y198 (≠ L218), L199 (≠ V219), H204 (= H224), Q228 (= Q248), E271 (= E296), L273 (= L298), E283 (= E311), I432 (≠ T464)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
44% identity, 61% coverage: 17:471/740 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K132), K159 (= K174), D190 (= D211), H203 (= H224), R229 (= R250), T268 (= T294), E270 (= E296), E282 (= E311), N284 (= N313), R286 (= R315), E290 (= E319), R332 (= R361)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K174), M163 (= M184), E195 (= E216), Y197 (≠ L218), L198 (≠ V219), E270 (= E296), L272 (= L298), E282 (= E311)
- binding bicarbonate ion: R286 (= R315), Q288 (= Q317), V289 (= V318)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 61% coverage: 17:471/740 of query aligns to 1:444/447 of 2vqdA
- active site: K116 (= K132), K159 (= K174), P196 (≠ D211), H209 (= H224), R235 (= R250), T274 (= T294), E276 (= E296), E288 (= E311), N290 (= N313), R292 (= R315), E296 (= E319), R338 (= R361)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K132), I157 (≠ L172), K159 (= K174), G164 (= G179), G166 (= G181), F203 (≠ L218), L204 (≠ V219), H209 (= H224), Q233 (= Q248), H236 (= H251), L278 (= L298), E288 (= E311), I437 (≠ T464)
- binding magnesium ion: E276 (= E296), E288 (= E311)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
44% identity, 61% coverage: 17:471/740 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K132), K159 (= K174), D194 (= D211), H207 (= H224), R233 (= R250), T272 (= T294), E274 (= E296), E286 (= E311), N288 (= N313), R290 (= R315), E294 (= E319), R336 (= R361)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K174), R165 (≠ K182), M167 (= M184), Y201 (≠ L218), L202 (≠ V219), E274 (= E296), L276 (= L298), E286 (= E311), N288 (= N313), I435 (≠ T464)
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, 61% coverage: 17:468/740 of query aligns to 3:443/453 of 7kctA
- active site: E276 (= E296), E289 (= E311), N291 (= N313), E297 (= E319), R339 (= R361)
- binding adenosine-5'-diphosphate: K117 (= K132), L157 (= L172), K159 (= K174), G164 (= G179), G165 (= G180), G166 (= G181), I169 (≠ M184), E201 (= E216), Y203 (≠ L218), I204 (≠ V219), H209 (= H224), Q233 (= Q248), Q237 (= Q252), K238 (= K253), I278 (≠ V299), E289 (= E311), R293 (= R315), Q295 (= Q317), V296 (= V318), E297 (= E319), R339 (= R361)
- binding bicarbonate ion: D116 (= D131), R119 (= R134)
- binding magnesium ion: E276 (= E296), E289 (= E311)
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
45% identity, 61% coverage: 17:471/740 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K132), K159 (= K174), D196 (= D211), H209 (= H224), R235 (= R250), T274 (= T294), E276 (= E296), E288 (= E311), N290 (= N313), R292 (= R315), E296 (= E319), R338 (= R361)
- binding calcium ion: E276 (= E296), E288 (= E311), N290 (= N313)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K174), M169 (= M184), E201 (= E216), Y203 (≠ L218), L204 (≠ V219), H236 (= H251), L278 (= L298), E288 (= E311), I437 (≠ T464)
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)
45% identity, 61% coverage: 17:471/740 of query aligns to 1:444/448 of P43873
- K116 (= K132) binding ATP
- K159 (= K174) binding ATP
- EKYL 201:204 (≠ ERLV 216:219) binding ATP
- E276 (= E296) binding ATP; binding Mg(2+)
- E288 (= E311) binding ATP; binding Mg(2+)
- N290 (= N313) binding Mg(2+)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
47% identity, 61% coverage: 17:469/740 of query aligns to 1:439/456 of 8hz4A
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
44% identity, 61% coverage: 17:471/740 of query aligns to 1:444/445 of 3jziA
- active site: K116 (= K132), K159 (= K174), D196 (= D211), H209 (= H224), R235 (= R250), T274 (= T294), E276 (= E296), E288 (= E311), N290 (= N313), R292 (= R315), E296 (= E319), R338 (= R361)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K132), K159 (= K174), A160 (≠ P175), G164 (= G179), G165 (= G180), M169 (= M184), Y199 (≠ F214), E201 (= E216), K202 (≠ R217), Y203 (≠ L218), H209 (= H224), Q233 (= Q248), H236 (= H251), L278 (= L298), I287 (≠ M310), E288 (= E311)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
44% identity, 61% coverage: 17:471/740 of query aligns to 1:444/445 of 2w6oA
- active site: K116 (= K132), K159 (= K174), D196 (= D211), H209 (= H224), R235 (= R250), T274 (= T294), E276 (= E296), E288 (= E311), N290 (= N313), R292 (= R315), E296 (= E319), R338 (= R361)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K174), K202 (≠ R217), Y203 (≠ L218), L204 (≠ V219), L278 (= L298), I437 (≠ T464)
Query Sequence
>WP_058929521.1 NCBI__GCF_001484605.1:WP_058929521.1
MTVSMPAVPSAIRQKPLFSTVLVANRGEIACRVIRTLRALGIRSVAVYSDADAGARHVRE
ADTAVRIGPAAAGESYLKIEAILQACRDTGAEAVHPGYGFLSENVDFARALEAAGITFIG
PGVESLNVMGDKIRSKNHVAGYGVPVVPGIAEPGMTDAQLMEAAPAVGFPLLIKPSAGGG
GKGMHIVERHEDLEATLATARRVAASAFGDDTLFLERLVRTPRHIEVQVLADNHGNVIHL
GERECSLQRRHQKVIEEAPSPLLESLHDGGATRARIGEAACQAARSVHYSGAGTVEFLVS
DEAPDEFFFMEMNTRLQVEHPVTEMVTGVDLVEWQVRIAAGEELTVRQADVELNGHAAEA
RVYAEIPERNFMPSTGTVLLLDEMPDHGAGMIRVDSALLEGLEISSSYDPMISKVIAWGP
DRTVALDTLDAALAGYTALGIDTNVEYLRLLINDDDVRAGHLDTGLIERKMPDFAFRRID
DAELVAAALYAVVSGEQDITGTPPGPWQASNGWRIGAPAPRRISLGTPDGGIATVSVTGR
VAAGPVQVCVGDGQWRTASLRLPGRGSLVLTLDGEPTDYSLAPADAGPVNLTRDNLPSGV
PAELFLGNGGWSCRLEPLTRESRLVRVLAAVEREEGTADPEVRSPMPGTVVSVAVSNGDT
VEAGQVLLSVEAMKMEHQLVAEVAGTVHISIKAGQPVKADQVLATIHPSTTDSDADSLQD
SNTESNKDSNKDSNNTGKGA
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