SitesBLAST
Comparing WP_085772374.1 NCBI__GCF_002117405.1:WP_085772374.1 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)
59% identity, 100% coverage: 1:668/669 of query aligns to 1:680/681 of Q5LUF3
- F348 (= F348) binding biotin
- W515 (≠ R501) mutation to L: No effect on holoenzyme formation.
- L599 (= L587) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ F590) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M591) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K635) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
58% identity, 100% coverage: 2:668/669 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 (= G542)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M634), K612 (= K635)
7ybuA Human propionyl-coenzyme a carboxylase
51% identity, 100% coverage: 2:668/669 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)
51% identity, 100% coverage: 2:668/669 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 (= G136) to E: in PA-1
- M229 (= M168) 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 (≠ S337) to R: in PA-1
- R399 (= R338) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P361) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ M474) natural variant: Missing (in PA-1)
- V551 (= V502) to F: in dbSNP:rs61749895
- W559 (≠ F510) to L: in PA-1; dbSNP:rs118169528
- G631 (= G574) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G609) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K635) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A653) 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: 5:668/669 of query aligns to 1:656/657 of 8sgxX
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
56% identity, 70% coverage: 203:668/669 of query aligns to 133:590/591 of 3n6rA
- active site: H138 (= H208), R164 (= R234), T203 (= T273), E205 (= E275), E218 (= E288), N220 (= N290), R222 (= R292), E226 (= E296), R268 (= R338), G464 (= G542)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M634), K557 (= K635)
Sites not aligning to the query:
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
52% identity, 67% coverage: 1:448/669 of query aligns to 1:445/654 of P9WPQ3
- K322 (≠ P320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
41% identity, 97% coverage: 2:649/669 of query aligns to 2:644/666 of 8rthA
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
50% identity, 67% coverage: 3:448/669 of query aligns to 1:442/448 of 2vpqB
- active site: V116 (≠ E118), 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 (≠ M168), F200 (= F202), I201 (= I203), E273 (= E275), I275 (≠ V277), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E275), E287 (= E288)
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)
48% identity, 68% coverage: 1:454/669 of query aligns to 3:449/453 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 (≠ M168), E201 (= E200), Y203 (≠ F202), I204 (= I203), 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 (≠ E118)
- binding magnesium ion: E276 (= E275), E289 (= E288)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
47% identity, 67% coverage: 1:446/669 of query aligns to 1:437/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (≠ F202), L201 (≠ I203), H233 (≠ N235), L275 (≠ V277), E285 (= E288)
- binding magnesium ion: E273 (= E275), E285 (= E288)
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
48% identity, 67% coverage: 4:450/669 of query aligns to 6:427/651 of 8j78I
Sites not aligning to the query:
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)
47% identity, 67% coverage: 1:446/669 of query aligns to 1:435/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E288), N285 (= N290), R287 (= R292), E291 (= E296), R333 (= R338)
- 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 (≠ M156), K159 (= K158), M164 (= M168), E196 (= E200), Y198 (≠ F202), L199 (≠ I203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (≠ V277), E283 (= E288), I432 (≠ T443)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
47% identity, 67% coverage: 1:446/669 of query aligns to 1:434/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E288), N284 (= N290), R286 (= R292), E290 (= E296), R332 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (≠ F202), L198 (≠ I203), E270 (= E275), L272 (≠ V277), E282 (= E288)
- binding bicarbonate ion: R286 (= R292), Q288 (= Q294), V289 (= V295)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 67% coverage: 1:446/669 of query aligns to 1:440/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (= F202), L204 (≠ I203), H209 (= H208), Q233 (= Q232), H236 (≠ N235), L278 (≠ V277), E288 (= E288), I437 (≠ T443)
- binding magnesium ion: E276 (= E275), E288 (= E288)
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: 1:446/669 of query aligns to 1:440/445 of 6ojhA
- 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 calcium ion: E276 (= E275), E288 (= E288), N290 (= N290)
- 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 (≠ F202), L204 (≠ I203), H236 (≠ N235), L278 (≠ V277), E288 (= E288), I437 (≠ T443)
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: 1:446/669 of query aligns to 1:440/448 of P43873
- K116 (= K116) binding ATP
- K159 (= K158) binding ATP
- EKYL 201:204 (≠ EKFI 200:203) binding ATP
- E276 (= E275) binding ATP; binding Mg(2+)
- E288 (= E288) binding ATP; binding Mg(2+)
- N290 (= N290) binding Mg(2+)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
49% identity, 67% coverage: 1:446/669 of query aligns to 1:437/456 of 8hz4A
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
47% identity, 67% coverage: 3:448/669 of query aligns to 38:483/1178 of Q05920
- K39 (= K4) modified: N6-acetyllysine
- K79 (≠ M44) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ A112) modified: N6-acetyllysine
- K152 (= K116) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N205) modified: N6-acetyllysine
- K434 (≠ P399) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
- 589 modified: N6-acetyllysine
- 717 modified: N6-acetyllysine
- 748 modified: N6-acetyllysine; K→Q: Reduced pyruvate carboxylase activity.
- 892 modified: N6-acetyllysine
- 969 modified: N6-acetyllysine
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
46% identity, 67% coverage: 3:448/669 of query aligns to 7:452/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ I18), T26 (≠ R22), R46 (≠ V42), Q47 (≠ E43), K48 (≠ M44), A49 (= A45), D50 (= D46), R367 (= R359), R414 (≠ D410), E418 (≠ R414), R420 (≠ V416), R422 (≠ D418)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K158), G168 (= G163), G169 (= G164), M173 (= M168), F207 (= F202), I208 (= I203), P211 (= P206), H240 (≠ N235)
Sites not aligning to the query:
Query Sequence
>WP_085772374.1 NCBI__GCF_002117405.1:WP_085772374.1
MFRKILIANRGEIACRVIKTARKMGIATVAVYSDADEDALHVEMADEKVHLGPPPAAQSY
LLIDKIIAACKQTGAEAVHPGYGFLSERAAFAKALADEGIVFIGPNPRAIEAMGDKIESK
KFAAKAKVNVVPGHLGVIKDGEEAVKIANEIGYPVMLKASAGGGGKGMRIAYKADEVVEG
FTRARSEAASSFGDDRVFIEKFIVNPRHIEIQVLGDKHGNVIHLNERECSIQRRNQKVIE
EAPSPLLDEKTRAEMGAQAVALAKAVDYDSAGTVEFVAGQDKSFYFLEMNTRLQVEHPVT
ELITGIDLVEQMIRVAAGLPLELRQKDVTIKGWAVESRIYAEDPTRNFLPSIGRLVKYRP
PHEESAEGITVRNDTGVTEGREISIHYDPMIAKLVTHGPNRLAAINAQADALDRFVIDGI
RQNIPFLSSLMMNERWRSGELSTGFIAEEYPGGFAPQEPKGELAHQLASVATLMDHIGNE
RKRQVSGQLRHGAPVQFERNRVCLLGDQRFFVSVLAQDEDLLVRFAGEEERQHRVTSQWR
PGDLVFEGSVDGKPVFVQTRPILNGYELSHQGVGVAARVYTQREAELAAFMPKKKDTGAA
KFLLCPMPGLVKTMDVKEGQEIKAGEALCMVEAMKMENVLRAERDATVKKILAKPGDSLA
VDAVIMEFA
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