SitesBLAST
Comparing WP_050656406.1 NCBI__GCF_002893965.1:WP_050656406.1 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)
43% identity, 98% coverage: 5:654/661 of query aligns to 4:654/654 of P9WPQ3
- K322 (≠ A314) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8xl6A Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
39% identity, 98% coverage: 3:653/661 of query aligns to 1:660/660 of 8xl6A
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
42% identity, 95% coverage: 3:630/661 of query aligns to 2:641/666 of 8rthA
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
37% identity, 99% coverage: 2:654/661 of query aligns to 3:650/651 of 8j78I
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)
38% identity, 98% coverage: 3:653/661 of query aligns to 2:681/681 of Q5LUF3
- F348 (≠ W340) binding biotin
- W515 (≠ K499) mutation to L: No effect on holoenzyme formation.
- L599 (≠ T570) 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 (≠ A572) 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
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
38% identity, 98% coverage: 3:653/661 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K117), K157 (= K150), D180 (= D186), H193 (= H200), R219 (= R226), T258 (= T267), E260 (= E269), E273 (= E282), N275 (= N284), R277 (= R286), E281 (= E290), R323 (= R330), G519 (vs. gap)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M618), K612 (= K619)
8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
37% identity, 99% coverage: 2:653/661 of query aligns to 2:668/668 of 8xl5A
7ybuA Human propionyl-coenzyme a carboxylase (see paper)
37% identity, 99% coverage: 2:653/661 of query aligns to 4:670/670 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)
37% identity, 99% coverage: 2:653/661 of query aligns to 62:728/728 of P05165
- A75 (= A15) to P: in PA-1; dbSNP:rs794727479
- R77 (= R17) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A78) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I104) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ P137) to E: in PA-1
- M229 (= M160) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q228) to R: in PA-1; dbSNP:rs2063109875
- D368 (= D301) to G: in PA-1
- M373 (≠ Q306) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G312) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V329) to R: in PA-1
- R399 (= R330) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P353) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L469) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W489) to L: in PA-1; dbSNP:rs118169528
- G631 (≠ S556) 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
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
46% identity, 67% coverage: 3:443/661 of query aligns to 2:438/442 of 4mv4A
- active site: K116 (= K117), K159 (= K150), D193 (≠ P187), H206 (= H200), R232 (= R226), T271 (= T267), E273 (= E269), E285 (= E282), N287 (= N284), R289 (= R286), E293 (= E290), R335 (= R330)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K150), G164 (= G155), M166 (= M160), E198 (= E192), Y200 (= Y194), L201 (= L195), H233 (= H227), L275 (= L271), E285 (= E282)
- binding magnesium ion: E273 (= E269), E285 (= E282)
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)
45% identity, 67% coverage: 3:443/661 of query aligns to 2:436/440 of 6oi8A
- active site: K116 (= K117), K159 (= K150), D191 (≠ P187), H204 (= H200), R230 (= R226), T269 (= T267), E271 (= E269), E283 (= E282), N285 (= N284), R287 (= R286), E291 (= E290), R333 (= R330)
- 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 (≠ L148), K159 (= K150), M164 (= M160), E196 (= E192), Y198 (= Y194), L199 (= L195), H204 (= H200), Q228 (= Q224), E271 (= E269), L273 (= L271), E283 (= E282), I432 (≠ T439)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
45% identity, 67% coverage: 3:443/661 of query aligns to 2:435/439 of 4mv3A
- active site: K116 (= K117), K159 (= K150), D190 (≠ P187), H203 (= H200), R229 (= R226), T268 (= T267), E270 (= E269), E282 (= E282), N284 (= N284), R286 (= R286), E290 (= E290), R332 (= R330)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K150), M163 (= M160), E195 (= E192), Y197 (= Y194), L198 (= L195), E270 (= E269), L272 (= L271), E282 (= E282)
- binding bicarbonate ion: R286 (= R286), Q288 (= Q288), V289 (= V289)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
47% identity, 67% coverage: 5:445/661 of query aligns to 4:440/456 of 8hz4A
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
46% identity, 67% coverage: 3:443/661 of query aligns to 2:441/445 of 6ojhA
- active site: K116 (= K117), K159 (= K150), D196 (≠ P187), H209 (= H200), R235 (= R226), T274 (= T267), E276 (= E269), E288 (= E282), N290 (= N284), R292 (= R286), E296 (= E290), R338 (= R330)
- binding calcium ion: E276 (= E269), E288 (= E282), N290 (= N284)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K150), M169 (= M160), E201 (= E192), Y203 (= Y194), L204 (= L195), H236 (= H227), L278 (= L271), E288 (= E282), I437 (≠ T439)
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)
46% identity, 67% coverage: 3:443/661 of query aligns to 2:441/448 of P43873
- K116 (= K117) binding ATP
- K159 (= K150) binding ATP
- EKYL 201:204 (≠ ERYL 192:195) binding ATP
- E276 (= E269) binding ATP; binding Mg(2+)
- E288 (= E282) binding ATP; binding Mg(2+)
- N290 (= N284) binding Mg(2+)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
44% identity, 67% coverage: 3:443/661 of query aligns to 37:482/1178 of Q05920
- K39 (≠ S5) modified: N6-acetyllysine
- K79 (≠ E45) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L113) modified: N6-acetyllysine
- K152 (= K117) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ T197) modified: N6-acetyllysine
- K434 (≠ P395) 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
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)
44% identity, 67% coverage: 3:445/661 of query aligns to 4:445/453 of 7kctA
- active site: E276 (= E269), E289 (= E282), N291 (= N284), E297 (= E290), R339 (= R330)
- binding adenosine-5'-diphosphate: K117 (= K117), L157 (= L148), K159 (= K150), G164 (= G155), G165 (= G156), G166 (= G157), I169 (≠ M160), E201 (= E192), Y203 (= Y194), I204 (≠ L195), H209 (= H200), Q233 (= Q224), Q237 (= Q228), K238 (= K229), I278 (≠ L271), E289 (= E282), R293 (= R286), Q295 (= Q288), V296 (= V289), E297 (= E290), R339 (= R330)
- binding bicarbonate ion: D116 (≠ S116), R119 (≠ E119)
- binding magnesium ion: E276 (= E269), E289 (= E282)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
44% identity, 67% coverage: 3:443/661 of query aligns to 2:441/447 of 2vqdA
- active site: K116 (= K117), K159 (= K150), P196 (= P187), H209 (= H200), R235 (= R226), T274 (= T267), E276 (= E269), E288 (= E282), N290 (= N284), R292 (= R286), E296 (= E290), R338 (= R330)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K117), I157 (≠ L148), K159 (= K150), G164 (= G155), G166 (= G157), F203 (≠ Y194), L204 (= L195), H209 (= H200), Q233 (= Q224), H236 (= H227), L278 (= L271), E288 (= E282), I437 (≠ T439)
- binding magnesium ion: E276 (= E269), E288 (= E282)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
43% identity, 67% coverage: 3:443/661 of query aligns to 6:451/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (= F19), T26 (≠ R23), R46 (≠ V43), Q47 (≠ A44), K48 (≠ E45), A49 (= A46), D50 (= D47), R367 (≠ S360), R414 (≠ S406), E418 (≠ R410), R420 (= R412), R422 (≠ H414)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K150), G168 (= G155), G169 (= G156), M173 (= M160), F207 (≠ Y194), I208 (≠ L195), P211 (≠ G198), H240 (= H227)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
43% identity, 67% coverage: 3:443/661 of query aligns to 5:450/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K150), G167 (= G155), G168 (= G156), F206 (≠ Y194), Q236 (= Q224), H239 (= H227), E292 (= E282)
- binding coenzyme a: F21 (= F19), R22 (≠ A20), T25 (≠ R23), R45 (≠ V43), Q46 (≠ A44), K47 (≠ E45), A48 (= A46), D49 (= D47), E50 (≠ A48), R366 (≠ S360), R413 (≠ S406), A416 (= A409), R419 (= R412)
Sites not aligning to the query:
Query Sequence
>WP_050656406.1 NCBI__GCF_002893965.1:WP_050656406.1
MTITSVLVANRGEIARRVFATCRKNGIGTVAVFSDADADSPHVAEADASVRLPGNTPAET
YLRGELVIAAAKASGADAIHPGYGFLSENAEFARSVIDAGLTWIGPPVESIELMGSKVES
KKIMDAAGVPVLSELDPAAVTEAHLPVLIKASAGGGGRGMRVVRELSALDGELEAARREA
QSAFGDPTVFCERYLETGRHIEVQVMADRHGAVWAVGERECSIQRRHQKVVEEAPSPLVQ
RIPAMRDKLFDASRLAANAIGYEGAGTVEFLADEKGDFFFLEMNTRLQVEHPVTECTTGL
DLVELQLQVASGEALPDDQPEIRGHSIEVRLYAEDPAKNWQPQSGTVHHIELPGDPQEFS
VLREQGVRLDSGVVDGSVVGVHYDPMLAKVISYAPTRTAAARLLASTLARTRIHGLRTNR
DLLVNVLAHPAFIAGDTDTAFFETHDLEKLSTPLADTDAERLSALAAALADAAHNRASAR
VIGRLPSGWRNLPSQPQSKSYSTASGDYDVRYSLSRSGVLSAEGFDDVRLVSATATRVVL
EQSGVQRSFDVAAYGSEIFVDSSLGPVALTAAPRFVDPSAEVAAGSLLAPMPGSVIRLGA
ALGDTVTAGQPILWLEAMKMEHTVTAPTAGVLVELPVAVGQQVEVGSVLARVEEPATEEE
A
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