SitesBLAST
Comparing WP_027720886.1 NCBI__GCF_000425265.1:WP_027720886.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
35% identity, 96% coverage: 7:459/472 of query aligns to 6:426/453 of 7kctA
- active site: E276 (= E300), E289 (= E313), N291 (= N315), E297 (= E321), R339 (= R369)
- binding adenosine-5'-diphosphate: K117 (= K121), L157 (≠ M171), K159 (= K173), G164 (= G178), G165 (= G179), G166 (= G180), I169 (= I183), E201 (= E215), Y203 (≠ R217), I204 (= I218), H209 (= H223), Q233 (= Q248), Q237 (= Q253), K238 (= K254), I278 (= I302), E289 (= E313), R293 (= R317), Q295 (= Q319), V296 (= V320), E297 (= E321), R339 (= R369)
- binding bicarbonate ion: D116 (= D120), R119 (≠ N123)
- binding magnesium ion: E276 (= E300), E289 (= E313)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
34% identity, 94% coverage: 7:451/472 of query aligns to 2:417/448 of 2vpqB
- active site: V116 (≠ N123), K156 (= K173), H206 (= H223), R232 (≠ N250), T271 (= T298), E273 (= E300), E287 (= E313), N289 (= N315), R291 (= R317), E295 (= E321), R337 (= R369)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K121), I154 (≠ M171), K156 (= K173), G161 (= G178), G163 (= G180), I166 (= I183), F200 (≠ R217), I201 (= I218), E273 (= E300), I275 (= I302), M286 (= M312), E287 (= E313)
- binding magnesium ion: E273 (= E300), E287 (= E313)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
34% identity, 94% coverage: 7:448/472 of query aligns to 4:414/447 of 2vqdA
- active site: K116 (= K121), K159 (= K173), P196 (≠ E210), H209 (= H223), R235 (≠ N250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K121), I157 (≠ M171), K159 (= K173), G164 (= G178), G166 (= G180), F203 (≠ R217), L204 (≠ I218), H209 (= H223), Q233 (= Q248), H236 (≠ N252), L278 (≠ I302), E288 (= E313)
- binding magnesium ion: E276 (= E300), E288 (= E313)
Sites not aligning to the query:
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
33% identity, 96% coverage: 7:459/472 of query aligns to 4:421/442 of 4mv4A
- active site: K116 (= K121), K159 (= K173), D193 (≠ E210), H206 (= H223), R232 (≠ N250), T271 (= T298), E273 (= E300), E285 (= E313), N287 (= N315), R289 (= R317), E293 (= E321), R335 (= R369)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K173), G164 (= G179), M166 (= M181), E198 (= E215), Y200 (≠ R217), L201 (≠ I218), H233 (≠ N252), L275 (≠ I302), E285 (= E313)
- binding magnesium ion: E273 (= E300), E285 (= E313)
7ybuA Human propionyl-coenzyme a carboxylase
32% identity, 93% coverage: 7:447/472 of query aligns to 7:419/670 of 7ybuA
Sites not aligning to the query:
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)
32% identity, 93% coverage: 7:447/472 of query aligns to 65:477/728 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 (= I108) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ S141) to E: in PA-1
- M229 (≠ I183) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q253) to R: in PA-1
- D368 (= D338) to G: in PA-1
- M373 (≠ Q343) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G349) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ Y368) to R: in PA-1
- R399 (= R369) to Q: in PA-1; dbSNP:rs1301904623
- P423 (≠ N392) to L: in PA-1; dbSNP:rs1443858896
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 532 natural variant: Missing (in PA-1)
- 551 V → F: in dbSNP:rs61749895
- 559 W → L: in PA-1; dbSNP:rs118169528
- 631 G → R: in PA-1; loss of function; dbSNP:rs796052018
- 668 G → R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- 694 modified: N6-biotinyllysine; by HLCS
- 712 natural variant: Missing (in PA-1; loss of biotinylation)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
35% identity, 83% coverage: 2:393/472 of query aligns to 3:370/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A21), T26 (≠ V25), R46 (= R46), Q47 (≠ F47), K48 (≠ A48), A49 (≠ R49), D50 (= D50), R367 (≠ G390)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K173), G168 (= G178), G169 (= G179), M173 (≠ I183), F207 (≠ R217), I208 (= I218), P211 (≠ F221), H240 (≠ N252)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 414, 418, 420, 422, 462, 463, 465, 1025
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 582, 839, 877, 880, 881
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
35% identity, 83% coverage: 2:393/472 of query aligns to 2:369/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K173), G167 (= G178), G168 (= G179), F206 (≠ R217), Q236 (= Q248), H239 (≠ N252), E292 (= E313)
- binding coenzyme a: F21 (≠ A21), R22 (≠ K22), T25 (≠ V25), R45 (= R46), Q46 (≠ F47), K47 (≠ A48), A48 (≠ R49), D49 (= D50), E50 (= E51), R366 (≠ G390)
Sites not aligning to the query:
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
35% identity, 83% coverage: 2:393/472 of query aligns to 34:401/1178 of P11498
- V145 (≠ I114) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (≠ K125) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (≠ N250) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y293) to C: in PC deficiency
Sites not aligning to the query:
- 451 R → C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
- 572 binding Mn(2+)
- 583 R → L: in PC deficiency; dbSNP:rs119103242
- 610 A → T: in PC deficiency; mild; dbSNP:rs28940589
- 631 R → Q: in PC deficiency; dbSNP:rs113994145
- 741 binding via carbamate group; modified: N6-carboxylysine
- 743 M → I: in PC deficiency; mild; dbSNP:rs28940590
- 771 binding Mn(2+)
- 773 binding Mn(2+)
- 1077 mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- 1131:1133 natural variant: Missing (in PC deficiency)
- 1144 modified: N6-biotinyllysine
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)
33% identity, 96% coverage: 7:459/472 of query aligns to 4:419/440 of 6oi8A
- active site: K116 (= K121), K159 (= K173), D191 (≠ E210), H204 (= H223), R230 (≠ N250), T269 (= T298), E271 (= E300), E283 (= E313), N285 (= N315), R287 (= R317), E291 (= E321), R333 (= R369)
- 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 (≠ M171), K159 (= K173), M164 (= M181), E196 (= E215), Y198 (≠ R217), L199 (≠ I218), H204 (= H223), Q228 (= Q248), E271 (= E300), L273 (≠ I302), E283 (= E313)
Sites not aligning to the query:
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
35% identity, 83% coverage: 2:393/472 of query aligns to 34:401/1178 of Q05920
- K35 (= K3) modified: N6-acetyllysine
- K39 (= K7) modified: N6-acetyllysine
- K79 (≠ A48) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ E117) modified: N6-acetyllysine
- K152 (= K121) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ G220) modified: N6-acetyllysine
Sites not aligning to the query:
- 434 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
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
32% identity, 94% coverage: 7:448/472 of query aligns to 4:412/444 of 2vr1A
- active site: K116 (= K121), K159 (= K173), D194 (≠ E210), H207 (= H223), R233 (≠ N250), T272 (= T298), E274 (= E300), E286 (= E313), N288 (= N315), R290 (= R317), E294 (= E321), R336 (= R369)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K173), R165 (≠ G179), M167 (= M181), Y201 (≠ R217), L202 (≠ I218), E274 (= E300), L276 (≠ I302), E286 (= E313), N288 (= N315)
Sites not aligning to the query:
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
32% identity, 96% coverage: 7:459/472 of query aligns to 4:418/439 of 4mv3A
- active site: K116 (= K121), K159 (= K173), D190 (≠ E210), H203 (= H223), R229 (≠ N250), T268 (= T298), E270 (= E300), E282 (= E313), N284 (= N315), R286 (= R317), E290 (= E321), R332 (= R369)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K173), M163 (≠ I183), E195 (= E215), Y197 (≠ R217), L198 (≠ I218), E270 (= E300), L272 (≠ I302), E282 (= E313)
- binding bicarbonate ion: R286 (= R317), Q288 (= Q319), V289 (= V320)
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)
33% identity, 96% coverage: 7:459/472 of query aligns to 4:424/448 of P43873
- K116 (= K121) binding ATP
- K159 (= K173) binding ATP
- EKYL 201:204 (≠ EQRI 215:218) binding ATP
- E276 (= E300) binding ATP; binding Mg(2+)
- E288 (= E313) binding ATP; binding Mg(2+)
- N290 (= N315) binding Mg(2+)
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
33% identity, 96% coverage: 7:459/472 of query aligns to 4:424/445 of 6ojhA
- active site: K116 (= K121), K159 (= K173), D196 (≠ E210), H209 (= H223), R235 (≠ N250), T274 (= T298), E276 (= E300), E288 (= E313), N290 (= N315), R292 (= R317), E296 (= E321), R338 (= R369)
- binding calcium ion: E276 (= E300), E288 (= E313), N290 (= N315)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K173), M169 (≠ I183), E201 (= E215), Y203 (≠ R217), L204 (≠ I218), H236 (≠ N252), L278 (≠ I302), E288 (= E313)
Sites not aligning to the query:
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
33% identity, 97% coverage: 7:464/472 of query aligns to 6:433/1150 of A0A0H3JRU9
- R21 (≠ K22) mutation to A: Complete loss of catalytic activity.
- K119 (= K121) binding ATP
- K161 (= K173) binding ATP
- H211 (= H223) binding ATP
- E278 (= E300) binding ATP
- K411 (≠ R435) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding substrate
- 542 binding Mn(2+)
- 580 A→T: Complete loss of catalytic activity.
- 614 R→A: Complete loss of catalytic activity.
- 621 Y→A: Complete loss of catalytic activity.
- 712 binding Mn(2+)
- 741 binding Mn(2+)
- 743 binding Mn(2+)
- 838 Q→A: About 2.5-fold loss of catalytic activity.
- 876 T→A: Complete loss of catalytic activity.
- 879 S→A: About 2-fold loss of catalytic activity.
- 880 K→T: Complete loss of catalytic activity.
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
35% identity, 81% coverage: 8:389/472 of query aligns to 1:354/657 of 8sgxX
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)
32% identity, 96% coverage: 8:462/472 of query aligns to 5:424/654 of P9WPQ3
- K322 (≠ S351) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
33% identity, 94% coverage: 7:448/472 of query aligns to 4:414/449 of P24182
- R19 (≠ K22) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (= E26) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K121) binding ATP
- K159 (= K173) binding ATP
- GG 165:166 (= GG 179:180) binding ATP
- EKYL 201:204 (≠ EQRI 215:218) binding ATP
- H209 (= H223) binding ATP
- H236 (≠ N252) binding ATP
- K238 (= K254) binding hydrogencarbonate
- E276 (= E300) binding ATP; binding Mg(2+)
- E288 (= E313) binding ATP; binding Mg(2+)
- R292 (= R317) active site; binding hydrogencarbonate
- V295 (= V320) binding hydrogencarbonate
- E296 (= E321) mutation to A: Severe reduction in catalytic activity.
- R338 (= R369) binding biotin; binding hydrogencarbonate; mutation to A: Severe reduction in catalytic activity.
- F363 (vs. gap) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (vs. gap) mutation to E: Loss of homodimerization. No effect on ATP binding.
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)
33% identity, 94% coverage: 7:448/472 of query aligns to 4:414/446 of 6oi9A
- active site: E276 (= E300), E288 (= E313), N290 (= N315), E296 (= E321), R338 (= R369)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K173), M169 (≠ I183), E201 (= E215), Y203 (≠ R217), L204 (≠ I218), H209 (= H223), Q233 (= Q248), H236 (≠ N252), E276 (= E300), L278 (≠ I302), E288 (= E313)
Sites not aligning to the query:
Query Sequence
>WP_027720886.1 NCBI__GCF_000425265.1:WP_027720886.1
MYKAEHKVLIANRGEIAIRIAKACVELGQDFTCVYTEADIDSGHVRFARDEGGENSLFRI
SSYRDANEIFSVADRCNATAIHPGYGFFAEDFRFARRVVDRNNPLIFIGPSWWIIQELGD
KINTKRLARSLGVPTVPGSDSPIYDELEAVELAESLFSFQREQGFQAPAIMVKASAGGGG
MGIEEVTDPDEFKSVYRRIRNYAKRQFNDEGVLIEQRIYGFNHLEVQIVSERSGKKHVHF
GTRNCSVQSNGNQKRIEVAPGFAPDEINYIFNAAEVMENITAHSLSMAREVAYDNVGTWE
WIVTPRGEPFLMEVNTRIQVENGVSASIAAIDGNDDVDIVREQVRLGLGESMEYAQDNVT
LGGVALEYRIIAENPDNYFNPWVGRITEFGWNEHDWLSVYTQVPTDRDYDIPTEFDPNLA
LAIVRGGTLEQARRRGVQFLEELILNGFDRSGRPLESNISYLIDKTSGLLEF
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