SitesBLAST
Comparing WP_091518618.1 NCBI__GCF_900115115.1:WP_091518618.1 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)
7ybuA Human propionyl-coenzyme a carboxylase (see paper)
55% identity, 92% coverage: 3:444/481 of query aligns to 7:450/670 of 7ybuA
Sites not aligning to the query:
8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
55% identity, 92% coverage: 3:444/481 of query aligns to 5:448/668 of 8xl5A
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)
55% identity, 92% coverage: 3:444/481 of query aligns to 65:508/728 of P05165
- A75 (= A13) to P: in PA-1; dbSNP:rs794727479
- R77 (= R15) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (≠ G76) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I102) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ H135) to E: in PA-1
- M229 (= M167) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1; dbSNP:rs2063109875
- D368 (= D306) to G: in PA-1
- M373 (≠ Q311) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G317) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ L336) to R: in PA-1
- R399 (= R337) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P360) 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)
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)
53% identity, 92% coverage: 2:444/481 of query aligns to 3:465/681 of Q5LUF3
- F348 (= F347) binding biotin
Sites not aligning to the query:
- 515 W→L: No effect on holoenzyme formation.
- 599 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 602 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 603 M→A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- 647 modified: N6-biotinyllysine
8xl6A Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
50% identity, 97% coverage: 1:465/481 of query aligns to 1:467/660 of 8xl6A
Sites not aligning to the query:
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
53% identity, 92% coverage: 2:444/481 of query aligns to 2:430/646 of 3n6rG
- active site: K115 (= K115), K157 (= K157), D180 (≠ E186), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E287), N275 (= N289), R277 (= R291), E281 (= E295), R323 (= R337)
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)
51% identity, 92% coverage: 4:447/481 of query aligns to 5:449/654 of P9WPQ3
- K322 (≠ V319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
49% identity, 92% coverage: 2:442/481 of query aligns to 1:442/448 of 2vpqB
- active site: V116 (≠ A117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E287), N289 (= N289), R291 (= R291), E295 (= E295), R337 (= R337)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ L155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ Y201), I201 (≠ V202), E273 (= E274), I275 (≠ L276), M286 (≠ L286), E287 (= E287)
- binding magnesium ion: E273 (= E274), E287 (= E287)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
49% identity, 96% coverage: 4:467/481 of query aligns to 1:469/657 of 8sgxX
Sites not aligning to the query:
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
51% identity, 92% coverage: 1:442/481 of query aligns to 2:439/456 of 8hz4A
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
51% identity, 92% coverage: 1:442/481 of query aligns to 2:439/442 of 4mv4A
- active site: K116 (= K115), K159 (= K157), D193 (≠ G194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (= M167), E198 (= E199), Y200 (= Y201), L201 (≠ V202), H233 (= H234), L275 (= L276), E285 (= E287)
- binding magnesium ion: E273 (= E274), E285 (= E287)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 92% coverage: 1:442/481 of query aligns to 2:440/444 of 2vr1A
- active site: K116 (= K115), K159 (= K157), D194 (≠ G194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E287), N288 (= N289), R290 (= R291), E294 (= E295), R336 (= R337)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (≠ K165), M167 (= M167), Y201 (= Y201), L202 (≠ V202), E274 (= E274), L276 (= L276), E286 (= E287), N288 (= N289), I435 (≠ T437)
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)
50% identity, 92% coverage: 1:442/481 of query aligns to 2:437/440 of 6oi8A
- active site: K116 (= K115), K159 (= K157), D191 (≠ G194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E287), N285 (= N289), R287 (= R291), E291 (= E295), R333 (= R337)
- 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 (≠ L155), K159 (= K157), M164 (= M167), E196 (= E199), Y198 (= Y201), L199 (≠ V202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (= L276), E283 (= E287), I432 (≠ T437)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
50% identity, 92% coverage: 1:442/481 of query aligns to 2:436/439 of 4mv3A
- active site: K116 (= K115), K159 (= K157), D190 (≠ G194), H203 (= H207), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E287), N284 (= N289), R286 (= R291), E290 (= E295), R332 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (= M167), E195 (= E199), Y197 (= Y201), L198 (≠ V202), E270 (= E274), L272 (= L276), E282 (= E287)
- binding bicarbonate ion: R286 (= R291), Q288 (= Q293), V289 (= V294)
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, 92% coverage: 1:442/481 of query aligns to 4:444/453 of 7kctA
- active site: E276 (= E274), E289 (= E287), N291 (= N289), E297 (= E295), R339 (= R337)
- binding adenosine-5'-diphosphate: K117 (= K115), L157 (= L155), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), I169 (≠ M167), E201 (= E199), Y203 (= Y201), I204 (≠ V202), H209 (= H207), Q233 (= Q231), Q237 (= Q235), K238 (= K236), I278 (≠ L276), E289 (= E287), R293 (= R291), Q295 (= Q293), V296 (= V294), E297 (= E295), R339 (= R337)
- binding bicarbonate ion: D116 (= D114), R119 (≠ A117)
- binding magnesium ion: E276 (= E274), E289 (= E287)
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)
51% identity, 92% coverage: 1:442/481 of query aligns to 2:442/448 of P43873
- K116 (= K115) binding ATP
- K159 (= K157) binding ATP
- EKYL 201:204 (≠ EKYV 199:202) binding ATP
- E276 (= E274) binding ATP; binding Mg(2+)
- E288 (= E287) binding ATP; binding Mg(2+)
- N290 (= N289) 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
51% identity, 92% coverage: 1:442/481 of query aligns to 2:442/445 of 6ojhA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding calcium ion: E276 (= E274), E288 (= E287), N290 (= N289)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K157), M169 (= M167), E201 (= E199), Y203 (= Y201), L204 (≠ V202), H236 (= H234), L278 (= L276), E288 (= E287), I437 (≠ T437)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
50% identity, 92% coverage: 1:442/481 of query aligns to 2:442/444 of 3rupA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding adenosine-5'-diphosphate: Y82 (= Y81), G83 (= G82), K116 (= K115), K159 (= K157), G164 (= G162), G164 (= G162), G165 (= G163), G166 (= G164), R167 (≠ K165), M169 (= M167), F193 (= F191), E201 (= E199), K202 (= K200), Y203 (= Y201), L204 (≠ V202), H209 (= H207), Q233 (= Q231), H236 (= H234), K238 (= K236), L278 (= L276), E288 (= E287), R292 (= R291), V295 (= V294), E296 (= E295), R338 (= R337), D382 (= D382), I437 (≠ T437)
- binding calcium ion: E87 (= E86), E276 (= E274), E288 (= E287), E288 (= E287), N290 (= N289)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
50% identity, 92% coverage: 1:442/481 of query aligns to 2:442/444 of 3g8cA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding adenosine-5'-diphosphate: I157 (≠ L155), K159 (= K157), G164 (= G162), M169 (= M167), E201 (= E199), K202 (= K200), Y203 (= Y201), L204 (≠ V202), Q233 (= Q231), H236 (= H234), L278 (= L276), E288 (= E287), I437 (≠ T437)
- binding bicarbonate ion: K238 (= K236), R292 (= R291), Q294 (= Q293), V295 (= V294), E296 (= E295)
- binding biotin: Y82 (= Y81), F84 (= F83), R292 (= R291), V295 (= V294), R338 (= R337), D382 (= D382)
- binding magnesium ion: E276 (= E274), E288 (= E287)
8uz2C E. Coli acetyl-coa carboxylase, narrow helical local reconstruction, 3.18 angstrom
50% identity, 92% coverage: 1:442/481 of query aligns to 2:442/446 of 8uz2C
- binding adenosine-5'-diphosphate: K116 (= K115), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), M169 (= M167), H209 (= H207), Q233 (= Q231), H236 (= H234), L278 (= L276), E288 (= E287), I437 (≠ T437)
- binding magnesium ion: E276 (= E274), E288 (= E287)
- binding : R356 (≠ T356), I410 (≠ K410)
Query Sequence
>WP_091518618.1 NCBI__GCF_900115115.1:WP_091518618.1
MKKILVANRGEIALRVMKTAKKMGIKTVAVYSVADRQSPHVKFADEAVCIGEAPSNQSYL
LGDKIIEVCKELGVDGIHPGYGFLSENSKFAELAEKNGITFIGPKSHAIEVMGDKLAAKD
TVKAYDIPMVPGLDHAITDIDEAKKVAKEVGFPILIKASAGGGGKGMRVVEKEEDFESQM
QRAISEATSAFGDGSVFIEKYVGSPRHIEIQVMADTHGNVVYLFERECSVQRRHQKVVEE
APSAVLTPEIRQAMGEAAVKVAKSCDYVGAGTVEFLLDENKNFYFLEMNTRLQVEHPVTE
LITGIDLVEMQIRVARGEVLPIKQEDLKIKGHALELRVYAEDPLNDFLPSVGNLSTYILP
EGEGVRVDNGFEQGMDVPIYYDPMLSKLITYGKDRNEAIELMLKAIQDYKIEGVSTTLPF
GTFVFKHDAFVSGDFDTNFVKKFYSADIIKESQAKEAEVAALIALKQYFADQKVLRVPTK
L
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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