SitesBLAST
Comparing Ac3H11_1927 FitnessBrowser__acidovorax_3H11:Ac3H11_1927 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)
44% identity, 99% coverage: 1:661/670 of query aligns to 2:652/654 of P9WPQ3
- K322 (≠ P318) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
49% identity, 67% coverage: 1:448/670 of query aligns to 2:464/681 of Q5LUF3
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
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
49% identity, 67% coverage: 1:448/670 of query aligns to 1:429/646 of 3n6rG
- active site: K115 (= K115), K157 (= K157), D180 (≠ E186), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E286), N275 (= N288), R277 (= R290), E281 (= E294), R323 (= R336)
Sites not aligning to the query:
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
45% identity, 67% coverage: 2:449/670 of query aligns to 1:444/448 of 2vpqB
- active site: V116 (≠ G117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E286), N289 (= N288), R291 (= R290), E295 (= E294), R337 (= R336)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ A201), I201 (≠ L202), E273 (= E274), I275 (≠ L276), M286 (= M285), E287 (= E286)
- binding magnesium ion: E273 (= E274), E287 (= E286)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
44% identity, 67% coverage: 1:447/670 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 (= E286), N288 (= N288), R290 (= R290), E294 (= E294), R336 (= R336)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (= R165), M167 (= M167), Y201 (≠ A201), L202 (= L202), E274 (= E274), L276 (= L276), E286 (= E286), N288 (= N288), I435 (≠ V442)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
34% identity, 98% coverage: 4:661/670 of query aligns to 1:656/657 of 8sgxX
7ybuA Human propionyl-coenzyme a carboxylase
35% identity, 99% coverage: 1:661/670 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)
35% identity, 99% coverage: 1:661/670 of query aligns to 63:727/728 of P05165
- A75 (= A13) to P: in PA-1; dbSNP:rs794727479
- R77 (= R15) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A76) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I102) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G135) to E: in PA-1
- M229 (= M167) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1
- D368 (= D305) to G: in PA-1
- M373 (≠ Q310) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G316) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V335) to R: in PA-1
- R399 (= R336) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P357) to L: in PA-1; dbSNP:rs1443858896
- L532 (vs. gap) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (≠ I459) to L: in PA-1; dbSNP:rs118169528
- G631 (= G546) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G602) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K628) modified: N6-biotinyllysine; by HLCS
- C712 (≠ V646) 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)
43% identity, 67% coverage: 1:447/670 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 (= E286), N287 (= N288), R289 (= R290), E293 (= E294), R335 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (= M167), E198 (= E199), Y200 (≠ A201), L201 (= L202), H233 (= H234), L275 (= L276), E285 (= E286)
- binding magnesium ion: E273 (= E274), E285 (= E286)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
47% identity, 67% coverage: 1:448/670 of query aligns to 2:440/456 of 8hz4A
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
43% identity, 67% coverage: 1:447/670 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 (= E286), N284 (= N288), R286 (= R290), E290 (= E294), R332 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (= M167), E195 (= E199), Y197 (≠ A201), L198 (= L202), E270 (= E274), L272 (= L276), E282 (= E286)
- binding bicarbonate ion: R286 (= R290), Q288 (= Q292), V289 (= V293)
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)
43% identity, 66% coverage: 1:445/670 of query aligns to 2:435/440 of 6oi8A
- active site: K116 (= K115), K159 (= K157), D191 (≠ G194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E286), N285 (= N288), R287 (= R290), E291 (= E294), R333 (= R336)
- 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 (≠ M155), K159 (= K157), M164 (= M167), E196 (= E199), Y198 (≠ A201), L199 (= L202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (= L276), E283 (= E286), I432 (≠ V442)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
44% identity, 66% coverage: 1:445/670 of query aligns to 2:440/447 of 2vqdA
- active site: K116 (= K115), K159 (= K157), P196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K115), I157 (≠ M155), K159 (= K157), G164 (= G162), G166 (= G164), F203 (≠ A201), L204 (= L202), H209 (= H207), Q233 (= Q231), H236 (= H234), L278 (= L276), E288 (= E286), I437 (≠ V442)
- binding magnesium ion: E276 (= E274), E288 (= E286)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
44% identity, 67% coverage: 1:447/670 of query aligns to 2:442/445 of 3jziA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K115), K159 (= K157), A160 (= A158), G164 (= G162), G165 (= G163), M169 (= M167), Y199 (≠ L197), E201 (= E199), K202 (≠ R200), Y203 (≠ A201), H209 (= H207), Q233 (= Q231), H236 (= H234), L278 (= L276), I287 (≠ M285), E288 (= E286)
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, 67% coverage: 1:447/670 of query aligns to 2:442/445 of 2w6oA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K157), K202 (≠ R200), Y203 (≠ A201), L204 (= L202), L278 (= L276), I437 (≠ V442)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
44% identity, 67% coverage: 1:447/670 of query aligns to 2:442/445 of 2w6nA
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M155), K159 (= K157), M169 (= M167), E201 (= E199), K202 (≠ R200), Y203 (≠ A201), L278 (= L276)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
44% identity, 67% coverage: 1:447/670 of query aligns to 2:442/445 of 2v59A
- active site: K116 (= K115), K159 (= K157), D196 (≠ G194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K157), Y203 (≠ A201), L204 (= L202), H209 (= H207), Q233 (= Q231), H236 (= H234), L278 (= L276), I437 (≠ V442)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 67% coverage: 1:447/670 of query aligns to 2:442/449 of P24182
- R19 (≠ H18) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ R22) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K115) binding
- K159 (= K157) binding
- GG 165:166 (= GG 163:164) binding
- EKYL 201:204 (≠ ERAL 199:202) binding
- H209 (= H207) binding
- H236 (= H234) binding
- K238 (= K236) binding
- E276 (= E274) binding ; binding
- E288 (= E286) binding ; binding
- R292 (= R290) active site; binding
- V295 (= V293) binding
- E296 (= E294) mutation to A: Severe reduction in catalytic activity.
- R338 (= R336) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ T360) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R371) mutation to E: Loss of homodimerization. No effect on ATP binding.
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
44% identity, 67% coverage: 1:447/670 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 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding adenosine-5'-diphosphate: Y82 (= Y81), G83 (= G82), K116 (= K115), K159 (= K157), G164 (= G162), G164 (= G162), G165 (= G163), G166 (= G164), R167 (= R165), M169 (= M167), F193 (= F191), E201 (= E199), K202 (≠ R200), Y203 (≠ A201), L204 (= L202), H209 (= H207), Q233 (= Q231), H236 (= H234), K238 (= K236), L278 (= L276), E288 (= E286), R292 (= R290), V295 (= V293), E296 (= E294), R338 (= R336), D382 (= D387), I437 (≠ V442)
- binding calcium ion: E87 (= E86), E276 (= E274), E288 (= E286), E288 (= E286), N290 (= N288)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
44% identity, 67% coverage: 1:447/670 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 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding adenosine-5'-diphosphate: I157 (≠ M155), K159 (= K157), G164 (= G162), M169 (= M167), E201 (= E199), K202 (≠ R200), Y203 (≠ A201), L204 (= L202), Q233 (= Q231), H236 (= H234), L278 (= L276), E288 (= E286), I437 (≠ V442)
- binding bicarbonate ion: K238 (= K236), R292 (= R290), Q294 (= Q292), V295 (= V293), E296 (= E294)
- binding biotin: Y82 (= Y81), F84 (= F83), R292 (= R290), V295 (= V293), R338 (= R336), D382 (= D387)
- binding magnesium ion: E276 (= E274), E288 (= E286)
Query Sequence
>Ac3H11_1927 FitnessBrowser__acidovorax_3H11:Ac3H11_1927
MKKILIANRSEIARRIIHTAHRMGIETVAVYSDPDASALHVREATQAVALGGAASADTYL
RTDKLLAAARATGADAVHPGYGFLSENADFAQAVVDAGLTWIGPPPAAIRALGSKAGAKA
LAVAHCVPCLPGYAGDDQSDERFAAEAARIGTPLMVKAVAGGGGRGMRLVTDLAQLPAAL
ASARSEALAGFGCGDLLIERALLQPRHVEVQIFADAHGACIHLGERDCSVQRRHQKIIEE
APSPAVDAALRERMGACAVALAQAAGYVGAGTVEFLLDGPDFYLMEMNTRLQVEHPVTEA
LTGLDLVEWQIRVARGEPLPLTQDQVHLQGHAIEVRLCAEDAHFRPHTGRVLQFSAPPAT
AFERAAPGALRFDHALEEGAEVTPHYDAMLGKLIVHAPTRAEAIAALVRALHSTRVLGLP
TNRAFLAACLQHPVFGAGHALVPFLAEHAAQLQGLLSNIELKVLVQSAVAVIFSSNSSGA
ASAQLPCALARPLRLRHQGQVVPLAVRELGAGRLWVEHAGGTTHLQLAPQAAGMVRITTM
QTGAVGEVHHADHTVRAVPVGPRRWHWQTGGVDGWVEDASWEPAARAGAAGGATELRAPF
NGKVVALPVAAGQALSAGDTVVVIESMKLEHSLASPVAATVAELLVAPGQQVSPGQVLAR
FAPATQGAPA
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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