SitesBLAST
Comparing WP_011444474.1 NCBI__GCF_000013325.1:WP_011444474.1 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)
61% identity, 100% coverage: 1:673/673 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F352) binding biotin
- W515 (= W512) mutation to L: No effect on holoenzyme formation.
- L599 (= L591) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ H594) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M595) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K639) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
59% identity, 100% coverage: 2:673/673 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E292), N275 (= N294), R277 (= R296), E281 (= E300), R323 (= R342), G519 (= G546)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M638), K612 (= K639)
7ybuA Human propionyl-coenzyme a carboxylase
50% identity, 100% coverage: 2:673/673 of query aligns to 5:670/670 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)
50% identity, 100% coverage: 2:673/673 of query aligns to 63:728/728 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 (= D311) to G: in PA-1
- M373 (= M316) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G322) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ N341) to R: in PA-1
- R399 (= R342) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P365) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L487) natural variant: Missing (in PA-1)
- V551 (≠ L506) to F: in dbSNP:rs61749895
- W559 (= W512) to L: in PA-1; dbSNP:rs118169528
- G631 (= G576) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G613) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K639) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A657) 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)
45% identity, 99% coverage: 5:673/673 of query aligns to 1:657/657 of 8sgxX
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
56% identity, 70% coverage: 203:673/673 of query aligns to 133:591/591 of 3n6rA
- active site: H138 (= H208), R164 (= R234), T203 (= T273), E205 (= E275), E218 (= E292), N220 (= N294), R222 (= R296), E226 (= E300), R268 (= R342), G464 (= G546)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M638), K557 (= K639)
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)
41% identity, 100% coverage: 1:673/673 of query aligns to 1:653/654 of P9WPQ3
- K322 (= K324) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
39% identity, 97% coverage: 2:653/673 of query aligns to 2:644/666 of 8rthA
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
40% identity, 100% coverage: 4:673/673 of query aligns to 6:649/651 of 8j78I
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, 70% coverage: 1:470/673 of query aligns to 3:452/453 of 7kctA
- active site: E276 (= E275), E289 (= E292), N291 (= N294), E297 (= E300), R339 (= R342)
- 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 (= I277), E289 (= E292), R293 (= R296), Q295 (= Q298), V296 (= V299), E297 (= E300), R339 (= R342)
- binding bicarbonate ion: D116 (= D115), R119 (≠ E118)
- binding magnesium ion: E276 (= E275), E289 (= E292)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
48% identity, 70% coverage: 1:471/673 of query aligns to 1:448/456 of 8hz4A
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
45% identity, 68% coverage: 1:459/673 of query aligns to 1:438/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E292), N288 (= N294), R290 (= R296), E294 (= E300), R336 (= R342)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (≠ F202), L202 (≠ I203), E274 (= E275), L276 (≠ I277), E286 (= E292), N288 (= N294), I435 (≠ T456)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
46% identity, 67% coverage: 1:452/673 of query aligns to 1:430/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E292), N287 (= N294), R289 (= R296), E293 (= E300), R335 (= R342)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (≠ F202), L201 (≠ I203), H233 (= H235), L275 (≠ I277), E285 (= E292)
- binding magnesium ion: E273 (= E275), E285 (= E292)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
46% identity, 68% coverage: 3:461/673 of query aligns to 1:442/448 of 2vpqB
- active site: V116 (≠ E118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E292), N289 (= N294), R291 (= R296), E295 (= E300), R337 (= R342)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (= F202), I201 (= I203), E273 (= E275), I275 (= I277), M286 (≠ L291), E287 (= E292)
- binding magnesium ion: E273 (= E275), E287 (= E292)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
45% identity, 68% coverage: 1:459/673 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 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (= F202), L204 (≠ I203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ I277), E288 (= E292), I437 (≠ T456)
- binding magnesium ion: E276 (= E275), E288 (= E292)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
46% identity, 67% coverage: 1:452/673 of query aligns to 1:427/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E292), N284 (= N294), R286 (= R296), E290 (= E300), R332 (= R342)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (≠ F202), L198 (≠ I203), E270 (= E275), L272 (≠ I277), E282 (= E292)
- binding bicarbonate ion: R286 (= R296), Q288 (= Q298), V289 (= V299)
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)
46% identity, 67% coverage: 1:452/673 of query aligns to 1:428/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E292), N285 (= N294), R287 (= R296), E291 (= E300), R333 (= R342)
- 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 (≠ I277), E283 (= E292)
Sites not aligning to the query:
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 68% coverage: 1:459/673 of query aligns to 1:440/449 of P24182
- R19 (≠ K19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ R23) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K116) binding ATP
- K159 (= K158) binding ATP
- GG 165:166 (= GG 164:165) binding ATP
- EKYL 201:204 (≠ EKFI 200:203) binding ATP
- H209 (= H208) binding ATP
- H236 (= H235) binding ATP
- K238 (= K237) binding hydrogencarbonate
- E276 (= E275) binding ATP; binding Mg(2+)
- E288 (= E292) binding ATP; binding Mg(2+)
- R292 (= R296) active site; binding hydrogencarbonate
- V295 (= V299) binding hydrogencarbonate
- E296 (= E300) mutation to A: Severe reduction in catalytic activity.
- R338 (= R342) binding biotin; binding hydrogencarbonate; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ D382) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R385) 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)
45% identity, 68% coverage: 1:459/673 of query aligns to 1:440/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K158), G164 (= G163), G164 (= G163), G165 (= G164), G166 (= G165), R167 (≠ K166), M169 (= M168), F193 (= F192), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (≠ I203), H209 (= H208), Q233 (= Q232), H236 (= H235), K238 (= K237), L278 (≠ I277), E288 (= E292), R292 (= R296), V295 (= V299), E296 (= E300), R338 (= R342), D382 (= D401), I437 (≠ T456)
- binding calcium ion: E87 (= E87), E276 (= E275), E288 (= E292), E288 (= E292), N290 (= N294)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
45% identity, 68% coverage: 1:459/673 of query aligns to 1:440/444 of 3g8cA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding adenosine-5'-diphosphate: I157 (≠ M156), K159 (= K158), G164 (= G163), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (≠ I203), Q233 (= Q232), H236 (= H235), L278 (≠ I277), E288 (= E292), I437 (≠ T456)
- binding bicarbonate ion: K238 (= K237), R292 (= R296), Q294 (= Q298), V295 (= V299), E296 (= E300)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R296), V295 (= V299), R338 (= R342), D382 (= D401)
- binding magnesium ion: E276 (= E275), E288 (= E292)
Query Sequence
>WP_011444474.1 NCBI__GCF_000013325.1:WP_011444474.1
MFKKILIANRGEIACRVIKTARRMGIQTVAVYSDADARAPFVQMADEAVHIGPAPAAQSY
LIADKIIAACKQTGAEAVHPGYGFLSERTSFAEALAAEGIEFIGPPVGAIAAMGDKIESK
KLAKEAGVNVVPGFVGEIEDTEHAVRISDEIGYPVMMKASAGGGGKGMRLAYNEKDVREG
FEAVKREGLNSFGDDRVFIEKFILNPRHIEIQILGDKHGNILYLNERECSIQRRHQKVVE
EAPSPFVTPKMRKAMGEQCVALARAVGYYSAGTVELIVSGADPSGESFYFLEMNTRLQVE
HPVTEAITGVDLVEQMIRVAAGEKLALTQDEVKIDGWAIENRVYAEDPYRGFLPSTGRLI
RYNPPVAGWTDDGAENGRRGIDGVRVDDGVYEGGEVSMFYDPMIAKLITWGKTRDEAADK
QIEALDAFEIEGLGHNIDFVNAIMQHPRFRSGELTTGFIAEEYPEGFTGAATSDELKQTL
AALAAFLATARADRARQVDNQLGHDLDPPSEWSVKVGGSTFAVELTEEEISVDGTPVDIA
LEYTPGDRMVHCEVDDKPLSVKVETTRAGFRLTTRGAIHDVQVLPARIAHLTRHMIEKVP
PDLSKFLICPMPGLLVSLNVGEGDTVEAGQPLAVVEAMKMENILRAEKAGKVKSVNAKAG
DSLAVDAIILEME
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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