SitesBLAST
Comparing WP_027457190.1 NCBI__GCF_000519045.1:WP_027457190.1 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)
57% identity, 100% coverage: 1:667/667 of query aligns to 1:681/681 of Q5LUF3
- F348 (= F349) binding biotin
- W515 (= W498) mutation to L: No effect on holoenzyme formation.
- L599 (= L585) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L588) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (= M589) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K633) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
56% identity, 100% coverage: 2:667/667 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 (= E289), N275 (= N291), R277 (= R293), E281 (= E297), R323 (= R339), G519 (= G540)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M632), K612 (= K633)
7ybuA Human propionyl-coenzyme a carboxylase
50% identity, 100% coverage: 2:667/667 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: 2:667/667 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 (≠ D136) to E: in PA-1
- M229 (≠ L168) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q236) to R: in PA-1
- D368 (= D308) to G: in PA-1
- M373 (= M313) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G319) to V: in PA-1; dbSNP:rs794727087
- C398 (= C338) to R: in PA-1
- R399 (= R339) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P362) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ V472) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (≠ Q497) to L: in PA-1; dbSNP:rs118169528
- G631 (= G570) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G607) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K633) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A651) 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)
47% identity, 99% coverage: 5:667/667 of query aligns to 1:657/657 of 8sgxX
3n6rA Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
54% identity, 70% coverage: 203:667/667 of query aligns to 133:591/591 of 3n6rA
- active site: H138 (= H208), R164 (= R234), T203 (= T273), E205 (= E275), E218 (= E289), N220 (= N291), R222 (= R293), E226 (= E297), R268 (= R339), G464 (= G540)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M556 (= M632), K557 (= K633)
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)
42% identity, 99% coverage: 1:663/667 of query aligns to 1:649/654 of P9WPQ3
- K322 (= K321) 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)
51% identity, 67% coverage: 3:447/667 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ E118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E289), N289 (= N291), R291 (= R293), E295 (= E297), R337 (= R339)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ L168), F200 (≠ Y202), I201 (≠ V203), E273 (= E275), I275 (≠ V277), M286 (≠ L288), E287 (= E289)
- binding magnesium ion: E273 (= E275), E287 (= E289)
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
51% identity, 67% coverage: 4:448/667 of query aligns to 6:427/651 of 8j78I
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:440/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E289), N288 (= N291), R290 (= R293), E294 (= E297), R336 (= R339)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (≠ L168), Y201 (= Y202), L202 (≠ V203), E274 (= E275), L276 (≠ V277), E286 (= E289), N288 (= N291), I435 (≠ T441)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:439/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E289), N287 (= N291), R289 (= R293), E293 (= E297), R335 (= R339)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (≠ L168), E198 (= E200), Y200 (= Y202), L201 (≠ V203), H233 (= H235), L275 (≠ V277), E285 (= E289)
- binding magnesium ion: E273 (= E275), E285 (= E289)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
51% identity, 67% coverage: 1:447/667 of query aligns to 1:440/456 of 8hz4A
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)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:437/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E289), N285 (= N291), R287 (= R293), E291 (= E297), R333 (= R339)
- 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 (≠ L168), E196 (= E200), Y198 (= Y202), L199 (≠ V203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (≠ V277), E283 (= E289), I432 (≠ T441)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:436/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E289), N284 (= N291), R286 (= R293), E290 (= E297), R332 (= R339)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (≠ L168), E195 (= E200), Y197 (= Y202), L198 (≠ V203), E270 (= E275), L272 (≠ V277), E282 (= E289)
- binding bicarbonate ion: R286 (= R293), Q288 (= Q295), V289 (= V296)
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)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:442/448 of P43873
- K116 (= K116) binding ATP
- K159 (= K158) binding ATP
- EKYL 201:204 (≠ EKYV 200:203) binding ATP
- E276 (= E275) binding ATP; binding Mg(2+)
- E288 (= E289) binding ATP; binding Mg(2+)
- N290 (= N291) 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
49% identity, 67% coverage: 1:446/667 of query aligns to 1:442/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E289), N290 (= N291), R292 (= R293), E296 (= E297), R338 (= R339)
- binding calcium ion: E276 (= E275), E288 (= E289), N290 (= N291)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (≠ L168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), H236 (= H235), L278 (≠ V277), E288 (= E289), I437 (≠ T441)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
49% identity, 67% coverage: 1:446/667 of query aligns to 3:444/447 of 3jzfB
- active site: K118 (= K116), K161 (= K158), D198 (= D195), H211 (= H208), R237 (= R234), T276 (= T273), E278 (= E275), E290 (= E289), N292 (= N291), R294 (= R293), E298 (= E297), R340 (= R339)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K158), A162 (= A159), G166 (= G163), G168 (= G165), R169 (≠ K166), G170 (= G167), M171 (≠ L168), Y201 (≠ F198), E203 (= E200), K204 (= K201), Y205 (= Y202), H211 (= H208), H238 (= H235), L280 (≠ V277), I289 (≠ L288), E290 (= E289)
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)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:442/446 of 6oi9A
- active site: E276 (= E275), E288 (= E289), N290 (= N291), E296 (= E297), R338 (= R339)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (≠ L168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), E276 (= E275), L278 (≠ V277), E288 (= E289), I437 (≠ T441)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:442/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E289), N290 (= N291), R292 (= R293), E296 (= E297), R338 (= R339)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (≠ V277), I437 (≠ T441)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
49% identity, 67% coverage: 1:446/667 of query aligns to 1:442/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E289), N290 (= N291), R292 (= R293), E296 (= E297), R338 (= R339)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ M156), K159 (= K158), G166 (= G165), M169 (≠ L168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), L278 (≠ V277)
Query Sequence
>WP_027457190.1 NCBI__GCF_000519045.1:WP_027457190.1
MFKKILIANRGEIACRVIKTARKMGIATVAVYSEADKDALHVDLADEAVCIGPAASKESY
LVMDKIIAACKQTGAEAVHPGYGFLSENAEFSRRLEEEGIKFIGPKHYSVAKMGDKIESK
KLAIEAKVNTIPGYNDAIAGPAEAVEIAKKIGYPVMIKASAGGGGKGLRVAYNDAEAFEG
FSSCVNEARNSFGDDRVFIEKYVLEPRHIEIQVLGDSHGNYVYLNERDCSIQRRHQKVIE
EAPSPFVDPEMRKAMGEQAVALARAVNYESAGTVEFVVSGATKEFYFLEMNTRLQVEHPV
TELITGLDLVEQMIRVAYGEKLPLTQADVQINGWAMECRINAEDPFRGFLPSTGRLVKFQ
PPKEIPGQVRVDTGVYDGGEISMFYDSMIAKLIVHGATREQAIARMRDALNGFVIRGISS
NIPFQAALMQHPVFHSGIFDTGFIPKHYPTGFDASMVPHDDPALLVSVAAYVYRAYTDRS
ASVSGQLQGHERIVGDQWMVVRLNKEGNEHHEVTARPIPGGYHVEYKGEQYEILSDWKLG
ESLFNGTCNGEEFTLQVERHKTKYSLFHWGTRADFMVMSARAAELLALMPEKPAPDLSKF
LLSPMPGLLREIAVQVGQEVKAGEKLAVIEAMKMENILKAEQDCKVKKISAAVGESLSVD
QIIIEFE
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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