SitesBLAST
Comparing WP_013418382.1 NCBI__GCF_000166055.1:WP_013418382.1 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)
8xl6A Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
43% identity, 98% coverage: 6:677/684 of query aligns to 1:660/660 of 8xl6A
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
41% identity, 99% coverage: 4:679/684 of query aligns to 2:651/651 of 8j78I
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 97% coverage: 6:668/684 of query aligns to 2:644/654 of P9WPQ3
- K322 (≠ T323) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
44% identity, 95% coverage: 6:656/684 of query aligns to 2:643/666 of 8rthA
7ybuA Human propionyl-coenzyme a carboxylase (see paper)
38% identity, 99% coverage: 4:677/684 of query aligns to 3:670/670 of 7ybuA
8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
38% identity, 99% coverage: 4:677/684 of query aligns to 1:668/668 of 8xl5A
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, 66% coverage: 6:458/684 of query aligns to 2:475/681 of Q5LUF3
- F348 (= F351) 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
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)
38% identity, 99% coverage: 4:677/684 of query aligns to 61:728/728 of P05165
- A75 (= A18) to P: in PA-1; dbSNP:rs794727479
- R77 (= R20) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A81) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V107) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G140) to E: in PA-1
- M229 (= M172) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q240) to R: in PA-1; dbSNP:rs2063109875
- D368 (= D310) to G: in PA-1
- M373 (≠ Q315) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G321) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A340) to R: in PA-1
- R399 (= R341) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P364) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ V467) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W495) to L: in PA-1; dbSNP:rs118169528
- G631 (= G573) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G617) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K643) modified: N6-biotinyllysine; by HLCS
- C712 (≠ V661) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
49% identity, 64% coverage: 8:448/684 of query aligns to 2:443/448 of 2vpqB
- active site: V116 (≠ A122), K156 (= K162), H206 (= H212), R232 (= R238), T271 (= T277), E273 (= E279), E287 (= E291), N289 (= N293), R291 (= R295), E295 (= E299), R337 (= R341)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K120), I154 (≠ L160), K156 (= K162), G161 (= G167), G163 (= G169), I166 (≠ M172), F200 (= F206), I201 (≠ V207), E273 (= E279), I275 (≠ V281), M286 (≠ I290), E287 (= E291)
- binding magnesium ion: E273 (= E279), E287 (= E291)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
48% identity, 66% coverage: 6:458/684 of query aligns to 1:440/646 of 3n6rG
- active site: K115 (= K120), K157 (= K162), D180 (= D199), H193 (= H212), R219 (= R238), T258 (= T277), E260 (= E279), E273 (= E291), N275 (= N293), R277 (= R295), E281 (= E299), R323 (= R341)
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
48% identity, 64% coverage: 8:448/684 of query aligns to 4:441/444 of 2vr1A
- active site: K116 (= K120), K159 (= K162), D194 (= D199), H207 (= H212), R233 (= R238), T272 (= T277), E274 (= E279), E286 (= E291), N288 (= N293), R290 (= R295), E294 (= E299), R336 (= R341)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K162), R165 (≠ K170), M167 (= M172), Y201 (≠ F206), L202 (≠ V207), E274 (= E279), L276 (≠ V281), E286 (= E291), N288 (= N293), I435 (≠ T442)
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, 65% coverage: 6:449/684 of query aligns to 4:445/453 of 7kctA
- active site: E276 (= E279), E289 (= E291), N291 (= N293), E297 (= E299), R339 (= R341)
- binding adenosine-5'-diphosphate: K117 (= K120), L157 (= L160), K159 (= K162), G164 (= G167), G165 (= G168), G166 (= G169), I169 (≠ M172), E201 (= E204), Y203 (≠ F206), I204 (≠ V207), H209 (= H212), Q233 (= Q236), Q237 (= Q240), K238 (= K241), I278 (≠ V281), E289 (= E291), R293 (= R295), Q295 (= Q297), V296 (= V298), E297 (= E299), R339 (= R341)
- binding bicarbonate ion: D116 (≠ S119), R119 (≠ A122)
- binding magnesium ion: E276 (= E279), E289 (= E291)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
47% identity, 65% coverage: 6:448/684 of query aligns to 2:440/442 of 4mv4A
- active site: K116 (= K120), K159 (= K162), D193 (= D199), H206 (= H212), R232 (= R238), T271 (= T277), E273 (= E279), E285 (= E291), N287 (= N293), R289 (= R295), E293 (= E299), R335 (= R341)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K162), G164 (= G167), M166 (= M172), E198 (= E204), Y200 (≠ F206), L201 (≠ V207), H233 (= H239), L275 (≠ V281), E285 (= E291)
- binding magnesium ion: E273 (= E279), E285 (= E291)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
46% identity, 65% coverage: 6:448/684 of query aligns to 2:437/439 of 4mv3A
- active site: K116 (= K120), K159 (= K162), D190 (= D199), H203 (= H212), R229 (= R238), T268 (= T277), E270 (= E279), E282 (= E291), N284 (= N293), R286 (= R295), E290 (= E299), R332 (= R341)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K162), M163 (= M172), E195 (= E204), Y197 (≠ F206), L198 (≠ V207), E270 (= E279), L272 (≠ V281), E282 (= E291)
- binding bicarbonate ion: R286 (= R295), Q288 (= Q297), V289 (= V298)
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, 65% coverage: 6:448/684 of query aligns to 2:438/440 of 6oi8A
- active site: K116 (= K120), K159 (= K162), D191 (= D199), H204 (= H212), R230 (= R238), T269 (= T277), E271 (= E279), E283 (= E291), N285 (= N293), R287 (= R295), E291 (= E299), R333 (= R341)
- 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 (≠ L160), K159 (= K162), M164 (= M172), E196 (= E204), Y198 (≠ F206), L199 (≠ V207), H204 (= H212), Q228 (= Q236), E271 (= E279), L273 (≠ V281), E283 (= E291), I432 (≠ T442)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
50% identity, 65% coverage: 6:447/684 of query aligns to 2:439/456 of 8hz4A
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
47% identity, 65% coverage: 6:448/684 of query aligns to 2:443/445 of 6ojhA
- active site: K116 (= K120), K159 (= K162), D196 (= D199), H209 (= H212), R235 (= R238), T274 (= T277), E276 (= E279), E288 (= E291), N290 (= N293), R292 (= R295), E296 (= E299), R338 (= R341)
- binding calcium ion: E276 (= E279), E288 (= E291), N290 (= N293)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K162), M169 (= M172), E201 (= E204), Y203 (≠ F206), L204 (≠ V207), H236 (= H239), L278 (≠ V281), E288 (= E291), I437 (≠ T442)
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)
47% identity, 65% coverage: 6:448/684 of query aligns to 2:443/448 of P43873
- K116 (= K120) binding ATP
- K159 (= K162) binding ATP
- EKYL 201:204 (≠ ERFV 204:207) binding ATP
- E276 (= E279) binding ATP; binding Mg(2+)
- E288 (= E291) binding ATP; binding Mg(2+)
- N290 (= N293) binding Mg(2+)
8uz2C E. Coli acetyl-coa carboxylase, narrow helical local reconstruction, 3.18 angstrom
48% identity, 64% coverage: 8:448/684 of query aligns to 4:443/446 of 8uz2C
- binding adenosine-5'-diphosphate: K116 (= K120), K159 (= K162), G164 (= G167), G165 (= G168), G166 (= G169), M169 (= M172), H209 (= H212), Q233 (= Q236), H236 (= H239), L278 (≠ V281), E288 (= E291), I437 (≠ T442)
- binding magnesium ion: E276 (= E279), E288 (= E291)
- binding : R356 (≠ Q360), I410 (≠ E415)
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)
48% identity, 64% coverage: 8:448/684 of query aligns to 4:443/446 of 6oi9A
- active site: E276 (= E279), E288 (= E291), N290 (= N293), E296 (= E299), R338 (= R341)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K162), M169 (= M172), E201 (= E204), Y203 (≠ F206), L204 (≠ V207), H209 (= H212), Q233 (= Q236), H236 (= H239), E276 (= E279), L278 (≠ V281), E288 (= E291), I437 (≠ T442)
Query Sequence
>WP_013418382.1 NCBI__GCF_000166055.1:WP_013418382.1
MTLRPFASLLIANRGEIACRIVRTARRMGLRTIAVYSEADARARHMKAADDARLIGPAPA
RDSYLDIGRIIEAAKASGAEAVHPGYGFLSEKAAFGEACAEAGLIFVGPPASAIRSMGSK
AAAKALMEAAGVPVVPGYGGAAQDAAAFAREAKRLGFPVLLKAVAGGGGKGMRIVRAADE
LEVALTAAKREAAAAFGDDTLMMERFVERPRHIEVQIFADSHGNVVSLFERECTLQRRHQ
KVVEEAPSPSLDDARREALCDAARKAAAAIGYVGAGTVEFVADETNAWFIEMNTRLQVEH
AVTEAITGLDLVEWQLRVAMGETLPLRQEEIARAGHAIEARIYAEDADAGFLPSTGTITQ
WRAPQAGQGLRIDTGFGAGDEVTPHYDPMLAKLIAHAPTRAAALARLRGVLSGFEIAGVA
TNVAFLARLLGEGAVAANAIDTGYIEREHAGLDASHTPGAVHLAAAVAAILSREADETRR
DPADPWSPWVAGAAWVADAACVAGAAWALFGSRGRVFEFRGKDGHAFTVRLEQSRNGMTL
AVEGEAARFAFERERGDPHRFAVTLGGARRAIGAVYGDGAVTVFDGPQPIRLAPVDPFAA
EATTHHHGTGTLAPMPGTVLTLLAEPGASLEAGAPILILEAMKMEHTVRAPSRGRVARYA
VAIGDFVSEGAALMEFEAEEARDG
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