SitesBLAST
Comparing Echvi_3962 FitnessBrowser__Cola:Echvi_3962 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
51% identity, 94% coverage: 6:472/499 of query aligns to 7:475/670 of 7ybuA
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)
51% identity, 94% coverage: 6:472/499 of query aligns to 65:533/728 of P05165
- A75 (= A16) to P: in PA-1; dbSNP:rs794727479
- R77 (= R18) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A79) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I105) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ H138) to E: in PA-1
- M229 (= M170) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q238) to R: in PA-1
- D368 (= D309) to G: in PA-1
- M373 (≠ Q314) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G320) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ T339) to R: in PA-1
- R399 (= R340) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P363) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L471) natural variant: Missing (in PA-1)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
50% identity, 89% coverage: 7:448/499 of query aligns to 5:448/654 of P9WPQ3
- K322 (≠ A322) 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, 97% coverage: 6:491/499 of query aligns to 4:509/681 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, 97% coverage: 6:491/499 of query aligns to 3:474/646 of 3n6rG
- active site: K115 (= K118), K157 (= K160), D180 (= D196), H193 (= H210), R219 (= R236), T258 (= T275), E260 (= E277), E273 (= E290), N275 (= N292), R277 (= R294), E281 (= E298), R323 (= R340)
Sites not aligning to the query:
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
47% identity, 93% coverage: 7:469/499 of query aligns to 1:463/657 of 8sgxX
Sites not aligning to the query:
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
50% identity, 89% coverage: 5:446/499 of query aligns to 3:440/456 of 8hz4A
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
49% identity, 89% coverage: 5:446/499 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ A120), K156 (= K160), H206 (= H210), R232 (= R236), T271 (= T275), E273 (= E277), E287 (= E290), N289 (= N292), R291 (= R294), E295 (= E298), R337 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K118), I154 (≠ L158), K156 (= K160), G161 (= G165), G163 (= G167), I166 (≠ M170), F200 (≠ Y204), I201 (= I205), E273 (= E277), I275 (= I279), M286 (≠ L289), E287 (= E290)
- binding magnesium ion: E273 (= E277), E287 (= E290)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 89% coverage: 4:448/499 of query aligns to 2:442/442 of 4mv4A
- active site: K116 (= K118), K159 (= K160), D193 (≠ G197), H206 (= H210), R232 (= R236), T271 (= T275), E273 (= E277), E285 (= E290), N287 (= N292), R289 (= R294), E293 (= E298), R335 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K160), G164 (= G165), M166 (= M170), E198 (= E202), Y200 (= Y204), L201 (≠ I205), H233 (= H237), L275 (≠ I279), E285 (= E290)
- binding magnesium ion: E273 (= E277), E285 (= E290)
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)
48% identity, 89% coverage: 4:448/499 of query aligns to 2:440/440 of 6oi8A
- active site: K116 (= K118), K159 (= K160), D191 (≠ G197), H204 (= H210), R230 (= R236), T269 (= T275), E271 (= E277), E283 (= E290), N285 (= N292), R287 (= R294), E291 (= E298), R333 (= R340)
- 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 (≠ L158), K159 (= K160), M164 (= M170), E196 (= E202), Y198 (= Y204), L199 (≠ I205), H204 (= H210), Q228 (= Q234), E271 (= E277), L273 (≠ I279), E283 (= E290), I432 (≠ T440)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
48% identity, 89% coverage: 4:448/499 of query aligns to 2:439/439 of 4mv3A
- active site: K116 (= K118), K159 (= K160), D190 (≠ G197), H203 (= H210), R229 (= R236), T268 (= T275), E270 (= E277), E282 (= E290), N284 (= N292), R286 (= R294), E290 (= E298), R332 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K160), M163 (= M170), E195 (= E202), Y197 (= Y204), L198 (≠ I205), E270 (= E277), L272 (≠ I279), E282 (= E290)
- binding bicarbonate ion: R286 (= R294), Q288 (= Q296), V289 (= V297)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
48% identity, 89% coverage: 1:445/499 of query aligns to 1:452/1150 of A0A0H3JRU9
- R21 (= R21) mutation to A: Complete loss of catalytic activity.
- K119 (= K118) binding
- K161 (= K160) binding
- H211 (= H210) binding
- E278 (= E277) binding
- K411 (= K404) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding
- 542 binding
- 580 A→T: Complete loss of catalytic activity.
- 614 R→A: Complete loss of catalytic activity.
- 621 Y→A: Complete loss of catalytic activity.
- 712 binding
- 741 binding
- 743 binding
- 838 Q→A: About 2.5-fold loss of catalytic activity.
- 876 T→A: Complete loss of catalytic activity.
- 879 S→A: About 2-fold loss of catalytic activity.
- 880 K→T: Complete loss of catalytic activity.
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
49% identity, 89% coverage: 6:448/499 of query aligns to 4:443/444 of 2vr1A
- active site: K116 (= K118), K159 (= K160), D194 (≠ G197), H207 (= H210), R233 (= R236), T272 (= T275), E274 (= E277), E286 (= E290), N288 (= N292), R290 (= R294), E294 (= E298), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K160), R165 (≠ K168), M167 (= M170), Y201 (= Y204), L202 (≠ I205), E274 (= E277), L276 (≠ I279), E286 (= E290), N288 (= N292), I435 (≠ T440)
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, 89% coverage: 5:446/499 of query aligns to 5:445/453 of 7kctA
- active site: E276 (= E277), E289 (= E290), N291 (= N292), E297 (= E298), R339 (= R340)
- binding adenosine-5'-diphosphate: K117 (= K118), L157 (= L158), K159 (= K160), G164 (= G165), G165 (= G166), G166 (= G167), I169 (≠ M170), E201 (= E202), Y203 (= Y204), I204 (= I205), H209 (= H210), Q233 (= Q234), Q237 (= Q238), K238 (= K239), I278 (= I279), E289 (= E290), R293 (= R294), Q295 (= Q296), V296 (= V297), E297 (= E298), R339 (= R340)
- binding bicarbonate ion: D116 (= D117), R119 (≠ A120)
- binding magnesium ion: E276 (= E277), E289 (= E290)
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, 89% coverage: 4:448/499 of query aligns to 2:445/448 of P43873
- K116 (= K118) binding
- K159 (= K160) binding
- EKYL 201:204 (≠ EKYI 202:205) binding
- E276 (= E277) binding ; binding
- E288 (= E290) binding ; binding
- N290 (= N292) binding
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, 89% coverage: 4:448/499 of query aligns to 2:445/445 of 6ojhA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding calcium ion: E276 (= E277), E288 (= E290), N290 (= N292)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K160), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (≠ I205), H236 (= H237), L278 (≠ I279), E288 (= E290), I437 (≠ T440)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
48% identity, 89% coverage: 4:447/499 of query aligns to 2:430/430 of 4mv1A
- active site: K116 (= K118), K159 (= K160), D182 (≠ Q191), H195 (= H210), R221 (= R236), T260 (= T275), E262 (= E277), E274 (= E290), N276 (= N292), R278 (= R294), E282 (= E298), R324 (= R340)
- binding adenosine-5'-diphosphate: K159 (= K160), E187 (= E202), K188 (= K203), Y189 (= Y204), L190 (≠ I205), L264 (≠ I279)
- binding phosphate ion: K224 (= K239), R278 (= R294), Q280 (= Q296), V281 (= V297), E282 (= E298)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
49% identity, 89% coverage: 3:446/499 of query aligns to 5:446/446 of 3ouuA
- active site: K162 (= K160), G168 (= G166), G169 (= G167), H212 (= H210), K241 (= K239), T277 (= T275), E279 (= E277), E292 (= E290), N294 (= N292), V299 (= V297), E300 (= E298), R341 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K118), I160 (≠ L158), K162 (= K160), G167 (= G165), G168 (= G166), G169 (= G167), M172 (= M170), E204 (= E202), Y206 (= Y204), I207 (= I205), H212 (= H210), Q236 (= Q234), H239 (= H237), L281 (≠ I279), E292 (= E290), T440 (= T440)
- binding calcium ion: E279 (= E277), E292 (= E290)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
49% identity, 89% coverage: 3:446/499 of query aligns to 4:445/445 of 3ouzA
- active site: K161 (= K160), G167 (= G166), G168 (= G167), H211 (= H210), K240 (= K239), T276 (= T275), E278 (= E277), E291 (= E290), N293 (= N292), V298 (= V297), E299 (= E298), R340 (= R340)
- binding adenosine-5'-diphosphate: K119 (= K118), I159 (≠ L158), K161 (= K160), G166 (= G165), G168 (= G167), M171 (= M170), E203 (= E202), Y205 (= Y204), I206 (= I205), H211 (= H210), Q235 (= Q234), L280 (≠ I279), E291 (= E290), T439 (= T440)
- binding magnesium ion: E278 (= E277), E291 (= E290)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
49% identity, 89% coverage: 6:448/499 of query aligns to 4:445/449 of P24182
- R19 (= R21) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (= E25) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K118) binding
- K159 (= K160) binding
- GG 165:166 (= GG 166:167) binding
- EKYL 201:204 (≠ EKYI 202:205) binding
- H209 (= H210) binding
- H236 (= H237) binding
- K238 (= K239) binding
- E276 (= E277) binding ; binding
- E288 (= E290) binding ; binding
- R292 (= R294) active site; binding
- V295 (= V297) binding
- E296 (= E298) mutation to A: Severe reduction in catalytic activity.
- R338 (= R340) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ P366) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R369) mutation to E: Loss of homodimerization. No effect on ATP binding.
Query Sequence
>Echvi_3962 FitnessBrowser__Cola:Echvi_3962
MPKIRKILVANRGEIALRIMRTIREMGLKSVAVYSEVDKNAPHVLYADESYCLGPAPSHK
SYLLGERIIEACQALGADAIHPGYGFLSENTAFAKKVADAGLIFIGPSPESIEIMGDKLA
AKKAVSHYDIPMVPGTDHAILDIQEAKKTAVEIGYPILIKASAGGGGKGMRIVQDEGEFE
EQMKRAVSEAQSAFGDGAVFIEKYITSPRHIEIQILADQHGNYLHLFERECSVQRRHQKV
IEEAPSAVVNQEMRKAMGQAAIDVAKACQYYGAGTVEFIVDEALNFYFLEMNTRLQVEHP
VTEMITGKDLVREQIFIAEGQALSFAQDDLTILGHAIETRVYAEDPTNNFLPDIGKLATY
RLPQGPGIRVDDGFREGMEIPIYYDPMIAKLVTFEEDRPKAIQKMVRAIDDYHITGISTT
LSFARFVMLHPAFQSGEFDTKFVEKHFAPSKLAENFSEEEEEILATIAAYLLPNAKQPST
NVNGQDQNNSKWKTRRMNG
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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