SitesBLAST
Comparing BPHYT_RS25975 BPHYT_RS25975 urea carboxylase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
43% identity, 82% coverage: 202:1188/1203 of query aligns to 132:1129/1130 of 3va7A
- active site: H138 (= H208), E205 (= E275), E219 (= E289), N221 (= N291), V226 (= V296), E227 (= E297), R269 (= R339), A550 (vs. gap), I648 (≠ L710), L730 (vs. gap), D760 (= D805), N762 (= N807), F895 (≠ Y941)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y695), T641 (= T703), P653 (= P715), G656 (= G718), F658 (= F720), P943 (= P988), G944 (= G989), K1096 (= K1155)
- binding urea: D893 (= D939), Y937 (= Y983), G944 (= G989), G945 (= G990), Y946 (= Y991)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
49% identity, 36% coverage: 3:440/1203 of query aligns to 1:426/646 of 3n6rG
- active site: K115 (= K117), K157 (= K158), D180 (≠ A195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E289), N275 (= N291), R277 (= R293), E281 (= E297), R323 (= R339)
Sites not aligning to the query:
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)
47% identity, 36% coverage: 3:440/1203 of query aligns to 2:461/681 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
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
45% identity, 36% coverage: 4:440/1203 of query aligns to 1:440/448 of 2vpqB
- active site: V116 (≠ T119), 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 (= K117), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (= F202), I201 (≠ V203), E273 (= E275), I275 (≠ V277), M286 (≠ L288), E287 (= E289)
- binding magnesium ion: E273 (= E275), E287 (= E289)
7ybuA Human propionyl-coenzyme a carboxylase
45% identity, 36% coverage: 3:441/1203 of query aligns to 5:447/670 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)
45% identity, 36% coverage: 3:441/1203 of query aligns to 63:505/728 of P05165
- A75 (= A15) to P: in PA-1; dbSNP:rs794727479
- R77 (= R17) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A78) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I104) 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 (= 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 (≠ V338) to R: in PA-1
- R399 (= R339) to Q: in PA-1; dbSNP:rs1301904623
- P423 (vs. gap) to L: in PA-1; dbSNP:rs1443858896
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 532 natural variant: Missing (in PA-1)
- 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)
45% identity, 40% coverage: 3:479/1203 of query aligns to 2:485/654 of P9WPQ3
- K322 (≠ L321) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 37% coverage: 3:442/1203 of query aligns to 2:442/447 of 2vqdA
- active site: K116 (= K117), K159 (= K158), P196 (≠ A195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E289), N290 (= N291), R292 (= R293), E296 (= E297), R338 (= R339)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K117), I157 (≠ M156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (= F202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (≠ N235), L278 (≠ V277), E288 (= E289), I437 (≠ T437)
- binding magnesium ion: E276 (= E275), E288 (= E289)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
46% identity, 37% coverage: 3:442/1203 of query aligns to 2:439/456 of 8hz4A
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)
44% identity, 37% coverage: 3:451/1203 of query aligns to 4:450/453 of 7kctA
- active site: E276 (= E275), E289 (= E289), N291 (= N291), E297 (= E297), R339 (= R339)
- binding adenosine-5'-diphosphate: K117 (= K117), L157 (≠ M156), K159 (= K158), G164 (= G163), G165 (= G164), G166 (= G165), I169 (≠ M168), E201 (= E200), Y203 (≠ F202), I204 (≠ V203), H209 (= H208), Q233 (= Q232), Q237 (= Q236), K238 (= K237), I278 (≠ V277), E289 (= E289), R293 (= R293), Q295 (= Q295), V296 (= V296), E297 (= E297), R339 (= R339)
- binding bicarbonate ion: D116 (≠ L116), R119 (≠ T119)
- binding magnesium ion: E276 (= E275), E289 (= E289)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
39% identity, 38% coverage: 2:459/1203 of query aligns to 3:469/1150 of A0A0H3JRU9
- R21 (= R20) mutation to A: Complete loss of catalytic activity.
- K119 (= K117) binding
- K161 (= K158) binding
- H211 (= H208) binding
- E278 (= E275) binding
- K411 (≠ A401) 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.
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
43% identity, 37% coverage: 3:442/1203 of query aligns to 2:439/442 of 4mv4A
- active site: K116 (= K117), K159 (= K158), D193 (≠ A195), 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 (= M168), E198 (= E200), Y200 (≠ F202), L201 (≠ V203), H233 (≠ N235), L275 (≠ V277), E285 (= E289)
- binding magnesium ion: E273 (= E275), E285 (= E289)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
44% identity, 36% coverage: 6:440/1203 of query aligns to 1:437/657 of 8sgxX
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
43% identity, 36% coverage: 5:442/1203 of query aligns to 4:440/444 of 2vr1A
- active site: K116 (= K117), K159 (= K158), D194 (≠ A195), 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 (≠ I166), M167 (= M168), Y201 (≠ F202), L202 (≠ V203), E274 (= E275), L276 (≠ V277), E286 (= E289), N288 (= N291), I435 (≠ T437)
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, 37% coverage: 3:442/1203 of query aligns to 2:437/440 of 6oi8A
- active site: K116 (= K117), K159 (= K158), D191 (≠ A195), 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 (= M168), E196 (= E200), Y198 (≠ F202), L199 (≠ V203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (≠ V277), E283 (= E289), I432 (≠ T437)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
43% identity, 36% coverage: 5:440/1203 of query aligns to 5:453/1129 of 3tw6B
- active site: K124 (= K117), K162 (= K158), H212 (= H208), R238 (= R234), T277 (= T273), E279 (= E275), E293 (= E289), N295 (= N291), R297 (= R293), E301 (= E297), R349 (= R339)
- binding adenosine-5'-diphosphate: K124 (= K117), K162 (= K158), G167 (= G163), G169 (= G165), M172 (= M168), E204 (= E200), L206 (≠ F202), V207 (= V203), H212 (= H208), Q236 (= Q232), N239 (= N235), L281 (≠ V277), E293 (= E289), T450 (= T437)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R339), D395 (= D382)
- binding magnesium ion: E279 (= E275), E293 (= E289)
Sites not aligning to the query:
- active site: 544, 650, 713, 742, 744, 877
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 1102
- binding magnesium ion: 529, 530, 532, 763
- binding zinc ion: 544, 713, 742, 744
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
43% identity, 37% coverage: 1:442/1203 of query aligns to 3:444/445 of 3ouzA
- active site: K161 (= K158), G167 (= G164), G168 (= G165), H211 (= H208), K240 (= K237), T276 (= T273), E278 (= E275), E291 (= E289), N293 (= N291), V298 (= V296), E299 (= E297), R340 (= R339)
- binding adenosine-5'-diphosphate: K119 (= K117), I159 (≠ M156), K161 (= K158), G166 (= G163), G168 (= G165), M171 (= M168), E203 (= E200), Y205 (≠ F202), I206 (≠ V203), H211 (= H208), Q235 (= Q232), L280 (≠ V277), E291 (= E289), T439 (= T437)
- binding magnesium ion: E278 (= E275), E291 (= E289)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
43% identity, 37% coverage: 1:442/1203 of query aligns to 4:445/446 of 3ouuA
- active site: K162 (= K158), G168 (= G164), G169 (= G165), H212 (= H208), K241 (= K237), T277 (= T273), E279 (= E275), E292 (= E289), N294 (= N291), V299 (= V296), E300 (= E297), R341 (= R339)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K117), I160 (≠ M156), K162 (= K158), G167 (= G163), G168 (= G164), G169 (= G165), M172 (= M168), E204 (= E200), Y206 (≠ F202), I207 (≠ V203), H212 (= H208), Q236 (= Q232), H239 (≠ N235), L281 (≠ V277), E292 (= E289), T440 (= T437)
- binding calcium ion: E279 (= E275), E292 (= E289)
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
43% identity, 37% coverage: 3:442/1203 of query aligns to 2:442/445 of 6ojhA
- active site: K116 (= K117), K159 (= K158), D196 (≠ A195), 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 (= M168), E201 (= E200), Y203 (≠ F202), L204 (≠ V203), H236 (≠ N235), L278 (≠ V277), E288 (= E289), I437 (≠ T437)
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)
43% identity, 37% coverage: 3:442/1203 of query aligns to 2:442/448 of P43873
- K116 (= K117) binding
- K159 (= K158) binding
- EKYL 201:204 (≠ EKFV 200:203) binding
- E276 (= E275) binding ; binding
- E288 (= E289) binding ; binding
- N290 (= N291) binding
Query Sequence
>BPHYT_RS25975 BPHYT_RS25975 urea carboxylase
MRFRKVLIANRGEIACRVIRTLKRLGIASVAVYSEADRHAMHVMLADEAVCIGPALAAQS
YLNSAAILDAARACGADAVHPGYGFLSENAAFAQACDDAGIRFIGPTPQHMREFGLKHTA
RELAQANDVALLPGTGLLPDVSAALREAESIGYPVMLKSTAGGGGIGMSLCRDAAQLEGV
FASVARLGEANFANAGVYVEKFVENARHIEVQVFGDGKGGVISLGERDCSVQRRNQKVIE
ETPAPGLTHAERSALHASAVRLAQAVKYKSAGTVEFVFDADTRRFYFLEVNTRLQVEHCV
TEEITGIDLVEWMIREAEGELAPLDTLATVPQGASIQVRLYAEDPHKQFQPSAGVLTHVA
FAADARVDTWVDSGTEVSAFYDPLLAKLIVKGETREAGLAALRAALEQTQLYGIETNLDY
LRAIAGSATFARGEQTTAFLGRFMFAPHTIDVLDGGVQTTVQQTPGRTGYWDIGVPPSGP
MDDLSFRLANELLGNPADAAGLECAMVGATLRFNTATLFVLGGAPLAATLDGAPVTLWQV
TRAPAGAVLKLGGVTGAGMRACLALKGGLQVPDYLGSKATFTLGQFGGHAGRALRKGDVL
HLADEAGSGAAGAQLDKSRVPVLTHDWTLGVLDGPHGAPDFFTPDDIAMLYGTRWTVHYN
SSRTGVRLIGPKPQWARTDGGEAGLHPSNIHDNAYAVGAVDFTGDMPVILGPDGPSLGGF
VCPVTVVGEELWKLGQLRPGDTVRFERMPVKAMLASPKHAMEASEAAAHDCILYRDPTAG
EGTGVVYRRSGDQNVLIEYGPLVLDLNLRFRVHALMNWLDAHRLPGIIDLTPGIRSLQVH
FDPRVLSHDTLLAHLQQAERELPAVDAMRVPNRIVHLPLSWDDPSTRIAIERYMQSVRPD
APWCPSNIEFIRRINGLNSIDDVKRIVFDARYLVMGLGDVYLGAPVATPLDPRHRLVTTK
YNPARTWTPENAVGIGGAYLCVYGMEGPGGYQFVGRTVQMWNRYRTTREFEAGKPWLLRF
FDEIRFYEVSEAELAELRTDFIAGRASLKIEESVFDLGAYNRFLKDEADSIAAFKSTQQA
AFDAERERWDAAGHAAYVGETDGDAAAGGNPANDTLATGQQGIVADVSGSVWKLLVKEGE
RVGDGQVVAIVESMKMEISVTASGDGVIETIDCAEGAAVVAGQRLMVMRAGIAADATEEA
TCK
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