SitesBLAST
Comparing WP_011444267.1 NCBI__GCF_000013325.1:WP_011444267.1 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)
3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
44% identity, 85% coverage: 171:1187/1197 of query aligns to 97:1123/1130 of 3va7A
- active site: H138 (= H208), E205 (= E275), E219 (= E289), N221 (= N291), V226 (= V296), E227 (= E297), R269 (= R339), A550 (vs. gap), I648 (≠ L706), L730 (≠ I784), D760 (= D813), N762 (≠ E815), F895 (≠ Y949)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y691), T641 (= T699), P653 (= P711), G656 (= G714), F658 (= F716), P943 (= P996), G944 (= G997), K1096 (= K1160)
- binding urea: D893 (= D947), Y937 (= Y991), G944 (= G997), G945 (= G998), Y946 (= Y999)
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, 37% coverage: 3:440/1197 of query aligns to 2:443/654 of P9WPQ3
- K322 (vs. gap) 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)
45% identity, 37% coverage: 6:442/1197 of query aligns to 3:442/448 of 2vpqB
- active site: V116 (≠ S119), 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 (≠ Y202), I201 (= I203), E273 (= E275), I275 (≠ L277), M286 (≠ L288), E287 (= E289)
- binding magnesium ion: E273 (= E275), E287 (= E289)
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)
46% identity, 36% coverage: 3:437/1197 of query aligns to 2:458/681 of Q5LUF3
- F348 (≠ Y349) 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
7ybuA Human propionyl-coenzyme a carboxylase
46% identity, 37% coverage: 3:443/1197 of query aligns to 5:449/670 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)
46% identity, 37% coverage: 3:443/1197 of query aligns to 63:507/728 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 (vs. gap) 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 (= P362) 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)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
46% identity, 36% coverage: 3:437/1197 of query aligns to 1:423/646 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:
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
45% identity, 37% coverage: 3:440/1197 of query aligns to 2:440/447 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 (≠ Y202), L204 (≠ I203), H209 (= H208), Q233 (= Q232), H236 (≠ N235), L278 (= L277), E288 (= E289), I437 (≠ T437)
- binding magnesium ion: E276 (= E275), E288 (= E289)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
45% identity, 37% coverage: 3:440/1197 of query aligns to 2:438/444 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 (= Y202), L202 (≠ I203), E274 (= E275), L276 (= L277), E286 (= E289), N288 (= N291), I435 (≠ T437)
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
43% identity, 36% coverage: 2:437/1197 of query aligns to 3:420/651 of 8j78I
Sites not aligning to the query:
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
44% identity, 36% coverage: 6:441/1197 of query aligns to 1:438/657 of 8sgxX
Sites not aligning to the query:
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
44% identity, 37% coverage: 3:440/1197 of query aligns to 2:437/442 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 (= Y202), L201 (≠ I203), H233 (≠ N235), L275 (= L277), E285 (= E289)
- binding magnesium ion: E273 (= E275), E285 (= E289)
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)
44% identity, 37% coverage: 3:440/1197 of query aligns to 2:435/440 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 (= Y202), L199 (≠ I203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (= L277), E283 (= E289), I432 (≠ T437)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
45% identity, 37% coverage: 1:441/1197 of query aligns to 4:444/446 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 (= Y202), I207 (= I203), H212 (= H208), Q236 (= Q232), H239 (≠ N235), L281 (= L277), E292 (= E289), T440 (= T437)
- binding calcium ion: E279 (= E275), E292 (= E289)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
45% identity, 37% coverage: 1:441/1197 of query aligns to 3:443/445 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 (= Y202), I206 (= I203), H211 (= H208), Q235 (= Q232), L280 (= L277), E291 (= E289), T439 (= T437)
- binding magnesium ion: E278 (= E275), E291 (= E289)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
47% identity, 36% coverage: 3:433/1197 of query aligns to 2:430/456 of 8hz4A
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, 37% coverage: 3:440/1197 of query aligns to 2:440/449 of P24182
- R19 (= R20) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ R24) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K117) binding ATP
- K159 (= K158) binding ATP
- GG 165:166 (= GG 164:165) binding ATP
- EKYL 201:204 (≠ ERYI 200:203) binding ATP
- H209 (= H208) binding ATP
- H236 (≠ N235) binding ATP
- K238 (= K237) binding hydrogencarbonate
- E276 (= E275) binding ATP; binding Mg(2+)
- E288 (= E289) binding ATP; binding Mg(2+)
- R292 (= R293) active site; binding hydrogencarbonate
- V295 (= V296) binding hydrogencarbonate
- E296 (= E297) mutation to A: Severe reduction in catalytic activity.
- R338 (= R339) binding biotin; binding hydrogencarbonate; mutation to A: Severe reduction in catalytic activity.
- F363 (vs. gap) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R366) mutation to E: Loss of homodimerization. No effect on ATP binding.
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
45% identity, 37% coverage: 3:440/1197 of query aligns to 2:440/445 of 3jziA
- 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 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K117), K159 (= K158), A160 (= A159), G164 (= G163), G165 (= G164), M169 (= M168), Y199 (≠ F198), E201 (= E200), K202 (≠ R201), Y203 (= Y202), H209 (= H208), Q233 (= Q232), H236 (≠ N235), L278 (= L277), I287 (≠ L288), E288 (= E289)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
45% identity, 37% coverage: 3:440/1197 of query aligns to 2:440/445 of 2w6oA
- 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 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K158), K202 (≠ R201), Y203 (= Y202), L204 (≠ I203), L278 (= L277), I437 (≠ T437)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
45% identity, 37% coverage: 3:440/1197 of query aligns to 2:440/445 of 2w6nA
- 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 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M156), K159 (= K158), M169 (= M168), E201 (= E200), K202 (≠ R201), Y203 (= Y202), L278 (= L277)
Query Sequence
>WP_011444267.1 NCBI__GCF_000013325.1:WP_011444267.1
MNFDTVLIANRGAIATRIIRTLRRMGLRSVAVYSEADKDSLHVVLADEAICIGAARAAES
YLNIPAILDAARRTGAGAIHPGYGFLAENVEFAEACEKEGIVFIGPTPNNIRTFGLKHSA
RALAAAHGVPLAPGTDLLTDETEAVQAANGIGYPVMLKATAGGGGIGMRVCEDEADVREG
FSAVARQGLGNFGDAGVFLERYIRQARHIEVQIFGDGRGRIVALGERDCSLQRRNQKVVE
EAPAPLLPPAVRSELIAAAIRLGQAAGYRSAGTVEFLYDAEREEFFFLEMNTRLQVEHGV
TEEVMGVDLVEWMVRGGGGDFGFLDDDPPRPSGHSIQVRLYAEDPALDYRPTSGTLTAVT
FPEGVRTETWCMAGTTVSTWYDPMLAKLIVHAESREAAVAAMQDALDRSRIDGFETNLRW
LRDVVRSPAFTSGEVSTRALSHVAHVPRSITVVSGGTATMAQDWPGRQRLWAVGVPPSGP
MDDLSFRLGNRLLGNPEGTAGLEVAITGPTLTFNTAARVCVTGADFGARLDGQPVPRGMA
IDIAAGQTLALGRASGGGMRGYILFAGGLDIAPYLGSRSTFELGQFGGHAARRLLAGDTL
HLGDEPAQPALPAANLPELSNEWALRVMYGPHGAPDFFTREDIDTLVAAEWQVHYNSNRT
GIRLVGPKPQWAREDGGEAGLHPSNIHDNPYAIGAVDFTGDMPIILGPDGPSLGGFVCPF
VVIAADRWKIGQLTPGDKLRFVPVNCADAAAANDQQRRFLETGKPAQGCPGRPMETLSPI
LAVIDESPRSPRTVYRQQGDRNILVEYGPIVLDIELRIRVQALMTELERLALPGVIDIVP
GIRSLQFHFDGDAMTQEAALSVLIAAEERLGDLEDFTIPSRIVHLPLSWRDPATIETIEK
YMGAVRDDAPWCPDNIEFIRRINGLPDVAAVENLIFEANYLVLGLGDVYLGAPVATPVDP
RHRLVTTKYNPARTWTPPNVVGIGGAYMCIYGMEGPGGYQLFGRTIQVWNTHRQTDAFID
GKPWLLRFFDQIRFYPVSAEELEEWRRDFPAGRRSIRIEPSEFRLADYRRYLADNAEGIA
EFEARRQAAFDEERAEWQRRGEFDRTDLVEPEAAEAGTVEVPDGADLVEAPFGGSVWKML
VSVGDEVEAGETIAIIEAMKMECRVESPGAGTVAALYAQERQSVQPGTPMLALTRHA
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