SitesBLAST
Comparing WP_055435097.1 NCBI__GCF_001418085.1:WP_055435097.1 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)
O81852 Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 71% coverage: 323:1126/1131 of query aligns to 85:908/916 of O81852
- I441 (= I661) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q663) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (≠ F738) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (≠ N740) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
35% identity, 39% coverage: 329:764/1131 of query aligns to 3:453/458 of 3c1nA
- binding threonine: G7 (= G333), G8 (= G334), T9 (≠ K335), S10 (= S336), W227 (≠ Y540), T228 (= T541), D229 (≠ H542), A406 (vs. gap), I409 (≠ T720), A410 (≠ F721), N423 (≠ I734), I424 (≠ P735), Q429 (≠ N740), E433 (≠ G744)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
35% identity, 39% coverage: 329:764/1131 of query aligns to 3:458/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G333), T229 (= T541), D230 (≠ H542), V231 (= V543), Y235 (= Y547), T237 (≠ A549), D238 (≠ N550), P239 (= P551), R240 (≠ D552), K265 (≠ T577), V266 (≠ I578)
- binding aspartic acid: S39 (= S365), T45 (= T371), F192 (= F504), R206 (= R518), G207 (≠ N519), S209 (= S521)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
35% identity, 39% coverage: 329:764/1131 of query aligns to 3:462/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K331), G7 (= G333), G8 (= G334), S39 (= S365), T229 (= T541), D230 (≠ H542), Y235 (= Y547), D238 (≠ N550), P239 (= P551), R240 (≠ D552), K265 (≠ T577), V266 (≠ I578)
- binding aspartic acid: T45 (= T371), E129 (= E439), F192 (= F504), R206 (= R518), G207 (≠ N519), S209 (= S521)
O94671 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 31% coverage: 774:1129/1131 of query aligns to 8:367/376 of O94671
- S201 (= S961) modified: Phosphoserine
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
34% identity, 32% coverage: 771:1129/1131 of query aligns to 2:357/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
34% identity, 32% coverage: 771:1129/1131 of query aligns to 2:357/358 of 1q7gA
- active site: D218 (= D987), K222 (= K991)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G782), V14 (≠ L783), V15 (= V784), E39 (≠ N814), N91 (= N862), T92 (= T863), S93 (= S864), I97 (≠ F868), P114 (≠ S885), K116 (= K887), A143 (≠ T915), S173 (= S945), K222 (= K991), A338 (= A1110), T343 (= T1115)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
34% identity, 32% coverage: 771:1129/1131 of query aligns to 2:357/358 of 1ebuD
- active site: D218 (= D987), K222 (= K991)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G780), A12 (≠ H781), G13 (= G782), V14 (≠ L783), V15 (= V784), E39 (≠ N814), A40 (≠ S815), N91 (= N862), S93 (= S864), K116 (= K887), T343 (= T1115)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
34% identity, 32% coverage: 771:1129/1131 of query aligns to 2:357/358 of 1ebfA
- active site: D218 (= D987), K222 (= K991)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ F779), A12 (≠ H781), G13 (= G782), V14 (≠ L783), V15 (= V784), E39 (≠ N814), A40 (≠ S815), T92 (= T863), S93 (= S864), P114 (≠ S885)
P31116 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
34% identity, 32% coverage: 771:1129/1131 of query aligns to 3:358/359 of P31116
- A13 (≠ H781) binding NAD(+)
- V15 (≠ L783) binding NAD(+)
- V16 (= V784) binding NAD(+)
- A41 (≠ S815) binding NAD(+)
- H79 (≠ F848) mutation to A: Reduces kcat 2-fold.
- T93 (= T863) binding NAD(+)
- K117 (= K887) mutation to A: Loss of activity.
- E143 (= E914) binding Na(+)
- V146 (= V917) binding Na(+)
- A148 (= A919) binding Na(+)
- L150 (= L921) binding Na(+)
- E208 (= E976) binding L-homoserine; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D987) binding L-homoserine; mutation to L: Reduces kcat 150-fold.
- K223 (= K991) mutation to V: Loss of activity.
- H309 (≠ S1079) mutation to A: Reduces kcat 40-fold. Affects dimer formation.
- G340 (= G1111) binding NAD(+)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
30% identity, 39% coverage: 329:768/1131 of query aligns to 6:459/470 of 2cdqA
- binding lysine: S40 (= S365), A41 (= A366), T46 (= T371), E124 (= E439), M327 (≠ L637), Q330 (≠ K640), F333 (≠ V643), L334 (≠ D644), S347 (= S657), V348 (= V658), D349 (≠ S659)
- binding s-adenosylmethionine: G345 (≠ N655), I346 (= I656), S347 (= S657), W368 (vs. gap), S369 (≠ N680), R370 (= R681), L372 (≠ V683), E376 (= E689)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
28% identity, 39% coverage: 331:768/1131 of query aligns to 6:446/447 of 2j0xA
- binding aspartic acid: F182 (= F504), G197 (≠ N519), G198 (= G520), S199 (= S521), D200 (≠ N522)
- binding lysine: M316 (≠ L637), S319 (≠ K640), F322 (≠ V643), L323 (≠ D644), S336 (= S657), V337 (= V658), D338 (≠ S659), S343 (= S666), E344 (= E667)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
28% identity, 39% coverage: 331:768/1131 of query aligns to 6:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T541), D220 (≠ H542), I224 (= I546), Y225 (= Y547), D228 (≠ N550), R230 (≠ D552), K255 (≠ T577), V256 (≠ I578)
- binding aspartic acid: S37 (= S365), T43 (= T371), E117 (= E439), F182 (= F504), R196 (= R518), G197 (≠ N519), S199 (= S521)
P08660 Lysine-sensitive aspartokinase 3; Aspartate kinase III; AKIII; Lysine-sensitive aspartokinase III; EC 2.7.2.4 from Escherichia coli (strain K12) (see paper)
28% identity, 39% coverage: 331:768/1131 of query aligns to 8:448/449 of P08660
- K8 (= K331) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E439) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R518) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (≠ N522) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
O60163 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 32% coverage: 406:768/1131 of query aligns to 113:495/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
P10869 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
23% identity, 40% coverage: 318:769/1131 of query aligns to 5:502/527 of P10869
- K18 (= K331) mutation K->R,A,Q: Reduces kcat.
- G25 (≠ A338) mutation to D: Decreases affinity for aspartate and ATP.
- K26 (≠ N339) mutation to I: Decreases affinity for aspartate and ATP.
- E254 (≠ H542) mutation to A: Reduces kcat.
- E279 (= E567) mutation to A: Reduces kcat and affects inhibition by threonine.
- H292 (= H580) mutation to A: Reduces kcat.
- A406 (≠ G671) mutation to T: Decreases enzyme stability.
- R419 (≠ I684) mutation to A: Reduces kcat.
- G452 (vs. gap) mutation to D: Disrupts threonine binding.
- H497 (= H764) mutation to A: Reduces kcat.
P45131 Homoserine O-acetyltransferase; HAT; Homoserine O-trans-acetylase; Homoserine transacetylase; HTA; EC 2.3.1.31 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see 2 papers)
27% identity, 26% coverage: 17:315/1131 of query aligns to 20:352/358 of P45131
- L306 (≠ F269) mutation to R: Can no longer use acetyl-CoA as acyl donor, but can use succinyl-CoA.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5w8oB Homoserine transacetylase metx from mycobacterium hassiacum (see paper)
28% identity, 25% coverage: 38:315/1131 of query aligns to 37:339/346 of 5w8oB
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
25% identity, 39% coverage: 329:764/1131 of query aligns to 4:390/397 of 5yeiC
- binding lysine: M342 (≠ L718), H345 (≠ F721), A346 (vs. gap), G347 (vs. gap), V348 (vs. gap), A349 (vs. gap), S350 (≠ H722)
- binding threonine: T265 (≠ K640), P266 (≠ V641), A269 (≠ D644), Q288 (= Q663), N362 (vs. gap), I363 (= I734)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
24% identity, 33% coverage: 329:705/1131 of query aligns to 5:345/405 of P61489
- K7 (= K331) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G333) mutation to M: Loss of aspartokinase activity.
- G10 (= G334) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S365) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A366) mutation to S: Loss of aspartokinase activity.
- T47 (= T371) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E439) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G503) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R518) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (≠ N522) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.; mutation to N: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- D174 (≠ H542) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (≠ N550) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
Query Sequence
>WP_055435097.1 NCBI__GCF_001418085.1:WP_055435097.1
MTDLQYIDSIDYVTQSGKATKIKLSYQVFGKALHTAPIVLVNHALTGNSNVAGEGGWWSD
LVGDNKVIDTKQYTVLAFNIPGNGYDGFLIENYKDFIARDIAKLFLIGLEKLNINSVYAM
VGGSLGGGIAWEMAVLKPNLATHFIPVATDWKATDWLMANCQIQEQFLVNSKNPVHDARM
HAMLCYRTPESFKSRFQRSKNEDLDLFNVESWLLHHGNKLQERFQLSAYKLMNQLLRTID
VTKGREPNTNVLDVIQSETTIVAVDSDLFFTAEENRETQKQLALTHSNVTYNEINSIHGH
DAFLIEFEQLENIIKGIFKPALKEKKMKILKFGGKSLANGEGLNRVISIIENKVKAEENI
AVVVSARGKATDQLESILEKAVKDEAYATDFDAFKNDQKGTIVVDFETEFLRLESLFAGV
QLLGDYSPKIKDEVLAQGELISAKLITGLLVDKNINAKVADARTFIKTDDTFGNAKPIDA
LSKKNVVAYFKQNNGTTVNIVTGFIASNRDNKTTTLGRNGSNYTAALLANYLDAEELQNY
THVNGIYTANPDLVADAIKIERLSFTEANELANFGTTILHAKTIIPLIEKNIPLRILNTF
NPEDKGTIITAQNKDKGIRSLSVLDNVALVNIEGRGLLGKVGVDARIFTALSKENISVSI
ISQGSSERGIGLVIEAEHANRAVIVLEQEFENDFYSQDINKISVIDDVSVISIIGQELST
FHKPFNNLIKNQIIPILFNNTITGENVSIVVKKKELHKAVNVIHGEIFGISKKINLAIFG
HGLVGGALVNQIIASAKDIEKRKGIKLNIFAIANSQKALFSKNGIDENWKNTLETNGENY
KIEDVFQFAKDNHLENLIAIDNTSSLEFVSNYIKLVEQGFDLVSSNKIANTIDLEFYNEL
RNTLEKHQKSYLYETNVGAGLPLIDTIKLLHLSGENIVRIRGVFSGSLSYLFNTFSSEDT
SFATVLQQALDKGFTEPNPREDLSGNDVARKLLILARELDLHNEIGDVTIENLIPEPLRE
IETSQFLDSLDEMNTVFQKIKEAQKEGHVLRYIGDLHGDLSQENGAQLDVKLESVPSQSP
LGALQGADSIFEIYTESYGEKPIVIQGAGAGASVTARGVFGDILRLTEKNN
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