SitesBLAST
Comparing WP_010876437.1 NCBI__GCF_000008645.1:WP_010876437.1 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)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
31% identity, 96% coverage: 5:393/406 of query aligns to 3:444/458 of 3c1nA
- binding threonine: G7 (= G9), G8 (= G10), T9 (= T11), S10 (= S12), W227 (≠ V179), T228 (= T180), D229 (= D181), A406 (≠ T357), I409 (= I360), A410 (≠ I361), N423 (= N374), I424 (= I375), Q429 (vs. gap), E433 (≠ Q382)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
30% identity, 96% coverage: 5:393/406 of query aligns to 3:449/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G9), T229 (= T180), D230 (= D181), V231 (= V182), Y235 (≠ M186), T237 (= T188), D238 (= D189), P239 (= P190), R240 (≠ N191), K265 (≠ Q216), V266 (= V217)
- binding aspartic acid: S39 (= S41), T45 (= T47), F192 (= F143), R206 (= R157), G207 (= G158), S209 (= S160)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
30% identity, 96% coverage: 5:393/406 of query aligns to 3:453/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K7), G7 (= G9), G8 (= G10), S39 (= S41), T229 (= T180), D230 (= D181), Y235 (≠ M186), D238 (= D189), P239 (= P190), R240 (≠ N191), K265 (≠ Q216), V266 (= V217)
- binding aspartic acid: T45 (= T47), E129 (= E75), F192 (= F143), R206 (= R157), G207 (= G158), S209 (= S160)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
31% identity, 100% coverage: 1:406/406 of query aligns to 1:401/405 of P61489
- K7 (= K7) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G9) mutation to M: Loss of aspartokinase activity.
- G10 (= G10) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S41) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A42) mutation to S: Loss of aspartokinase activity.
- T47 (= T47) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E75) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G142) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R157) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D161) 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 (= D181) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D189) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
31% identity, 96% coverage: 3:390/406 of query aligns to 2:378/397 of 5yeiC
- binding lysine: M342 (≠ F354), H345 (≠ T357), A346 (≠ P358), G347 (= G359), V348 (≠ I360), A349 (≠ I361), S350 (= S362)
- binding threonine: T265 (≠ K281), P266 (= P282), A269 (≠ L285), Q288 (≠ I302), N362 (= N374), I363 (= I375)
P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 2 papers)
30% identity, 97% coverage: 1:393/406 of query aligns to 1:393/421 of P26512
- G277 (= G283) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ L285) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (vs. gap) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ I300) mutation to F: Absence of inhibition upon addition of threonine and lysine or lysine alone.; mutation to Y: Feedback-resistant and enhanced expression of the asd gene.
- V360 (≠ I360) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ I361) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (= E363) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ I364) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
30% identity, 97% coverage: 1:393/406 of query aligns to 1:393/421 of P41398
- D345 (≠ A345) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
30% identity, 97% coverage: 3:397/406 of query aligns to 2:396/585 of 3l76A
- binding lysine: D286 (≠ N298), I287 (vs. gap), D288 (vs. gap), M353 (≠ F354), R356 (≠ T357), I359 (= I360), S380 (= S381), E381 (≠ Q382)
- binding threonine: R269 (≠ K281), V272 (≠ I284), A273 (≠ L285), Q292 (≠ I300), N373 (= N374), I374 (= I375)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
29% identity, 97% coverage: 1:393/406 of query aligns to 1:376/392 of 3aawC
- binding lysine: K7 (= K7), S41 (= S41), G136 (= G159), S137 (= S160), D138 (= D161), M337 (≠ F354), H340 (≠ T357), T344 (≠ I361), S364 (= S381)
- binding threonine: K258 (= K281), G260 (= G283), E261 (≠ I284), A262 (≠ L285), Q281 (vs. gap), N357 (= N374), I358 (= I375)
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)
26% identity, 98% coverage: 5:401/406 of query aligns to 91:547/916 of O81852
- I441 (= I302) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (vs. gap) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I378) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (vs. gap) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 76% coverage: 5:314/406 of query aligns to 6:363/470 of 2cdqA
- binding lysine: S40 (= S41), A41 (= A42), T46 (= T47), E124 (= E75), M327 (≠ I278), Q330 (≠ K281), F333 (≠ I284), L334 (= L285), S347 (≠ N298), V348 (≠ I299), D349 (≠ I300)
- binding s-adenosylmethionine: G345 (≠ S296), I346 (= I297), S347 (≠ N298)
Sites not aligning to the query:
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 98% coverage: 4:402/406 of query aligns to 16:491/519 of O60163
- S326 (≠ D241) modified: Phosphoserine
- T328 (≠ S243) modified: Phosphothreonine
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
28% identity, 96% coverage: 3:393/406 of query aligns to 2:355/370 of 3ab4A
- binding lysine: M316 (≠ F354), H319 (≠ T357), P320 (= P358), V322 (≠ I360), T323 (≠ I361), S343 (= S381), E344 (≠ Q382)
- binding threonine: K239 (= K281), G241 (= G283), E242 (≠ I284), A243 (≠ L285), Q262 (vs. gap), N336 (= N374), I337 (= I375)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
25% identity, 98% coverage: 2:399/406 of query aligns to 1:439/447 of 2j0xA
- binding aspartic acid: F182 (= F143), G197 (= G158), G198 (= G159), S199 (= S160), D200 (= D161)
- binding lysine: M316 (≠ I278), S319 (≠ K281), F322 (≠ I284), L323 (= L285), S336 (≠ N298), V337 (≠ I299), D338 (≠ I300), S343 (≠ G305), E344 (≠ Q306)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
25% identity, 98% coverage: 2:399/406 of query aligns to 1:439/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T180), D220 (= D181), I224 (≠ V185), Y225 (≠ M186), D228 (= D189), R230 (≠ N191), K255 (≠ Q216), V256 (= V217)
- binding aspartic acid: S37 (≠ V39), T43 (vs. gap), E117 (= E75), F182 (= F143), R196 (= R157), G197 (= G158), S199 (= S160)
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)
25% identity, 98% coverage: 2:399/406 of query aligns to 3:441/449 of P08660
- K8 (= K7) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E75) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R157) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D161) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
23% identity, 98% coverage: 1:397/406 of query aligns to 1:428/439 of 3tviE
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
22% identity, 97% coverage: 3:397/406 of query aligns to 1:420/429 of 3tviA
2ji5A Structure of ump kinase from pyrococcus furiosus complexed with utp
40% identity, 16% coverage: 160:224/406 of query aligns to 122:184/219 of 2ji5A
Sites not aligning to the query:
Q8U122 Uridylate kinase; UK; Uridine monophosphate kinase; UMP kinase; UMPK; EC 2.7.4.22 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see paper)
39% identity, 14% coverage: 160:216/406 of query aligns to 120:176/225 of Q8U122
- T120 (≠ S160) binding Mg(2+)
- D121 (= D161) binding Mg(2+); binding Mg(2+)
Sites not aligning to the query:
- 6 binding Mg(2+)
- 44 binding UMP
- 66 binding UMP
- 114:120 binding UMP
- 179 binding UMP
- 182 binding Mg(2+)
Query Sequence
>WP_010876437.1 NCBI__GCF_000008645.1:WP_010876437.1
MELIVAKFGGTSIGNGRRIKKAARSVVKEYMKGRKVVVVVSAINKTTDELLQIVDEAMED
AVTEKQLAEIVSMGEMTSVRIFSSAIEALGVKSEYIDPFMDEWPIITDSNLLNAKVDFEA
TEEKSRELLKLLDQGIIPVVCGFLGRDPNGYITTLGRGGSDITAFLLGHCLKADEVIIVT
DVGGVMSTDPNKLQGAKKLDKISVEEMRDLATHGAQVLHPHALKYKDPDIKAKIIGFEHG
DLSAPGTEIIGPSKNKMVKTTTLNPDPISVVAVVGEKILNKPGILARLTSRLAENSINII
GISTGQNSVTIFVDKKDADEAHRLLHDVVIADDDLSSLSLGRDIAMITISSPDFIDTPGI
ISEITKPLRDNDLNIVEISSSQTSVVIFVDWNDGKKAYELVRGVLE
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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