SitesBLAST
Comparing WP_013645478.1 NCBI__GCF_000191585.1:WP_013645478.1 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)
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)
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
31% identity, 80% coverage: 3:326/406 of query aligns to 2:390/397 of 5yeiC
- binding lysine: M342 (≠ I278), H345 (≠ K281), A346 (≠ T282), G347 (= G283), V348 (= V284), A349 (≠ L285), S350 (= S286)
- binding threonine: T265 (vs. gap), P266 (vs. gap), A269 (vs. gap), Q288 (vs. gap), N362 (= N298), I363 (= I299)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
31% 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 (= K216), 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)
31% 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 (= K216), 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)
28% 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.
P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (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 (≠ Y300) 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 (≠ R363) 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.
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: 5:403/406 of query aligns to 91:549/916 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.
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
30% 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 (≠ V284), A262 (≠ L285), Q281 (vs. gap), N357 (= N374), I358 (= I375)
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
28% 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 (= V284), A273 (≠ L285), Q292 (≠ Y300), 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
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 54% coverage: 5:224/406 of query aligns to 6:273/470 of 2cdqA
Sites not aligning to the query:
- binding lysine: 327, 330, 333, 334, 347, 348, 349
- binding s-adenosylmethionine: 345, 346, 347, 368, 369, 370, 372, 376
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, 100% coverage: 2:405/406 of query aligns to 3:447/449 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.
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
25% identity, 100% coverage: 2:405/406 of query aligns to 1:445/447 of 2j0xA
- binding aspartic acid: F182 (= F143), G197 (= G158), G198 (= G159), S199 (= S160), D200 (= D161)
- binding lysine: M316 (≠ I278), S319 (≠ K281), F322 (≠ V284), L323 (= L285), S336 (≠ N298), V337 (≠ I299), D338 (≠ Y300), S343 (≠ G305), E344 (≠ Q306)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
25% identity, 100% coverage: 2:405/406 of query aligns to 1:445/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T180), D220 (= D181), I224 (≠ V185), Y225 (≠ M186), D228 (= D189), R230 (≠ N191), K255 (= K216), V256 (= V217)
- binding aspartic acid: S37 (= S41), T43 (= T47), E117 (= E75), F182 (= F143), R196 (= R157), G197 (= G158), S199 (= S160)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
25% identity, 98% coverage: 1:397/406 of query aligns to 1:428/439 of 3tviE
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 (≠ V284), A243 (≠ L285), Q262 (vs. gap), N336 (= N374), I337 (= I375)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 94% coverage: 4:385/406 of query aligns to 16:472/519 of O60163
- S326 (≠ N255) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
25% 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
38% identity, 16% coverage: 160:224/406 of query aligns to 122:184/219 of 2ji5A
Sites not aligning to the query:
2bmuB Ump kinase from pyrococcus furiosus complexed with its substrate ump and its substrate analog amppnp (see paper)
38% identity, 14% coverage: 160:214/406 of query aligns to 121:175/226 of 2bmuB
Sites not aligning to the query:
- binding phosphoaminophosphonic acid-adenylate ester: 9, 10, 44, 45, 46, 182, 183, 184
- binding magnesium ion: 7, 183, 184
- binding uridine-5'-monophosphate: 44, 45, 67, 70, 71, 114, 115, 116, 119, 120, 179
Query Sequence
>WP_013645478.1 NCBI__GCF_000191585.1:WP_013645478.1
MEIIVAKFGGTSIGNGDRIRKAAESVVKEYMKGKKVVVVVSAINKTTDDILKTVDDAIGE
SITPKQLADIVSMGEITSVRIFSSTIESLGVKSEYIDPRAEGWPIITDSDYLNADVNFEL
TEKKCEELIKILDQGIIPVLCGFVGRDEDGTITTLGRGGSDITAFLLGHCLKAEEVVIVT
DVGGVMSTDPNRLQSAKKLDKISVEEMRDLATHGAKVLHPHALKYKDPLINAKIIGFEHG
DLSAAGTEIIGPAGNHMLKTTALNVEPISVIAVVGEEILTKTGVLSELTDALAQNSINIY
GISTGQNSVTLFIDKSIVDRAHNILHEVVVENQDLSSISVGTDIAMITVTSQDFIDTPGI
ITRITEPLRKKKINIVEISSSQTSVVVFVEWKDGKRAYELVRSVLE
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