SitesBLAST
Comparing WP_011868345.1 NCBI__GCF_000016125.1:WP_011868345.1 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)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
67% identity, 99% coverage: 3:463/468 of query aligns to 2:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G8), T229 (= T230), D230 (= D231), V231 (= V232), Y235 (≠ L236), T237 (≠ A238), D238 (= D239), P239 (= P240), R240 (= R241), K265 (= K266), V266 (= V267)
- binding aspartic acid: S39 (= S40), T45 (= T46), F192 (= F193), R206 (= R207), G207 (= G208), S209 (= S210)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
67% identity, 99% coverage: 3:463/468 of query aligns to 2:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K6), G7 (= G8), G8 (= G9), S39 (= S40), T229 (= T230), D230 (= D231), Y235 (≠ L236), D238 (= D239), P239 (= P240), R240 (= R241), K265 (= K266), V266 (= V267)
- binding aspartic acid: T45 (= T46), E129 (= E130), F192 (= F193), R206 (= R207), G207 (= G208), S209 (= S210)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
67% identity, 99% coverage: 3:463/468 of query aligns to 2:458/458 of 3c1nA
- binding threonine: G7 (= G8), G8 (= G9), T9 (= T10), S10 (= S11), W227 (= W229), T228 (= T230), D229 (= D231), A406 (= A411), I409 (= I414), A410 (= A415), N423 (= N428), I424 (= I429), Q429 (= Q434), E433 (= E438)
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)
35% identity, 99% coverage: 1:461/468 of query aligns to 88:551/916 of O81852
- I441 (= I352) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q354) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I432) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q434) 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)
33% identity, 98% coverage: 4:463/468 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (= S40), A41 (= A41), T46 (= T46), E124 (= E130), M327 (= M328), Q330 (≠ V331), F333 (≠ T334), L334 (≠ A335), S347 (≠ N348), V348 (= V349), D349 (≠ I350)
- binding s-adenosylmethionine: G345 (≠ N346), I346 (≠ A347), S347 (≠ N348), W368 (≠ E371), S369 (≠ A372), R370 (≠ K373), L372 (≠ C375), E376 (= E378)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 98% coverage: 4:463/468 of query aligns to 17:496/519 of O60163
- S326 (≠ V308) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
31% identity, 98% coverage: 4:461/468 of query aligns to 4:393/397 of 5yeiC
- binding lysine: M342 (= M408), H345 (≠ A411), A346 (≠ K412), G347 (= G413), V348 (≠ I414), A349 (= A415), S350 (≠ G416)
- binding threonine: T265 (≠ V331), P266 (≠ S332), A269 (= A335), Q288 (= Q354), N362 (= N428), I363 (= I429)
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, 99% coverage: 2:463/468 of query aligns to 4:449/449 of P08660
- K8 (= K6) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E130) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R207) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D211) 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)
28% identity, 99% coverage: 2:463/468 of query aligns to 2:447/447 of 2j0xA
- binding aspartic acid: F182 (= F193), G197 (= G208), G198 (= G209), S199 (= S210), D200 (= D211)
- binding lysine: M316 (= M328), S319 (≠ V331), F322 (≠ T334), L323 (≠ A335), S336 (≠ N348), V337 (= V349), D338 (≠ I350), S343 (= S357), E344 (= E358)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
28% identity, 99% coverage: 2:463/468 of query aligns to 2:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T230), D220 (= D231), I224 (≠ V235), Y225 (≠ L236), D228 (= D239), R230 (= R241), K255 (= K266), V256 (= V267)
- binding aspartic acid: S37 (= S40), T43 (= T46), E117 (= E130), F182 (= F193), R196 (= R207), G197 (= G208), S199 (= S210)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
30% identity, 99% coverage: 2:463/468 of query aligns to 3:438/439 of 3tviE
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
31% identity, 84% coverage: 71:461/468 of query aligns to 15:400/405 of P61489
- S41 (= S99) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (≠ S100) mutation to S: Loss of aspartokinase activity.
- T47 (≠ E105) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E130) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G192) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R207) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D211) 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 (= D231) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D239) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
Sites not aligning to the query:
- 7 K→A: Loss of aspartokinase activity.; K→M: Loss of aspartokinase activity.
- 9 G→M: Loss of aspartokinase activity.
- 10 G→A: Significant decrease in the catalytic efficiency.
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
29% identity, 98% coverage: 2:461/468 of query aligns to 1:428/429 of 3tviA
P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
31% identity, 73% coverage: 120:461/468 of query aligns to 64:405/421 of P41398
- D345 (= D395) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
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)
31% identity, 73% coverage: 120:461/468 of query aligns to 64:405/421 of P26512
- G277 (= G333) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A335) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q354) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (vs. gap) 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 (≠ I414) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A415) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ K417) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ L418) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
29% identity, 98% coverage: 4:461/468 of query aligns to 4:404/585 of 3l76A
- binding lysine: D286 (≠ N348), I287 (≠ V349), D288 (≠ I350), M353 (= M408), R356 (≠ A411), I359 (= I414), S380 (= S437), E381 (= E438)
- binding threonine: R269 (≠ V331), V272 (≠ T334), A273 (= A335), Q292 (= Q354), N373 (= N428), I374 (= I429)
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)
30% identity, 73% coverage: 120:461/468 of query aligns to 64:388/392 of 3aawC
- binding lysine: G136 (= G209), S137 (= S210), D138 (= D211), M337 (= M408), H340 (≠ A411), T344 (≠ A415), S364 (= S437)
- binding threonine: K258 (≠ V331), G260 (= G333), E261 (≠ T334), A262 (= A335), Q281 (= Q354), N357 (= N428), I358 (= I429)
Sites not aligning to the query:
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
27% identity, 73% coverage: 120:461/468 of query aligns to 63:367/370 of 3ab4A
- binding lysine: M316 (= M408), H319 (≠ A411), P320 (≠ K412), V322 (≠ I414), T323 (≠ A415), S343 (= S437), E344 (= E438)
- binding threonine: K239 (≠ V331), G241 (= G333), E242 (≠ T334), A243 (= A335), Q262 (= Q354), N336 (= N428), I337 (= I429)
2re1A Crystal structure of aspartokinase alpha and beta subunits
35% identity, 28% coverage: 333:461/468 of query aligns to 24:146/148 of 2re1A
2dt9A Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus (see paper)
31% identity, 29% coverage: 327:461/468 of query aligns to 16:152/153 of 2dt9A
Query Sequence
>WP_011868345.1 NCBI__GCF_000016125.1:WP_011868345.1
MVTVMKFGGTSVGNGERIRNVAKIVVNKTNEDKDVVVVTSAMTQVTNSLVEISAQALDVR
DIAKINNFIEDLRRKHEIAIEQAIENHDIRVEVSKTIQSSINDLEKVLVGVSYLGELTPK
SKDFILSFGERLSAPILSGAIRDMGKHSLFLAGRDAGIITDDTFTCAKILRLDVADKIEP
LLKDGFIPVVTGFVAGTEEGHITTLGRGGSDYSAALVGRGLMANMVEIWTDVSGVLSADP
RMVENVKKIPKMSYIEAMELAYFGAKVLHPRTMEPVMEKKIPLRIKNTFEPENEGTLITD
SSETSNGVIKAITTIKDVILINIFGGGMVGVSGTAARIFNVLGKSNANVILITQGSSETN
ISIVIYDGELEAKKCVRELRSEFGECHLIKDISFDKDVCVVSVVGSGMKGAKGIAGKLFD
AVAESGANIKMIAQGSSETNISFVINEDKLEPCLKNLHKTFVEDDINF
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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