SitesBLAST
Comparing WP_012467305.1 NCBI__GCF_000020465.1:WP_012467305.1 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)
40% identity, 96% coverage: 3:455/471 of query aligns to 3:462/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T230), D230 (= D231), V231 (= V232), Y235 (≠ M236), T237 (≠ C238), D238 (= D239), P239 (= P240), R240 (= R241), K265 (= K266), V266 (= V267)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (≠ Y193), R206 (= R207), G207 (= G208), S209 (= S210)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
40% identity, 96% coverage: 3:455/471 of query aligns to 3:466/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T230), D230 (= D231), Y235 (≠ M236), D238 (= D239), P239 (= P240), R240 (= R241), K265 (= K266), V266 (= V267)
- binding aspartic acid: T45 (= T44), E129 (= E127), F192 (≠ Y193), R206 (= R207), G207 (= G208), S209 (= S210)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
40% identity, 96% coverage: 3:455/471 of query aligns to 3:457/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W229), T228 (= T230), D229 (= D231), A406 (≠ S406), I409 (≠ V409), A410 (= A410), N423 (= N421), I424 (≠ L422), Q429 (= Q427), E433 (= E431)
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)
39% identity, 97% coverage: 1:455/471 of query aligns to 4:448/449 of P08660
- K8 (= K5) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E127) 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)
39% identity, 97% coverage: 1:455/471 of query aligns to 2:446/447 of 2j0xA
- binding aspartic acid: F182 (≠ Y193), G197 (= G208), G198 (= G209), S199 (= S210), D200 (= D211)
- binding lysine: M316 (= M333), S319 (≠ R336), F322 (= F339), L323 (≠ M340), S336 (= S353), V337 (≠ I354), D338 (≠ E355), S343 (= S360), E344 (= E361)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
39% identity, 97% coverage: 1:455/471 of query aligns to 2:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T230), D220 (= D231), I224 (≠ V235), Y225 (≠ M236), D228 (= D239), R230 (= R241), K255 (= K266), V256 (= V267)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E127), F182 (≠ Y193), R196 (= R207), G197 (= G208), S199 (= S210)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
37% identity, 96% coverage: 3:455/471 of query aligns to 6:459/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E127), M327 (= M333), Q330 (≠ R336), F333 (= F339), L334 (≠ M340), S347 (= S353), V348 (≠ I354), D349 (≠ E355)
- binding s-adenosylmethionine: G345 (= G351), I346 (≠ V352), S347 (= S353), W368 (≠ F373), S369 (= S374), R370 (≠ E375), L372 (= L377), E376 (vs. gap)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 100% coverage: 3:471/471 of query aligns to 17:508/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
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)
32% identity, 97% coverage: 2:460/471 of query aligns to 90:557/916 of O81852
- I441 (= I357) 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 (= I425) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q427) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 97% coverage: 1:457/471 of query aligns to 3:439/439 of 3tviE
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 96% coverage: 1:454/471 of query aligns to 1:428/429 of 3tviA
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
31% identity, 96% coverage: 1:454/471 of query aligns to 2:393/397 of 5yeiC
- binding lysine: M342 (≠ L403), H345 (≠ S406), A346 (≠ K407), G347 (= G408), V348 (= V409), A349 (= A410), S350 (≠ G411)
- binding threonine: T265 (≠ R336), P266 (≠ Y337), A269 (≠ M340), Q288 (≠ S359), N362 (= N421), I363 (≠ L422)
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, 75% coverage: 117:470/471 of query aligns to 64:419/421 of P26512
- G277 (= G338) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ M340) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (≠ S359) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ V362) 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 (= V409) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A410) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R412) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ I413) 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)
31% identity, 75% coverage: 117:470/471 of query aligns to 64:419/421 of P41398
- D345 (≠ A394) 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, 72% coverage: 117:454/471 of query aligns to 63:404/585 of 3l76A
- binding lysine: D286 (≠ S353), I287 (= I354), D288 (≠ E355), M353 (≠ L403), R356 (≠ S406), I359 (≠ V409), S380 (= S430), E381 (= E431)
- binding threonine: R269 (= R336), V272 (≠ F339), A273 (≠ M340), Q292 (vs. gap), N373 (= N421), I374 (≠ L422)
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)
31% identity, 72% coverage: 117:457/471 of query aligns to 64:391/392 of 3aawC
- binding lysine: G136 (= G209), S137 (= S210), D138 (= D211), M337 (≠ L403), H340 (≠ S406), T344 (≠ A410), S364 (= S430)
- binding threonine: K258 (≠ R336), G260 (= G338), E261 (≠ F339), A262 (≠ M340), Q281 (≠ S359), N357 (≠ R423), I358 (≠ M424)
Sites not aligning to the query:
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
28% identity, 72% coverage: 117:454/471 of query aligns to 64:400/405 of P61489
- E74 (= E127) 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.
- 41 S→A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- 42 A→S: Loss of aspartokinase activity.
- 47 T→A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
30% identity, 57% coverage: 189:457/471 of query aligns to 98:370/370 of 3ab4A
- binding lysine: M316 (≠ L403), H319 (≠ S406), P320 (≠ K407), V322 (= V409), T323 (≠ A410), S343 (= S430), E344 (= E431)
- binding threonine: K239 (≠ R336), G241 (= G338), E242 (≠ F339), A243 (≠ M340), Q262 (vs. gap), N336 (≠ R423), I337 (≠ M424)
2re1A Crystal structure of aspartokinase alpha and beta subunits
32% identity, 30% coverage: 314:454/471 of query aligns to 2:146/148 of 2re1A
2v4yA The structure of e. Coli ump kinase in complex with its allosteric regulator gtp (see paper)
29% identity, 37% coverage: 128:300/471 of query aligns to 77:237/237 of 2v4yA
- binding guanosine-5'-triphosphate: D89 (≠ E140), H92 (= H143), N97 (≠ D149), A98 (≠ V150), R99 (= R151), W115 (≠ G175), A116 (= A176), S120 (≠ P180), R123 (≠ D183), R126 (≠ T186), T140 (= T203)
Sites not aligning to the query:
Query Sequence
>WP_012467305.1 NCBI__GCF_000020465.1:WP_012467305.1
MAVMKFGGTSVGNARAMQQAIDLVVREKLNGAPLVVLSACSGITNKLVRLAEASGRSALD
EALLLAGEVRQHHIDLTAELIQAPELQAELEAKVEEYVAGLEMLARGVDIVGELTERSKD
TFCSFGELLSTTIFAAAMKEQGHDAEWLDVRRVMITDDNHGFARPLGDICRENAGAIISP
LLDAGTIVITQGYIGAALNGRTTTLGRGGSDYSAALLGAWLNANAIQIWTDVDGVMTCDP
RLVPEARSIRIMTFSEAAELAYLGAKVLHPDTIAPAVEKNIPVWVLNTWHPDAKGTLITD
DTERLSGMSYGGLVKSIAVKKGQCIINVRSNRMLGRYGFMAELFGAFSRYGVSIEMISSS
EVSVSVTVDDTCFSEELLQDLRVLGQVDIEHRVATVSVVGDNLRMSKGVAGRIFSSLRDV
NLRMISQGASEINVGFVVEENDVERAVNTLHHEFFSGEETAGIFEKPAGTS
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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