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Comparing CA265_RS23475 FitnessBrowser__Pedo557:CA265_RS23475 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)
40% identity, 99% coverage: 3:814/817 of query aligns to 91:910/916 of O81852
- I441 (= I347) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q349) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I428) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q430) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
42% identity, 56% coverage: 3:458/817 of query aligns to 3:462/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T225), D230 (= D226), V231 (= V227), Y235 (≠ M231), T237 (≠ A233), D238 (= D234), P239 (= P235), R240 (= R236), K265 (= K261), V266 (= V262)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (= F188), R206 (= R202), G207 (= G203), S209 (= S205)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
42% identity, 56% coverage: 3:458/817 of query aligns to 3:466/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T225), D230 (= D226), Y235 (≠ M231), D238 (= D234), P239 (= P235), R240 (= R236), K265 (= K261), V266 (= V262)
- binding aspartic acid: T45 (= T44), E129 (= E124), F192 (= F188), R206 (= R202), G207 (= G203), S209 (= S205)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
42% identity, 56% coverage: 3:458/817 of query aligns to 3:457/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W224), T228 (= T225), D229 (= D226), A406 (≠ T407), I409 (≠ M410), A410 (≠ S411), N423 (= N424), I424 (≠ V425), Q429 (= Q430), E433 (= E434)
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 40% coverage: 462:789/817 of query aligns to 5:341/376 of O94671
- S201 (≠ G652) modified: Phosphoserine
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
32% identity, 56% coverage: 3:458/817 of query aligns to 6:459/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E124), M327 (= M323), Q330 (≠ K326), F333 (= F329), L334 (≠ S330), S347 (≠ V345), V348 (≠ L346), D349 (≠ I347)
- binding s-adenosylmethionine: G345 (≠ N343), I346 (≠ V344), S347 (≠ V345), W368 (≠ Q367), S369 (≠ A368), R370 (≠ I369), L372 (= L371), E376 (= E377)
P31116 Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
38% identity, 43% coverage: 463:813/817 of query aligns to 4:356/359 of P31116
- 11:18 (vs. 470:477, 38% identical) binding
- T93 (= T555) binding
- K117 (= K579) binding
- E208 (= E667) binding ; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D678) mutation to L: Reduces kcat 150-fold.
- K223 (= K682) mutation to V: Loss of activity.
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
38% identity, 43% coverage: 463:813/817 of query aligns to 3:355/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
38% identity, 43% coverage: 463:813/817 of query aligns to 3:355/358 of 1q7gA
- active site: D218 (= D678), K222 (= K682)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G473), V14 (≠ N474), V15 (≠ I475), E39 (≠ N505), N91 (= N554), T92 (= T555), S93 (≠ A556), I97 (≠ P560), P114 (≠ C577), K116 (= K579), A143 (≠ T607), S173 (= S637), K222 (= K682), A338 (= A796), T343 (= T801)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
38% identity, 43% coverage: 463:813/817 of query aligns to 3:355/358 of 1ebuD
- active site: D218 (= D678), K222 (= K682)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G471), A12 (≠ T472), G13 (= G473), V14 (≠ N474), V15 (≠ I475), E39 (≠ N505), A40 (≠ T506), N91 (= N554), S93 (≠ A556), K116 (= K579), T343 (= T801)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
38% identity, 43% coverage: 463:813/817 of query aligns to 3:355/358 of 1ebfA
- active site: D218 (= D678), K222 (= K682)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ L470), A12 (≠ T472), G13 (= G473), V14 (≠ N474), V15 (≠ I475), E39 (≠ N505), A40 (≠ T506), T92 (= T555), S93 (≠ A556), P114 (≠ C577)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
32% identity, 56% coverage: 3:458/817 of query aligns to 4:446/447 of 2j0xA
- binding aspartic acid: F182 (= F188), G197 (= G203), G198 (= G204), S199 (= S205), D200 (= D206)
- binding lysine: M316 (= M323), S319 (≠ K326), F322 (= F329), L323 (≠ S330), S336 (≠ N343), V337 (= V344), D338 (≠ V345), S343 (= S350), E344 (≠ S351)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
32% identity, 56% coverage: 3:458/817 of query aligns to 4:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T225), D220 (= D226), I224 (≠ M230), Y225 (≠ M231), D228 (= D234), R230 (= R236), K255 (= K261), V256 (= V262)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E124), F182 (= F188), R196 (= R202), G197 (= G203), S199 (= S205)
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)
32% identity, 56% coverage: 3:458/817 of query aligns to 6:448/449 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 (= E124) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R202) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D206) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 56% coverage: 3:461/817 of query aligns to 17:498/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
34% identity, 35% coverage: 175:457/817 of query aligns to 152:436/439 of 3tviE
Sites not aligning to the query:
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
33% identity, 35% coverage: 175:457/817 of query aligns to 148:428/429 of 3tviA
Sites not aligning to the query:
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
28% identity, 56% coverage: 3:460/817 of query aligns to 4:396/397 of 5yeiC
- binding lysine: M342 (= M404), H345 (≠ T407), A346 (≠ P408), G347 (= G409), V348 (≠ M410), A349 (≠ S411), S350 (≠ G412)
- binding threonine: T265 (≠ K326), P266 (≠ A327), A269 (≠ S330), Q288 (= Q349), N362 (= N424), I363 (≠ V425)
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, 56% coverage: 3:457/817 of query aligns to 5:405/421 of P26512
- G277 (= G328) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ S330) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q349) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (= S352) 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 (≠ M410) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ S411) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R413) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ L414) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
28% identity, 56% coverage: 3:460/817 of query aligns to 5:403/405 of P61489
- K7 (= K5) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G7) mutation to M: Loss of aspartokinase activity.
- G10 (= G8) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S38) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A39) mutation to S: Loss of aspartokinase activity.
- T47 (= T44) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E124) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G187) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R202) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D206) 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 (= D226) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D234) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
Query Sequence
>CA265_RS23475 FitnessBrowser__Pedo557:CA265_RS23475
MKVLKFGGTSVGSAENIKTLLRLVGEEKQKNSPVVVLSAMSGVTNLLTEMAEMAERGEDY
DTHLKEIEAKHFAVIRSLLPAAAQNPVFTRLKIFFNELEDLLQAVANLRELSLQTKDQIL
SYGERCSTFMISHIASKNIGDSIYVNGSDLIKTDSNFGQAKVETELTEMLINNFYQENKD
KVLFVTGFIASNAAGRVTTLGRGGSDYTAAVWGAALNAEEIEIWTDVNGMMTADPRMVKK
AFSLPELSYTEAMELSYFGAKVIYPPTMIPAFMKKIPIVIKNTFEPDFAGTYIKSDVKAS
SLPIKGISSIDHISIINLTGSGMVGKAGFSGRLFSLLSREQINVVLITQSSSEHSITFAV
KPTDASQAISLIKKEFELELDAKKLELPEVENNLAVLAIVGENMKRTPGMSGRLFNALGR
NGINVRAIAQGSSEYNISVIISKDDLSKAVNAVHDAFFTDLKRTLNVFCLGTGNIGKTLF
NQLKEQMPFLAANNDLQVKVTGISNTRKMIFSADGLSLENWETELNTNGEPADLAGFVAK
MKALNLPNCVFVDNTAAESPIEFYQGIFESSISVVTCNKKGNSADYAQYKSFKDTARKFG
VDFYYETNVGAGLPIIRTLRELMMSGDKVARIEAILSGTISYIFNNFKGEAGFYETVKEA
QELGYTEPDPRDDLNGKDFMRKMLILARDAGYPLEASDVKIDNILPEACLNASSVEDFYS
ELQANAAYFENLKQTAANDGKVLRYIGKLEDGNVEISLQMVDDSHPFYMLSGSDNIISFT
TDRYKSRPLVVKGPGAGAEVTAAGVFADIINVGTLNK
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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