SitesBLAST
Comparing 6936718 FitnessBrowser__SB2B:6936718 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)
38% identity, 99% coverage: 3:815/821 of query aligns to 91:911/916 of O81852
- I441 (= I349) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q351) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I430) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q432) 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)
36% identity, 56% coverage: 3:461/821 of query aligns to 3:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T227), D230 (= D228), V231 (= V229), Y235 (= Y233), T237 (= T235), D238 (= D236), P239 (= P237), R240 (= R238), K265 (= K263), V266 (= V264)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (= F190), R206 (= R204), G207 (≠ N205), S209 (= S207)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
36% identity, 56% coverage: 3:461/821 of query aligns to 3:458/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W226), T228 (= T227), D229 (= D228), A406 (≠ H409), I409 (≠ V412), A410 (= A413), N423 (= N426), I424 (= I427), Q429 (= Q432), E433 (= E436)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
36% identity, 56% coverage: 3:461/821 of query aligns to 3:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T227), D230 (= D228), Y235 (= Y233), D238 (= D236), P239 (= P237), R240 (= R238), K265 (= K263), V266 (= V264)
- binding aspartic acid: T45 (= T44), E129 (= E127), F192 (= F190), R206 (= R204), G207 (≠ N205), S209 (= S207)
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 43% coverage: 466:817/821 of query aligns to 8:369/376 of O94671
- S201 (= S652) modified: Phosphoserine
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)
31% identity, 56% coverage: 3:461/821 of query aligns to 6:449/449 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 (= R204) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D208) 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)
31% identity, 56% coverage: 3:461/821 of query aligns to 4:447/447 of 2j0xA
- binding aspartic acid: F182 (= F190), G197 (≠ N205), G198 (= G206), S199 (= S207), D200 (= D208)
- binding lysine: M316 (= M325), S319 (≠ M328), F322 (≠ M331), L323 (≠ A332), S336 (= S345), V337 (= V346), D338 (≠ S347), S343 (= S352), E344 (≠ S353)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
31% identity, 56% coverage: 3:461/821 of query aligns to 4:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T227), D220 (= D228), I224 (≠ V232), Y225 (= Y233), D228 (= D236), R230 (= R238), K255 (= K263), V256 (= V264)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E127), F182 (= F190), R196 (= R204), G197 (≠ N205), S199 (= S207)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
31% identity, 56% coverage: 3:461/821 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E127), M327 (= M325), Q330 (≠ M328), F333 (≠ M331), L334 (≠ A332), S347 (= S345), V348 (= V346), D349 (≠ S347)
- binding s-adenosylmethionine: G345 (= G343), I346 (≠ V344), S347 (= S345), W368 (≠ Q371), S369 (= S372), R370 (≠ A373), L372 (≠ E375), E376 (= E379)
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
33% identity, 39% coverage: 464:787/821 of query aligns to 3:331/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
33% identity, 39% coverage: 464:787/821 of query aligns to 3:331/358 of 1q7gA
- active site: D218 (= D678), K222 (= K682)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G474), V14 (≠ N475), V15 (= V476), E39 (≠ N505), N91 (≠ C554), T92 (= T555), S93 (= S556), I97 (≠ V560), P114 (= P577), K116 (= K579), A143 (≠ T607), S173 (= S637), K222 (= K682)
Sites not aligning to the query:
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
33% identity, 39% coverage: 464:787/821 of query aligns to 3:331/358 of 1ebuD
- active site: D218 (= D678), K222 (= K682)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G472), A12 (= A473), G13 (= G474), V14 (≠ N475), V15 (= V476), E39 (≠ N505), A40 (≠ S506), N91 (≠ C554), S93 (= S556), K116 (= K579)
Sites not aligning to the query:
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
33% identity, 39% coverage: 464:787/821 of query aligns to 3:331/358 of 1ebfA
- active site: D218 (= D678), K222 (= K682)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ V471), A12 (= A473), G13 (= G474), V14 (≠ N475), V15 (= V476), E39 (≠ N505), A40 (≠ S506), T92 (= T555), S93 (= S556), P114 (= P577)
P31116 Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 39% coverage: 464:787/821 of query aligns to 4:332/359 of P31116
- 11:18 (vs. 471:478, 63% 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.
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
35% identity, 34% coverage: 179:459/821 of query aligns to 124:393/397 of 5yeiC
- binding lysine: M342 (= M406), H345 (= H409), A346 (≠ K410), G347 (= G411), V348 (= V412), A349 (= A413), S350 (≠ A414)
- binding threonine: T265 (≠ M328), P266 (≠ V329), A269 (= A332), Q288 (= Q351), N362 (= N426), I363 (= I427)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
29% identity, 56% coverage: 3:459/821 of query aligns to 5:436/439 of 3tviE
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 56% coverage: 3:461/821 of query aligns to 17:496/519 of O60163
- S326 (≠ L304) modified: Phosphoserine
- T328 (≠ V306) modified: Phosphothreonine
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 56% coverage: 3:459/821 of query aligns to 3:428/429 of 3tviA
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
33% identity, 34% coverage: 179:459/821 of query aligns to 125:400/405 of P61489
- G135 (= G189) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R204) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D208) 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 (= D228) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D236) 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.
- 74 E→A: Loss of aspartokinase activity.; E→Q: Loss of aspartokinase activity.
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)
28% identity, 56% coverage: 3:459/821 of query aligns to 5:405/421 of P26512
- G277 (= G330) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A332) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q351) 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 (= V412) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A413) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ K415) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (= F416) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
Query Sequence
>6936718 FitnessBrowser__SB2B:6936718
MKVMKFGGTSLANWQRFDMAAAIVAEAAKASQVAAVLSAPATVTNGLLDMVDVAVTGGDY
QAVLGRVVGVFEALFDDACQHQVPQCREHLFAALSAQKHAWQTRLEGVALLGECPDGVRA
EIVVAGERLSTELMVALMNAHWLSADKLDPRALFLAHGTPLESVVDIGVSKPRFKQLPLD
SKRVWVMPGFTAADDKGRTVTLGRNGSDYSAAVLAACLDASSCEIWTDVDGVYNTDPRVV
ADAKLLSQLSYQEAMELSYFGAKVLHPKTIAPIAQFHIPCYIKNSFNPEAPGTLVSNAVD
ETGLQVKAISSLDNQTMFDVSGPGMKGMVGMASRTLGAIARAGVSVSLITQSSCEYSISF
CVAGKDAAKVQSALEQEFELELKSELLEPLEMQSGLAIVSLIGDGMRTHKGVAAKFFSAL
AQASVNIRAIAQGSSERSISAVVEQRKVQNAIGACHQRFFDVQQYLDVFLVGAGNVGAGL
LAQVKNQAEALKEQHISIRVCGIANSRKMLLDERGIDLANWQGLLNDSETGCDLGAMLAW
AKEKQLLNPVLVDCTSSAAVADRYLEVMEAGMHVVTPNKKANTRDLGYYRALREAALRHR
RQFLYETNVGAGLPVIDNLKKLLCAGDKLHKFNGILSGSLSFIFGKLEEGMSLSEATSIA
RDKCFTEPDPRDDLSGMDVARKVLILAREVGMPLELEDVVVDSVLPASFDANGDVSTFMA
NLHKADTEIATMVENARSEGKVLRYVGQIDESGCRVSIQAVGPEAPLFSVKGGENALAFY
SRYYQPIPFVLRGYGAGTDVTAAGAFADLLRTLNWTREVSL
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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