SitesBLAST
Comparing WP_012504858.1 NCBI__GCF_000020625.1:WP_012504858.1 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)
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, 100% coverage: 1:818/819 of query aligns to 89:912/916 of O81852
- I441 (= I350) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q352) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (≠ V431) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q433) 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)
41% identity, 56% coverage: 2:461/819 of query aligns to 2:462/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T225), D230 (= D226), V231 (= V227), Y235 (≠ F231), T237 (≠ A233), D238 (= D234), P239 (= P235), R240 (≠ K236), K265 (= K261), V266 (= V262)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (≠ Y188), R206 (= R202), G207 (= G203), S209 (= S205)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
41% identity, 56% coverage: 2:461/819 of query aligns to 2:457/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W224), T228 (= T225), D229 (= D226), A406 (≠ H410), I409 (≠ V413), A410 (≠ S414), N423 (= N427), I424 (≠ V428), Q429 (= Q433), E433 (= E437)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
41% identity, 56% coverage: 2:461/819 of query aligns to 2:466/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T225), D230 (= D226), Y235 (≠ F231), D238 (= D234), P239 (= P235), R240 (≠ K236), K265 (= K261), V266 (= V262)
- binding aspartic acid: T45 (= T44), E129 (= E125), F192 (≠ Y188), R206 (= R202), G207 (= G203), S209 (= S205)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
33% identity, 56% coverage: 3:463/819 of query aligns to 6:461/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E125), M327 (= M326), Q330 (≠ V329), F333 (≠ I332), L334 (≠ A333), S347 (≠ N346), V348 (≠ I347), D349 (≠ I348)
- binding s-adenosylmethionine: G345 (≠ M344), I346 (= I345), S347 (≠ N346), W368 (≠ S369), S369 (≠ K370), R370 (≠ A371), L372 (≠ M373), E376 (≠ D377)
O94671 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 43% coverage: 463:816/819 of query aligns to 4:366/376 of O94671
- S201 (vs. gap) modified: Phosphoserine
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 56% coverage: 3:461/819 of query aligns to 17:495/519 of O60163
- S326 (= S303) modified: Phosphoserine
- T328 (≠ R305) modified: Phosphothreonine
P31116 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
33% identity, 44% coverage: 462:818/819 of query aligns to 1:359/359 of P31116
- A13 (≠ T474) binding NAD(+)
- V15 (≠ T476) binding NAD(+)
- V16 (≠ I477) binding NAD(+)
- A41 (= A506) binding NAD(+)
- H79 (≠ R542) mutation to A: Reduces kcat 2-fold.
- T93 (= T557) binding NAD(+)
- E143 (= E608) binding Na(+)
- V146 (= V611) binding Na(+)
- A148 (= A613) binding Na(+)
- L150 (= L615) binding Na(+)
- E208 (= E669) binding L-homoserine; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D680) binding L-homoserine; mutation to L: Reduces kcat 150-fold.
- K223 (= K684) mutation to V: Loss of activity.
- H309 (≠ N767) mutation to A: Reduces kcat 40-fold. Affects dimer formation.
- G340 (= G799) binding NAD(+)
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
33% identity, 43% coverage: 463:818/819 of query aligns to 1:358/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
33% identity, 43% coverage: 463:818/819 of query aligns to 1:358/358 of 1q7gA
- active site: D218 (= D680), K222 (= K684)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G475), V14 (≠ T476), V15 (≠ I477), E39 (≠ M505), N91 (≠ C556), T92 (= T557), S93 (≠ A558), I97 (≠ V562), P114 (≠ A579), K116 (= K581), A143 (≠ T609), S173 (= S639), K222 (= K684), A338 (= A798), T343 (= T803)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
33% identity, 43% coverage: 463:818/819 of query aligns to 1:358/358 of 1ebuD
- active site: D218 (= D680), K222 (= K684)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G473), A12 (≠ T474), G13 (= G475), V14 (≠ T476), V15 (≠ I477), E39 (≠ M505), A40 (= A506), N91 (≠ C556), S93 (≠ A558), K116 (= K581), T343 (= T803)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
33% identity, 43% coverage: 463:818/819 of query aligns to 1:358/358 of 1ebfA
- active site: D218 (= D680), K222 (= K684)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ A472), A12 (≠ T474), G13 (= G475), V14 (≠ T476), V15 (≠ I477), E39 (≠ M505), A40 (= A506), T92 (= T557), S93 (≠ A558), P114 (≠ A579)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
33% identity, 42% coverage: 119:464/819 of query aligns to 68:404/405 of P61489
- E74 (= E125) 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.
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.
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
30% identity, 56% coverage: 3:461/819 of query aligns to 4:446/447 of 2j0xA
- binding aspartic acid: F182 (≠ Y188), G197 (= G203), G198 (= G204), S199 (= S205), D200 (= D206)
- binding lysine: M316 (= M326), S319 (≠ V329), F322 (≠ I332), L323 (≠ A333), S336 (≠ N346), V337 (≠ I347), D338 (≠ I348), S343 (= S355), E344 (= E356)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
30% identity, 56% coverage: 3:461/819 of query aligns to 4:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T225), D220 (= D226), I224 (≠ F230), Y225 (≠ F231), D228 (= D234), R230 (≠ K236), K255 (= K261), V256 (= V262)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E125), F182 (≠ Y188), 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)
30% identity, 56% coverage: 3:461/819 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 (= E125) 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.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 56% coverage: 3:460/819 of query aligns to 5:436/439 of 3tviE
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 56% coverage: 3:460/819 of query aligns to 3:428/429 of 3tviA
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
30% identity, 42% coverage: 119:462/819 of query aligns to 67:395/397 of 5yeiC
- binding lysine: M342 (= M407), H345 (= H410), A346 (≠ P411), G347 (= G412), V348 (= V413), A349 (≠ S414), S350 (≠ A415)
- binding threonine: T265 (≠ V329), P266 (= P330), A269 (= A333), Q288 (= Q352), N362 (= N427), I363 (≠ V428)
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)
29% identity, 58% coverage: 3:475/819 of query aligns to 5:420/421 of P26512
- G277 (= G331) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A333) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q352) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ A353) 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 (= V413) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ S414) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ H416) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ L417) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
Query Sequence
>WP_012504858.1 NCBI__GCF_000020625.1:WP_012504858.1
MNVLKFGGTSIENGKRIRNVLNIIRDAMHDGPVIVVVSAIRKVTDLLLDAALTACRGGGD
YKEKLVDIERLHTALVEDLLTGEKAEDVQRYLCGVLSELGDVLHGVSLLRELSEKSSALI
MSFGERFSAYIISSYLSQEGVAASYVDARGMIVTDTSHGDARVDMEASALQIRERLNNAD
SIPVVTGYIGSAPDGTVTTLGRGGSDYTATIIGSVLGAGEIQIWTDVDGFFSADPKRVRD
AYALPFISYAEAMELSHAGAKVLHPYAVHPAMKAGIPITIRNSMNPGAPGTRIEKLSSEE
AVSARPVTGLSSISDIVLLNISGSGMVGVPGIASRLFSCLARHMINIIFISQASSEQSIS
LAINALQASKAQMALDDEFAVELGSRQIESLTVRQDISMIAVVGKSMSGHPGVSAHLFET
LGKNGINVIAVAQGANEMNISFVIDSHDEDKALNCVHESFFLSRRKVHVFIAGTGTISSS
LIGQIRDHHETLSVGKNLDIVVCGMANTRMMALNNEGIDLNDWQSALQPREGERTIGDYL
ARIRSRNLHNTIFVDCTASADVAAAYPELLRSNISVVTANKLGMAGSWDLYETINDALNS
SNAKFLYETNVGAGLPIINTLNDLRNSGDKILKIEGVLSGTLSYIFNELRKGGAFSRIVR
QARDAGFTEPDPREDLSGADFARKFLILGRELGFRINYEDIQCESLVPDHLMGQMPVEEF
LEKLACVDEEYDDMNRKAAAEGMTIAYAGEINGGKAKISVKMLPLSNPVAGLNGTENMVV
FTTDRYFDTPLVVKGPGAGGEVTAGGVFADILRIASYLV
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