SitesBLAST
Comparing 7023927 Shewana3_1139 bifunctional aspartokinase I/homeserine dehydrogenase I (RefSeq) 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)
36% identity, 99% coverage: 3:812/822 of query aligns to 91:907/916 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 (= I431) 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)
37% identity, 56% coverage: 3:462/822 of query aligns to 3:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T228), D230 (= D229), V231 (= V230), Y235 (= Y234), T237 (= T236), D238 (= D237), P239 (= P238), R240 (= R239), K265 (= K264), V266 (= V265)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (= F191), R206 (= R205), G207 (≠ N206), S209 (= S208)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
37% identity, 56% coverage: 3:462/822 of query aligns to 3:458/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W227), T228 (= T228), D229 (= D229), A406 (≠ H410), I409 (≠ V413), A410 (= A414), N423 (= N427), I424 (= I428), Q429 (= Q433), E433 (= E437)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
37% identity, 56% coverage: 3:462/822 of query aligns to 3:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T228), D230 (= D229), Y235 (= Y234), D238 (= D237), P239 (= P238), R240 (= R239), K265 (= K264), V266 (= V265)
- binding aspartic acid: T45 (= T44), E129 (= E128), F192 (= F191), R206 (= R205), G207 (≠ N206), S209 (= S208)
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 43% coverage: 467:818/822 of query aligns to 8:369/376 of O94671
- S201 (≠ T653) modified: Phosphoserine
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
32% identity, 56% coverage: 3:462/822 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E128), M327 (= M326), Q330 (≠ M329), F333 (≠ M332), L334 (≠ A333), S347 (= S346), V348 (= V347), D349 (≠ S348)
- binding s-adenosylmethionine: G345 (= G344), I346 (≠ V345), S347 (= S346), W368 (≠ K372), S369 (= S373), R370 (≠ A374), L372 (≠ E376), E376 (= E380)
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: 3:462/822 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 (= E128) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R205) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D209) 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)
30% identity, 56% coverage: 3:462/822 of query aligns to 4:447/447 of 2j0xA
- binding aspartic acid: F182 (= F191), G197 (≠ N206), G198 (= G207), S199 (= S208), D200 (= D209)
- binding lysine: M316 (= M326), S319 (≠ M329), F322 (≠ M332), L323 (≠ A333), S336 (= S346), V337 (= V347), D338 (≠ S348), S343 (= S353), E344 (≠ S354)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
30% identity, 56% coverage: 3:462/822 of query aligns to 4:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T228), D220 (= D229), I224 (≠ V233), Y225 (= Y234), D228 (= D237), R230 (= R239), K255 (= K264), V256 (= V265)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E128), F182 (= F191), R196 (= R205), G197 (≠ N206), S199 (= S208)
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
33% identity, 39% coverage: 465:788/822 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: 465:788/822 of query aligns to 3:331/358 of 1q7gA
- active site: D218 (= D679), K222 (= K683)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G475), V14 (≠ N476), V15 (= V477), E39 (≠ N506), N91 (≠ C555), T92 (= T556), S93 (= S557), I97 (≠ V561), P114 (= P578), K116 (= K580), A143 (≠ T608), S173 (= S638), K222 (= K683)
Sites not aligning to the query:
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
33% identity, 39% coverage: 465:788/822 of query aligns to 3:331/358 of 1ebuD
- active site: D218 (= D679), K222 (= K683)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G473), A12 (≠ C474), G13 (= G475), V14 (≠ N476), V15 (= V477), E39 (≠ N506), A40 (≠ S507), N91 (≠ C555), S93 (= S557), K116 (= K580)
Sites not aligning to the query:
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
33% identity, 39% coverage: 465:788/822 of query aligns to 3:331/358 of 1ebfA
- active site: D218 (= D679), K222 (= K683)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ V472), A12 (≠ C474), G13 (= G475), V14 (≠ N476), V15 (= V477), E39 (≠ N506), A40 (≠ S507), T92 (= T556), S93 (= S557), P114 (= P578)
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
32% identity, 41% coverage: 123:460/822 of query aligns to 68:393/397 of 5yeiC
- binding lysine: M342 (= M407), H345 (= H410), A346 (≠ K411), G347 (= G412), V348 (= V413), A349 (= A414), S350 (≠ A415)
- binding threonine: T265 (≠ M329), P266 (≠ V330), A269 (= A333), Q288 (= Q352), N362 (= N427), I363 (= I428)
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: 465:788/822 of query aligns to 4:332/359 of P31116
- 11:18 (vs. 472:479, 50% identical) binding
- T93 (= T556) binding
- K117 (= K580) binding
- E208 (= E668) binding ; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D679) mutation to L: Reduces kcat 150-fold.
- K223 (= K683) mutation to V: Loss of activity.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 56% coverage: 3:460/822 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)
27% identity, 56% coverage: 3:462/822 of query aligns to 17:496/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 56% coverage: 3:460/822 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)
32% identity, 41% coverage: 123:460/822 of query aligns to 69:400/405 of P61489
- E74 (= E128) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G190) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R205) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D209) 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 (= D229) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D237) 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.
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, 41% coverage: 123:460/822 of query aligns to 69:405/421 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 (= S353) 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 (≠ A414) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R416) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (= F417) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
Query Sequence
>7023927 Shewana3_1139 bifunctional aspartokinase I/homeserine dehydrogenase I (RefSeq)
MKVMKFGGTSLANWQRFSMAADIVAKAAKAEPVATVLSAPATVTNALLEMVDVAVKGEDY
SPVIQHVERVFTSLYQDAVSSGLSSSQSEVLFAGLSVQLARWQDRLRGITLLQECPDGVR
AEIVVAGERLSAALMEQVMLAKGITSAQLDPRELFLGRGRPLESVVDIAVSKPRFKNLAL
DEKRVWVMPGFTAADEDGKVVTLGRNGSDYSAAVLAACLDASSCEIWTDVDGVYNTDPRV
VTDAKLLSQLSYQEAMELSYFGAKVLHPKTIAPIAQFHIPCYIKNSFNPDAPGTLVSNQA
DESGLQVKAISNLDNQTMFDVSGPGMKGMVGMASRTLAAISRSGVSVSLITQSSCEYSIS
FCVATSDAAKVKSALEQEFELEIKSDLLEPIEMRHDLAIVSLIGDGMRTHKGVAARFFQA
LAQASVNIIAIAQGSSERSISTVIEQRKTKHAVAACHQGFFDVQQYLDVFLVGCGNVGAG
LLEQIKHQASVLKEQHISIRVCGIVNSSKMLLDSAGIDLNNWQNLLADSQQPSDLSALLA
WVKEQQLLNPVLVDCTSSDQVSNQYLEVMNAGMHVVTPNKKANTRDYAYYQALRQTALKQ
RRQFLYETNVGAGLPVIDNLKKLLFAGDKLHKFNGILSGSLSFIFGKLDEGMTLSEATKL
AREKCFTEPDPRDDLSGMDVARKVLILAREVGLKLELSDIVVDSVLPDDFDDSGDVESFM
ARLTEADAAIAARVAEAKAQGKVLRYVGQIEEGACYVRITEVDATDPLYSVKGGENALAF
YSRYYQPIPFVLRGYGAGTEVTAAGAFADVLRTLNWTREVSV
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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