SitesBLAST
Comparing WP_066329102.1 NCBI__GCF_900100165.1:WP_066329102.1 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)
38% identity, 100% coverage: 3:814/815 of query aligns to 91:910/916 of O81852
- I441 (= I348) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q350) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I429) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q431) 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: 3:461/815 of query aligns to 3:464/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T226), D230 (= D227), V231 (= V228), Y235 (≠ F232), T237 (≠ A234), D238 (≠ N235), P239 (= P236), R240 (≠ K237), K265 (= K262), V266 (= V263)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (= F189), R206 (= R203), G207 (= G204), S209 (= S206)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
41% identity, 56% coverage: 3:461/815 of query aligns to 3:468/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T226), D230 (= D227), Y235 (≠ F232), D238 (≠ N235), P239 (= P236), R240 (≠ K237), K265 (= K262), V266 (= V263)
- binding aspartic acid: T45 (= T44), E129 (= E125), F192 (= F189), R206 (= R203), G207 (= G204), S209 (= S206)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
41% identity, 56% coverage: 3:460/815 of query aligns to 3:458/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W225), T228 (= T226), D229 (= D227), A406 (≠ H408), I409 (≠ L411), A410 (≠ S412), N423 (= N425), I424 (= I426), Q429 (= Q431), E433 (= E435)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
31% identity, 56% coverage: 3:460/815 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E125), M327 (= M324), Q330 (≠ V327), F333 (≠ S330), L334 (≠ S331), S347 (≠ N344), V348 (= V345), D349 (≠ I346)
- binding s-adenosylmethionine: G345 (= G342), I346 (= I343), S347 (≠ N344), W368 (≠ F377), S369 (≠ E378), R370 (≠ I379), L372 (≠ I381), E376 (≠ K385)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 56% coverage: 3:460/815 of query aligns to 17:496/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
O94671 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 43% coverage: 466:812/815 of query aligns to 8:364/376 of O94671
- S201 (= S652) modified: Phosphoserine
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
31% identity, 56% coverage: 3:460/815 of query aligns to 4:447/447 of 2j0xA
- binding aspartic acid: F182 (= F189), G197 (= G204), G198 (= G205), S199 (= S206), D200 (= D207)
- binding lysine: M316 (= M324), S319 (≠ V327), F322 (≠ S330), L323 (≠ S331), S336 (≠ N344), V337 (= V345), D338 (≠ I346), S343 (= S353), E344 (= E354)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
31% identity, 56% coverage: 3:460/815 of query aligns to 4:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T226), D220 (= D227), I224 (≠ M231), Y225 (≠ F232), D228 (≠ N235), R230 (≠ K237), K255 (= K262), V256 (= V263)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E125), F182 (= F189), R196 (= R203), G197 (= G204), S199 (= S206)
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: 3:460/815 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 (= E125) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R203) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D207) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
P31116 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
35% identity, 43% coverage: 462:814/815 of query aligns to 2:357/359 of P31116
- A13 (≠ V473) binding NAD(+)
- V15 (≠ N475) binding NAD(+)
- V16 (= V476) binding NAD(+)
- A41 (≠ S507) binding NAD(+)
- H79 (≠ N545) mutation to A: Reduces kcat 2-fold.
- T93 (= T555) binding NAD(+)
- E143 (= E606) binding Na(+)
- V146 (= V609) binding Na(+)
- A148 (= A611) binding Na(+)
- L150 (= L613) binding Na(+)
- E208 (= E667) 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 (= D678) binding L-homoserine; mutation to L: Reduces kcat 150-fold.
- K223 (= K682) mutation to V: Loss of activity.
- H309 (= H765) mutation to A: Reduces kcat 40-fold. Affects dimer formation.
- G340 (= G797) binding NAD(+)
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
35% identity, 43% coverage: 462:814/815 of query aligns to 1:356/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
35% identity, 43% coverage: 462:814/815 of query aligns to 1:356/358 of 1q7gA
- active site: D218 (= D678), K222 (= K682)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G474), V14 (≠ N475), V15 (= V476), E39 (≠ N506), N91 (≠ I554), T92 (= T555), S93 (≠ A556), I97 (≠ V560), 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)
35% identity, 43% coverage: 462:814/815 of query aligns to 1:356/358 of 1ebuD
- active site: D218 (= D678), K222 (= K682)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G472), A12 (≠ V473), G13 (= G474), V14 (≠ N475), V15 (= V476), E39 (≠ N506), A40 (≠ S507), N91 (≠ I554), S93 (≠ A556), K116 (= K579), T343 (= T801)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
35% identity, 43% coverage: 462:814/815 of query aligns to 1:356/358 of 1ebfA
- active site: D218 (= D678), K222 (= K682)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ M471), A12 (≠ V473), G13 (= G474), V14 (≠ N475), V15 (= V476), E39 (≠ N506), A40 (≠ S507), T92 (= T555), S93 (≠ A556), P114 (≠ C577)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
29% identity, 56% coverage: 3:460/815 of query aligns to 5:438/439 of 3tviE
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 56% coverage: 3:458/815 of query aligns to 3:428/429 of 3tviA
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
29% identity, 49% coverage: 63:458/815 of query aligns to 19:393/397 of 5yeiC
- binding lysine: M342 (= M405), H345 (= H408), A346 (≠ Q409), G347 (= G410), V348 (≠ L411), A349 (≠ S412), S350 (≠ G413)
- binding threonine: T265 (≠ M324), P266 (≠ I325), A269 (≠ S331), Q288 (= Q350), N362 (= N425), I363 (= I426)
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
31% identity, 42% coverage: 115:458/815 of query aligns to 63:404/585 of 3l76A
- binding lysine: D286 (≠ N344), I287 (≠ V345), D288 (≠ I346), M353 (= M405), R356 (≠ H408), I359 (≠ L411), S380 (= S434), E381 (= E435)
- binding threonine: R269 (≠ M324), V272 (= V327), A273 (≠ S331), Q292 (= Q350), N373 (= N425), I374 (= I426)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
26% identity, 56% coverage: 3:458/815 of query aligns to 5:400/405 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 (= E84) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G188) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R203) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D207) 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 (= D227) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (≠ N235) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
Query Sequence
>WP_066329102.1 NCBI__GCF_900100165.1:WP_066329102.1
MRVLKFGGTSVANAKNIKLVLDIVLNKAKKDKLIVVVSALSKVTDLLQLAASKAAANDES
YKEIVAEIEKKHLDALKELIPVSEQSSLLSHIKRIINHLETILDGCFLLGELSARTSDTI
LSFGELLSSYIIAEALKQNLKNSSYKDSRELIKTNNNYGKAAVNFEVTNSLTTAFFANND
AQVVVMPGFIASSLDEINTTLGRGGSDYTAAILAGALNADELEIWTDVNGMFTANPKIVK
QAQPIATISYQEAMELSHFGAKVLYPPTIQPVLRKNIPIHIKNTFEPEAEGTYISNVSVS
NGIPVRGISHIDNITLITLEGPGMIGVSGSSKRLFEVLSNEGINVIFITQASSEHSICIG
ILNSDAEVAENAINKAFEIEIAQNKIDPCIVEQNLCIIALVGENMKNHQGLSGRMFSTLG
KNNVNIRAIAQGASERNISAVINERDVKKALNTLHENFFEENTKQLNLFVMGVGNVGEKF
IEQIHQQKKFLKENLKINVRVIALSNSRKMLFDEDAIDLNSWQAALENGETANKELFIEK
VAALNLRNSIFVDITANADVAAIYERFLKQSVGVVTCNKIACASAYDNYKNLKKLSRQYN
APFLFETNVGAGLPIIDTVKNLIASGDKVHKIQAVLSGSLNFIFNNFDENNSFHDVVKEA
GVQGFTEPDPKIDLSGIDVARKILILIRESGYKMEIENIENNSFLPAACMATTNNEDFFK
SLIEYNSHFEGILAEAKAKDSRLKFVAEFINGKANVGLQFIPKDHPFYNLEGKDNIVLFY
TDRYVDQPLLIKGAGAGAAVTASGIFADVIRIGNV
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