SitesBLAST
Comparing WP_066549662.1 NCBI__GCF_001636925.1:WP_066549662.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4pg7A Crystal structure of s. Aureus homoserine dehydrogenase at ph7.5 (see paper)
27% identity, 51% coverage: 276:572/583 of query aligns to 2:306/402 of 4pg7A
Sites not aligning to the query:
F9VNG5 Homoserine dehydrogenase; HDH; HSD; StHSD; EC 1.1.1.3 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 3 papers)
29% identity, 41% coverage: 337:574/583 of query aligns to 65:301/304 of F9VNG5
- S73 (≠ L345) binding NADP(+)
- T100 (≠ A368) binding NADP(+)
- K102 (= K370) binding NADP(+)
- G182 (= G451) binding NADP(+)
- E185 (= E454) binding NADP(+)
- G284 (= G557) binding NADP(+)
Sites not aligning to the query:
- 8 binding NADP(+)
- 10 binding NADP(+)
- 11 binding NADP(+)
- 38 binding NADP(+)
- 39 binding NADP(+)
- 303 modified: Interchain
7f4cA The crystal structure of the immature holo-enzyme of homoserine dehydrogenase complexed with NADP and 1,4-butandiol from the hyperthermophilic archaeon sulfurisphaera tokodaii. (see paper)
29% identity, 41% coverage: 337:574/583 of query aligns to 65:297/300 of 7f4cA
Sites not aligning to the query:
6a0tB Homoserine dehydrogenase k99a mutant from thermus thermophilus hb8 complexed with hse and NADP+ (see paper)
34% identity, 34% coverage: 279:475/583 of query aligns to 4:201/332 of 6a0tB
- active site: D191 (= D465), K195 (= K469)
- binding l-homoserine: N150 (= N424), G151 (= G425), T152 (= T426), Y178 (≠ F452), E180 (= E454), D186 (= D460), K195 (= K469)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G285), G11 (≠ C286), G12 (= G287), T13 (≠ V288), V14 (= V289), L42 (= L309), V43 (= V310), R44 (= R311), D45 (≠ N312), K48 (= K315), R50 (= R317), A73 (= A344), M74 (≠ L345), G75 (≠ S346), A97 (= A368), N98 (= N369), G177 (= G451), E180 (= E454)
Sites not aligning to the query:
6a0sA Homoserine dehydrogenase from thermus thermophilus hb8 complexed with hse and NADPH (see paper)
34% identity, 34% coverage: 279:475/583 of query aligns to 4:201/331 of 6a0sA
- active site: D191 (= D465), K195 (= K469)
- binding l-homoserine: K99 (= K370), N150 (= N424), G151 (= G425), T152 (= T426), Y178 (≠ F452), E180 (= E454), D186 (= D460), K195 (= K469)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (≠ C286), G12 (= G287), T13 (≠ V288), V14 (= V289), L42 (= L309), V43 (= V310), R44 (= R311), D45 (≠ N312), K48 (= K315), R50 (= R317), A73 (= A344), M74 (≠ L345), A97 (= A368), K99 (= K370), G177 (= G451), E180 (= E454)
Sites not aligning to the query:
2ejwA Homoserine dehydrogenase from thermus thermophilus hb8
34% identity, 34% coverage: 279:475/583 of query aligns to 4:201/331 of 2ejwA
Q5F8J4 Homoserine dehydrogenase; HDH; HSD; NAD(+)-dependent homoserine dehydrogenase; NAD(+)-dependent HSD; NgHSD; EC 1.1.1.3 from Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) (see paper)
30% identity, 46% coverage: 314:581/583 of query aligns to 48:325/435 of Q5F8J4
Sites not aligning to the query:
- 45 L→R: Shows a marked increase in the catalytic efficiency with NADP(+).
- 45:46 LS→RD: Does not impair the catalytic activity with NAD(+). Slightly increases the activity, but slightly decreases the affinity for NADP(+).; LS→RR: Causes a shift in coenzyme preference from NAD(+) to NADP(+) by a factor of 974. Shows a slight decrease in the catalytic efficiency with NAD(+) and a 4.5-fold increase in catalytic efficiency with NADP(+).
5x9dA Crystal structure of homoserine dehydrogenase in complex with l- cysteine and NAD (see paper)
29% identity, 41% coverage: 337:574/583 of query aligns to 65:299/302 of 5x9dA
- active site: D196 (= D465), K200 (= K469)
- binding (2R)-3-[[(4S)-3-aminocarbonyl-1-[(2R,3R,4S,5R)-5-[[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]-4H-pyridin-4-yl]sulfanyl]-2-azanyl-propanoic acid: V72 (≠ A344), S73 (≠ L345), S74 (= S346), P82 (≠ A350), T100 (≠ A368), N101 (= N369), K102 (= K370), G127 (≠ A395), S131 (≠ G399), N155 (= N424), G156 (= G425), T157 (= T426), Y183 (≠ F452), A184 (= A453), E185 (= E454), D191 (= D460), D196 (= D465), K200 (= K469), A281 (= A556), G282 (= G557), A286 (≠ T561)
Sites not aligning to the query:
- binding (2R)-3-[[(4S)-3-aminocarbonyl-1-[(2R,3R,4S,5R)-5-[[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]-4H-pyridin-4-yl]sulfanyl]-2-azanyl-propanoic acid: 6, 7, 8, 9, 10, 11, 37, 38
4xb1A Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH (see paper)
29% identity, 27% coverage: 325:483/583 of query aligns to 71:229/319 of 4xb1A
Sites not aligning to the query:
O58802 Homoserine dehydrogenase; HDH; HSD; HseDH; EC 1.1.1.3 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
29% identity, 27% coverage: 325:483/583 of query aligns to 71:229/319 of O58802
- S92 (≠ L345) binding NADPH
- S93 (= S346) binding NADPH
- S114 (≠ A368) binding NADPH
- K116 (= K370) binding NADPH
- E140 (≠ S394) binding Na(+)
- V143 (= V397) binding Na(+)
- A145 (≠ G399) binding Na(+)
- T147 (≠ S401) binding Na(+)
Sites not aligning to the query:
- 10 binding NADPH
- 12 binding NADPH
- 13 binding NADPH
- 40 binding NADPH; R→A: Increases activity with NADP.
- 57 binding NADPH; K→A: Increases activity with NADP.
- 296 binding NADPH
4xb2A Hyperthermophilic archaeal homoserine dehydrogenase mutant in complex with NADPH (see paper)
29% identity, 27% coverage: 325:483/583 of query aligns to 71:229/319 of 4xb2A
- active site: D211 (= D465), K215 (= K469)
- binding l-homoserine: A171 (≠ G425), S172 (≠ T426), D206 (= D460), K215 (= K469)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V91 (≠ A344), S92 (≠ L345), S93 (= S346), S114 (≠ A368), N115 (= N369), K116 (= K370), S141 (≠ A395)
Sites not aligning to the query:
6dzsA Mycobacterial homoserine dehydrogenase thra in complex with NADP
34% identity, 38% coverage: 278:497/583 of query aligns to 4:233/431 of 6dzsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G285), L12 (≠ C286), G13 (= G287), N14 (≠ V288), V15 (= V289), V45 (= V310), R46 (= R311), R47 (≠ N312), R52 (= R317), I63 (≠ P330), L78 (≠ A344), M79 (≠ L345), P84 (≠ A350), A102 (= A368), K104 (= K370)
Sites not aligning to the query:
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
34% identity, 31% coverage: 29:209/583 of query aligns to 2:182/397 of 5yeiC
Sites not aligning to the query:
- binding lysine: 342, 345, 346, 347, 348, 349, 350
- binding threonine: 265, 266, 269, 288, 362, 363
3ingA Crystal structure of homoserine dehydrogenase (np_394635.1) from thermoplasma acidophilum at 1.95 a resolution
27% identity, 34% coverage: 279:479/583 of query aligns to 3:223/319 of 3ingA
- active site: D209 (= D465), K213 (= K469)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G285), T10 (≠ C286), G11 (= G287), N12 (≠ V288), V13 (= V289), D38 (vs. gap), S39 (≠ V310), K57 (vs. gap), C85 (vs. gap), T86 (vs. gap), P87 (vs. gap), A112 (= A368), N113 (= N369), K114 (= K370), A139 (= A395), E198 (= E454), S199 (≠ E455)
Sites not aligning to the query:
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
32% identity, 31% coverage: 29:210/583 of query aligns to 3:184/405 of P61489
- K7 (= K33) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G35) mutation to M: Loss of aspartokinase activity.
- G10 (≠ S36) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S67) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A68) mutation to S: Loss of aspartokinase activity.
- T47 (= T73) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E100) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G161) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R176) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D180) 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 (= D200) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D208) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
37% identity, 31% coverage: 29:209/583 of query aligns to 3:184/421 of P41398
Sites not aligning to the query:
- 345 D→G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
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)
37% identity, 31% coverage: 29:209/583 of query aligns to 3:184/421 of P26512
Sites not aligning to the query:
- 277 G→A: Change in the inhibitory profile upon addition of threonine.
- 279 A→V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- 298 Q→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- 301 S→F: Absence of inhibition upon addition of threonine and lysine or lysine alone.; S→Y: Feedback-resistant and enhanced expression of the asd gene.
- 360 V→A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- 361 T→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- 363 E→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- 364 F→A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
3jsaA Homoserine dehydrogenase from thermoplasma volcanium complexed with NAD
29% identity, 25% coverage: 335:481/583 of query aligns to 81:228/321 of 3jsaA
Sites not aligning to the query:
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)
32% identity, 22% coverage: 359:487/583 of query aligns to 662:794/916 of O81852
Sites not aligning to the query:
- 441 I→A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- 443 Q→A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- 522 I→A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- 524 Q→A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
33% identity, 31% coverage: 29:209/583 of query aligns to 2:173/585 of 3l76A
Sites not aligning to the query:
- binding lysine: 286, 287, 288, 353, 356, 359, 380, 381, 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 269, 272, 273, 292, 373, 374, 440, 443, 463, 542, 543
Query Sequence
>WP_066549662.1 NCBI__GCF_001636925.1:WP_066549662.1
MSAQLAVVEKSESLGPSSQPSPDLVGPEVVVLKFGSSILRSPAEAPLVASAVYGHVRAGR
KVVAVVSAFGGATDRLLGEARALGLAHSNDLLPGYVALGEEKSAALVAIACDRIGLDACA
LSVRELGIVAEGEPEHSRPCGLRPDHLKQALDRHEVVVVPGFGAVRPDGKVALLGRGGSD
LTAVFLAAELGLKKVRLVKDVDGLYDHDPNDKTAPALRYRRASWDVARKLGGALVQHDAI
DLGESRGVEIEVAALDRADGTVIGDRSAPPGPAPALPPLKVAVAGCGVVGGGVLGKLLND
PRYEVVGVLVRNPKKARDVDCPASLFTSNPADLWAKKPDVVLEALSEGEAGHAVIRAALE
AGCDVASANKQAVSRDPGGLQELAKANGRRMFWSASVGGGSPMIETVRAARAAGEVVGFE
AVLNGTVNFMLERLGDGAAFNEALADARAAGFAEEDPSSDLEGLDAAAKVRLLCHEAFGR
SPDGDVPRDHLTEATSAAGGVRQIGAAHLKDGVIRPSVSLNADHGDPLFSTLRGEGNALK
VYGADGRVWRCRGRGAGRWATTESIMADLAEIVRARRADAGLN
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