SitesBLAST
Comparing WP_010964316.1 NCBI__GCF_000008765.1:WP_010964316.1 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)
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)
43% identity, 95% coverage: 22:429/429 of query aligns to 22:434/435 of Q5F8J4
- L45 (≠ R45) mutation to R: Shows a marked increase in the catalytic efficiency with NADP(+).
- LS 45:46 (≠ RN 45:46) mutation to RD: Does not impair the catalytic activity with NAD(+). Slightly increases the activity, but slightly decreases the affinity for NADP(+).; mutation to 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(+).
6dzsA Mycobacterial homoserine dehydrogenase thra in complex with NADP
40% identity, 99% coverage: 4:427/429 of query aligns to 5:430/431 of 6dzsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G10), L12 (= L11), G13 (= G12), N14 (= N13), V15 (= V14), V45 (= V44), R46 (= R45), R47 (≠ N46), R52 (= R51), I63 (≠ P64), L78 (≠ V79), M79 (≠ I80), P84 (= P85), A102 (= A103), K104 (= K105), G306 (= G302), T310 (= T306)
4pg7A Crystal structure of s. Aureus homoserine dehydrogenase at ph7.5 (see paper)
45% identity, 82% coverage: 1:351/429 of query aligns to 2:335/402 of 4pg7A
Sites not aligning to the query:
6a0tB Homoserine dehydrogenase k99a mutant from thermus thermophilus hb8 complexed with hse and NADP+ (see paper)
35% identity, 75% coverage: 1:320/429 of query aligns to 1:308/332 of 6a0tB
- active site: D191 (= D201), K195 (= K205)
- binding l-homoserine: N150 (= N159), G151 (= G160), T152 (= T161), Y178 (≠ F188), E180 (= E190), D186 (= D196), K195 (= K205)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G10), G11 (≠ L11), G12 (= G12), T13 (≠ N13), V14 (= V14), L42 (= L43), V43 (= V44), R44 (= R45), D45 (≠ N46), K48 (= K49), R50 (= R51), A73 (≠ V79), M74 (≠ I80), G75 (= G81), A97 (= A103), N98 (= N104), G177 (= G187), E180 (= E190), A289 (= A301), G290 (= G302), T294 (= T306)
6a0sA Homoserine dehydrogenase from thermus thermophilus hb8 complexed with hse and NADPH (see paper)
35% identity, 75% coverage: 1:320/429 of query aligns to 1:308/331 of 6a0sA
- active site: D191 (= D201), K195 (= K205)
- binding l-homoserine: K99 (= K105), N150 (= N159), G151 (= G160), T152 (= T161), Y178 (≠ F188), E180 (= E190), D186 (= D196), K195 (= K205)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (≠ L11), G12 (= G12), T13 (≠ N13), V14 (= V14), L42 (= L43), V43 (= V44), R44 (= R45), D45 (≠ N46), K48 (= K49), R50 (= R51), A73 (≠ V79), M74 (≠ I80), A97 (= A103), K99 (= K105), G177 (= G187), E180 (= E190), A289 (= A301), G290 (= G302), T294 (= T306)
2ejwA Homoserine dehydrogenase from thermus thermophilus hb8
35% identity, 75% coverage: 1:320/429 of query aligns to 1:308/331 of 2ejwA
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)
31% identity, 74% coverage: 4:319/429 of query aligns to 1:301/304 of F9VNG5
- Y8 (≠ L11) binding NADP(+)
- N10 (= N13) binding NADP(+)
- V11 (= V14) binding NADP(+)
- R38 (≠ N50) binding NADP(+)
- R39 (= R51) binding NADP(+)
- S73 (≠ E71) binding NADP(+)
- T100 (≠ A103) binding NADP(+)
- K102 (= K105) binding NADP(+)
- G182 (= G187) binding NADP(+)
- E185 (= E190) binding NADP(+)
- G284 (= G302) binding NADP(+)
Sites not aligning to the query:
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)
31% identity, 74% coverage: 4:319/429 of query aligns to 1:297/300 of 7f4cA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F6 (≠ L9), G7 (= G10), Y8 (≠ L11), G9 (= G12), N10 (= N13), V11 (= V14), T37 (≠ K49), R38 (≠ N50), R39 (= R51), V72 (≠ D70), S73 (≠ E71), S74 (= S72), T100 (≠ A103), K102 (= K105), G127 (≠ A130), S131 (≠ G134), E185 (= E190), G280 (= G302), A284 (≠ T306)
5x9dA Crystal structure of homoserine dehydrogenase in complex with l- cysteine and NAD (see paper)
31% identity, 74% coverage: 4:319/429 of query aligns to 1:299/302 of 5x9dA
- active site: D196 (= D201), K200 (= K205)
- 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: F6 (≠ L9), G7 (= G10), Y8 (≠ L11), G9 (= G12), N10 (= N13), V11 (= V14), T37 (≠ K49), R38 (≠ N50), V72 (≠ D70), S73 (≠ E71), S74 (= S72), P82 (= P85), T100 (≠ A103), N101 (= N104), K102 (= K105), G127 (≠ A130), S131 (≠ G134), N155 (= N159), G156 (= G160), T157 (= T161), Y183 (≠ F188), A184 (= A189), E185 (= E190), D191 (= D196), D196 (= D201), K200 (= K205), A281 (= A301), G282 (= G302), A286 (≠ T306)
4xb2A Hyperthermophilic archaeal homoserine dehydrogenase mutant in complex with NADPH (see paper)
30% identity, 73% coverage: 3:315/429 of query aligns to 2:309/319 of 4xb2A
- active site: D211 (= D201), K215 (= K205)
- binding l-homoserine: A171 (≠ G160), S172 (≠ T161), D206 (= D196), K215 (= K205)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F8 (≠ L9), F10 (≠ L11), G11 (= G12), T12 (≠ N13), V13 (= V14), R40 (= R32), V91 (= V79), S92 (≠ G81), S93 (≠ G82), S114 (≠ A103), N115 (= N104), K116 (= K105), S141 (≠ A130), G295 (≠ A301), T300 (= T306)
4xb1A Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH (see paper)
30% identity, 73% coverage: 3:315/429 of query aligns to 2:309/319 of 4xb1A
- active site: D211 (= D201), K215 (= K205)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F8 (≠ L9), F10 (≠ L11), G11 (= G12), T12 (≠ N13), V13 (= V14), D39 (≠ K31), R40 (= R32), K57 (≠ V44), V91 (= V79), S92 (≠ G81), S93 (≠ G82), S114 (≠ A103), K116 (= K105), S141 (≠ A130), G295 (≠ A301), T300 (= T306)
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)
30% identity, 73% coverage: 3:315/429 of query aligns to 2:309/319 of O58802
- F10 (≠ L11) binding NADPH
- T12 (≠ N13) binding NADPH
- V13 (= V14) binding NADPH
- R40 (= R32) binding NADPH; mutation to A: Increases activity with NADP.
- K57 (≠ V44) binding NADPH; mutation to A: Increases activity with NADP.
- S92 (≠ G81) binding NADPH
- S93 (≠ G82) binding NADPH
- S114 (≠ A103) binding NADPH
- K116 (= K105) binding NADPH
- E140 (= E129) binding Na(+)
- V143 (= V132) binding Na(+)
- A145 (≠ G134) binding Na(+)
- T147 (≠ I136) binding Na(+)
- G296 (= G302) binding NADPH
3ingA Crystal structure of homoserine dehydrogenase (np_394635.1) from thermoplasma acidophilum at 1.95 a resolution
29% identity, 53% coverage: 3:228/429 of query aligns to 2:236/319 of 3ingA
- active site: D209 (= D201), K213 (= K205)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G10), T10 (≠ L11), G11 (= G12), N12 (= N13), V13 (= V14), D38 (vs. gap), S39 (vs. gap), K57 (≠ I47), C85 (≠ E78), T86 (≠ V79), P87 (≠ I80), A112 (= A103), N113 (= N104), K114 (= K105), A139 (= A130), E198 (= E190), S199 (≠ A191)
Sites not aligning to the query:
3jsaA Homoserine dehydrogenase from thermoplasma volcanium complexed with NAD
28% identity, 60% coverage: 1:259/429 of query aligns to 1:256/321 of 3jsaA
- active site: D212 (= D201), K216 (= K205)
- binding nicotinamide-adenine-dinucleotide: G10 (= G10), L11 (= L11), G12 (= G12), N13 (= N13), V14 (= V14), D42 (vs. gap), S43 (vs. gap), A90 (≠ I83), T91 (≠ N84), P92 (= P85), A117 (= A103), N118 (= N104), A144 (= A130)
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)
27% identity, 51% coverage: 99:317/429 of query aligns to 667:908/916 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.
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
28% identity, 29% coverage: 89:213/429 of query aligns to 100:230/358 of 1tveA
Sites not aligning to the query:
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
28% identity, 29% coverage: 89:213/429 of query aligns to 100:230/358 of 1q7gA
Sites not aligning to the query:
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
28% identity, 29% coverage: 89:213/429 of query aligns to 100:230/358 of 1ebuD
Sites not aligning to the query:
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
28% identity, 29% coverage: 89:213/429 of query aligns to 100:230/358 of 1ebfA
Sites not aligning to the query:
P31116 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
28% identity, 29% coverage: 89:213/429 of query aligns to 101:231/359 of P31116
- E143 (= E129) binding Na(+)
- V146 (= V132) binding Na(+)
- A148 (≠ G134) binding Na(+)
- L150 (≠ I136) binding Na(+)
- E208 (= E190) 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 (= D201) binding L-homoserine; mutation to L: Reduces kcat 150-fold.
- K223 (= K205) mutation to V: Loss of activity.
Sites not aligning to the query:
- 13 binding NAD(+)
- 15 binding NAD(+)
- 16 binding NAD(+)
- 41 binding NAD(+)
- 79 H→A: Reduces kcat 2-fold.
- 93 binding NAD(+)
- 309 H→A: Reduces kcat 40-fold. Affects dimer formation.
- 340 binding NAD(+)
Query Sequence
>WP_010964316.1 NCBI__GCF_000008765.1:WP_010964316.1
MDKIKIGILGLGNVGRGVLKILNTNKEEIQKRSGYDIEIGKILVRNIDKNRGIDVPRELL
TVDPDDILEDESIKIVIEVIGGINPAKDYILRAMKNKKHVVTANKMLLATEGDELFDTAE
EEGVMFYYEASVAGGIPIIHAINESLTANKIEQLIGIINGTTNYILTKMTLEKMNFHDAL
REAQEKGFAEADPTSDIEAYDAMYKLAILSSLSFGTKINVDDVYREGITKIEPIDIEFAR
EFGYVIKLVAIVKETETGLEMRVHPTMIPERHPLANVNDSFNAIFIKGNAVGDIMLYGRG
AGDLPTGSAVVADVISILRGNVDLSAISTVKKNYWNREINPMDKTRSEYYVRITVKDLPG
VLGEISMIFGEEGVSLLSVMQKGKREECVTVVYFTHSANEGMIKSAIDRIKSSKYTKSVD
NIIRIENIQ
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