SitesBLAST
Comparing N515DRAFT_0577 FitnessBrowser__Dyella79:N515DRAFT_0577 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 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)
44% identity, 93% coverage: 27:380/382 of query aligns to 555:914/916 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.
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 93% coverage: 27:380/382 of query aligns to 5:370/376 of O94671
- S201 (≠ P214) modified: Phosphoserine
P31116 Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
37% identity, 92% coverage: 28:378/382 of query aligns to 4:359/359 of P31116
- 11:18 (vs. 35:42, 75% identical) binding
- T93 (≠ S118) binding
- K117 (= K142) binding
- E208 (= E229) binding ; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D240) mutation to L: Reduces kcat 150-fold.
- K223 (= K244) mutation to V: Loss of activity.
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
37% identity, 92% coverage: 28:378/382 of query aligns to 3:358/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
37% identity, 92% coverage: 28:378/382 of query aligns to 3:358/358 of 1q7gA
- active site: D218 (= D240), K222 (= K244)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G38), V14 (≠ R39), V15 (= V40), E39 (≠ A69), N91 (≠ C117), T92 (≠ S118), S93 (≠ A119), I97 (≠ V123), P114 (= P140), K116 (= K142), A143 (= A169), S173 (= S199), K222 (= K244), A338 (= A358), T343 (= T363)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
37% identity, 92% coverage: 28:378/382 of query aligns to 3:358/358 of 1ebuD
- active site: D218 (= D240), K222 (= K244)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G36), A12 (≠ P37), G13 (= G38), V14 (≠ R39), V15 (= V40), E39 (≠ A69), A40 (≠ S70), N91 (≠ C117), S93 (≠ A119), K116 (= K142), T343 (= T363)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
37% identity, 92% coverage: 28:378/382 of query aligns to 3:358/358 of 1ebfA
- active site: D218 (= D240), K222 (= K244)
- binding nicotinamide-adenine-dinucleotide: I10 (= I35), A12 (≠ P37), G13 (= G38), V14 (≠ R39), V15 (= V40), E39 (≠ A69), A40 (≠ S70), T92 (≠ S118), S93 (≠ A119), P114 (= P140)
4xb1A Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH (see paper)
25% identity, 90% coverage: 30:373/382 of query aligns to 3:310/319 of 4xb1A
- active site: D211 (= D240), K215 (= K244)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F8 (≠ I35), F10 (≠ P37), G11 (= G38), T12 (≠ R39), V13 (= V40), D39 (vs. gap), R40 (≠ A69), K57 (≠ N83), V91 (≠ C117), S92 (= S118), S93 (≠ A119), S114 (≠ P140), K116 (= K142), S141 (≠ A169), G295 (≠ A358), T300 (= T363)
4xb2A Hyperthermophilic archaeal homoserine dehydrogenase mutant in complex with NADPH (see paper)
25% identity, 90% coverage: 30:373/382 of query aligns to 3:310/319 of 4xb2A
- active site: D211 (= D240), K215 (= K244)
- binding l-homoserine: A171 (≠ G200), S172 (≠ T201), D206 (= D235), K215 (= K244)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F8 (≠ I35), F10 (≠ P37), G11 (= G38), T12 (≠ R39), V13 (= V40), R40 (≠ A69), V91 (≠ C117), S92 (= S118), S93 (≠ A119), S114 (≠ P140), N115 (= N141), K116 (= K142), S141 (≠ A169), G295 (≠ A358), T300 (= T363)
3ingA Crystal structure of homoserine dehydrogenase (np_394635.1) from thermoplasma acidophilum at 1.95 a resolution
30% identity, 60% coverage: 34:262/382 of query aligns to 7:232/319 of 3ingA
- active site: D209 (= D240), K213 (= K244)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G36), T10 (≠ P37), G11 (= G38), N12 (≠ R39), V13 (= V40), D38 (≠ A69), S39 (= S70), K57 (≠ R88), C85 (= C117), T86 (≠ S118), P87 (vs. gap), A112 (≠ P140), N113 (= N141), K114 (= K142), A139 (= A169), E198 (= E229), S199 (≠ P230)
Sites not aligning to the query:
6a0tB Homoserine dehydrogenase k99a mutant from thermus thermophilus hb8 complexed with hse and NADP+ (see paper)
33% identity, 53% coverage: 131:333/382 of query aligns to 88:268/332 of 6a0tB
- active site: D191 (= D240), K195 (= K244)
- binding l-homoserine: N150 (≠ S199), G151 (= G200), T152 (= T201), Y178 (= Y227), E180 (= E229), D186 (= D235), K195 (= K244)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A97 (≠ P140), N98 (= N141), G177 (= G226), E180 (= E229)
Sites not aligning to the query:
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 10, 11, 12, 13, 14, 42, 43, 44, 45, 48, 50, 73, 74, 75, 289, 290, 294
6a0sA Homoserine dehydrogenase from thermus thermophilus hb8 complexed with hse and NADPH (see paper)
33% identity, 53% coverage: 131:333/382 of query aligns to 88:268/331 of 6a0sA
- active site: D191 (= D240), K195 (= K244)
- binding l-homoserine: K99 (= K142), N150 (≠ S199), G151 (= G200), T152 (= T201), Y178 (= Y227), E180 (= E229), D186 (= D235), K195 (= K244)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: A97 (≠ P140), K99 (= K142), G177 (= G226), E180 (= E229)
Sites not aligning to the query:
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 11, 12, 13, 14, 42, 43, 44, 45, 48, 50, 73, 74, 289, 290, 294
2ejwA Homoserine dehydrogenase from thermus thermophilus hb8
33% identity, 53% coverage: 131:333/382 of query aligns to 88:268/331 of 2ejwA
Q5F8J4 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, 65% coverage: 131:380/382 of query aligns to 93:322/435 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(+).
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)
25% identity, 64% coverage: 127:372/382 of query aligns to 87:293/300 of 7f4cA
Sites not aligning to the query:
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 6, 7, 8, 9, 10, 11, 37, 38, 39, 72, 73, 74
5x9dA Crystal structure of homoserine dehydrogenase in complex with l- cysteine and NAD (see paper)
26% identity, 64% coverage: 127:372/382 of query aligns to 87:295/302 of 5x9dA
- active site: D196 (= D240), K200 (= K244)
- 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: T100 (≠ P140), N101 (= N141), K102 (= K142), G127 (≠ A169), S131 (≠ A173), N155 (≠ S199), G156 (= G200), T157 (= T201), Y183 (= Y227), A184 (≠ T228), E185 (= E229), D191 (= D235), D196 (= D240), K200 (= K244), A281 (= A358), G282 (= G359), A286 (≠ T363)
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, 72, 73, 74, 82
6dzsA Mycobacterial homoserine dehydrogenase thra in complex with NADP
31% identity, 65% coverage: 131:377/382 of query aligns to 93:324/431 of 6dzsA
Sites not aligning to the query:
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 11, 12, 13, 14, 15, 45, 46, 47, 52, 63, 78, 79, 84
3jsaA Homoserine dehydrogenase from thermoplasma volcanium complexed with NAD
32% identity, 37% coverage: 125:267/382 of query aligns to 102:240/321 of 3jsaA
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 10, 11, 12, 13, 14, 42, 43, 90, 91, 92, 308
4pg7A Crystal structure of s. Aureus homoserine dehydrogenase at ph7.5 (see paper)
21% identity, 92% coverage: 28:380/382 of query aligns to 3:312/402 of 4pg7A
Sites not aligning to the query:
Query Sequence
>N515DRAFT_0577 FitnessBrowser__Dyella79:N515DRAFT_0577
MNALAPQLEHPKHPVLVRALPTTTPRRRMLAVGLIGPGRVGSALLTQLRAAQTRLSESGL
ELKLCGVAASKRMWLDCDDPDLNRRCDRAQIWRPADLRQFARHVLGDDGRHALLIDCSAN
DEVAAHYAGWLAEGVHVVTPNKLAGSGPLERWQAIRAASHAGARFRYEATVCAGLPVVQT
LRDLLDTGDELLAVDGMFSGTLAWLCNRHDGGRPFSALVREAHALGYTEPDPRDDLSGLD
VARKLVILAREAGWALSLDDVDVQSLVPAELAALDADAFMARLDELDAPMAAQLAIARAE
GGVLRHVASLDRDGRASVKLAVLPASHPFAHTRLTDNVVQFTTRRYHDNPLLVQGPGAGP
EVTAAGVFGDLLRIAESLEARA
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