SitesBLAST
Comparing WP_068461703.1 NCBI__GCF_001541235.1:WP_068461703.1 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)
Q5F8J4 NAD(+)-dependent homoserine dehydrogenase; NAD(+)-dependent HSD; NgHSD; EC 1.1.1.3 from Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) (see paper)
44% identity, 93% coverage: 33:442/443 of query aligns to 33:433/435 of Q5F8J4
- L45 (≠ R45) mutation to R: Shows a marked increase in the catalytic efficiency with NADP(+).
- LS 45:46 (≠ RS 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: 3:440/443 of query aligns to 3:429/431 of 6dzsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G11), L12 (= L12), G13 (= G13), N14 (≠ T14), V15 (= V15), V45 (≠ A44), R46 (= R45), R47 (≠ S46), R52 (= R51), I63 (= I66), L78 (= L80), M79 (≠ I81), P84 (≠ G86), A102 (= A105), K104 (= K107), G306 (= G304), T310 (= T308)
4pg7A Crystal structure of s. Aureus homoserine dehydrogenase at ph7.5 (see paper)
36% identity, 73% coverage: 3:327/443 of query aligns to 3:316/402 of 4pg7A
Sites not aligning to the query:
6a0tB Homoserine dehydrogenase k99a mutant from thermus thermophilus hb8 complexed with hse and NADP+ (see paper)
36% identity, 63% coverage: 3:281/443 of query aligns to 2:269/332 of 6a0tB
- active site: D191 (= D203), K195 (= K207)
- binding l-homoserine: N150 (= N161), G151 (= G162), T152 (= T163), Y178 (= Y190), E180 (= E192), D186 (= D198), K195 (= K207)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G11), G11 (≠ L12), G12 (= G13), T13 (= T14), V14 (= V15), L42 (≠ S43), V43 (≠ A44), R44 (= R45), D45 (≠ S46), K48 (= K49), R50 (= R51), A73 (≠ L80), M74 (≠ I81), G75 (= G82), A97 (= A105), N98 (= N106), G177 (= G189), E180 (= E192)
Sites not aligning to the query:
6a0sA Homoserine dehydrogenase from thermus thermophilus hb8 complexed with hse and NADPH (see paper)
36% identity, 63% coverage: 3:281/443 of query aligns to 2:269/331 of 6a0sA
- active site: D191 (= D203), K195 (= K207)
- binding l-homoserine: K99 (= K107), N150 (= N161), G151 (= G162), T152 (= T163), Y178 (= Y190), E180 (= E192), D186 (= D198), K195 (= K207)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (≠ L12), G12 (= G13), T13 (= T14), V14 (= V15), L42 (≠ S43), V43 (≠ A44), R44 (= R45), D45 (≠ S46), K48 (= K49), R50 (= R51), A73 (≠ L80), M74 (≠ I81), A97 (= A105), K99 (= K107), G177 (= G189), E180 (= E192)
Sites not aligning to the query:
2ejwA Homoserine dehydrogenase from thermus thermophilus hb8
36% identity, 63% coverage: 3:281/443 of query aligns to 2:269/331 of 2ejwA
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)
33% identity, 72% coverage: 5:321/443 of query aligns to 1:297/300 of 7f4cA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F6 (≠ A10), G7 (= G11), Y8 (≠ L12), G9 (= G13), N10 (≠ T14), V11 (= V15), T37 (≠ S43), R38 (≠ A44), R39 (= R45), V72 (= V76), S73 (≠ F77), S74 (vs. gap), T100 (≠ A105), K102 (= K107), G127 (≠ A132), S131 (≠ G136), E185 (= E192), G280 (= G304), A284 (≠ T308)
4xb2A Hyperthermophilic archaeal homoserine dehydrogenase mutant in complex with NADPH (see paper)
28% identity, 71% coverage: 5:317/443 of query aligns to 3:309/319 of 4xb2A
- active site: D211 (= D203), K215 (= K207)
- binding l-homoserine: A171 (≠ G162), S172 (≠ T163), D206 (= D198), K215 (= K207)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F8 (≠ A10), F10 (≠ L12), G11 (= G13), T12 (= T14), V13 (= V15), R40 (= R45), V91 (≠ L80), S92 (≠ I81), S93 (≠ G82), S114 (≠ A105), N115 (= N106), K116 (= K107), S141 (≠ A132), G295 (≠ A303), T300 (= T308)
4xb1A Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH (see paper)
28% identity, 71% coverage: 5:317/443 of query aligns to 3:309/319 of 4xb1A
- active site: D211 (= D203), K215 (= K207)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F8 (≠ A10), F10 (≠ L12), G11 (= G13), T12 (= T14), V13 (= V15), D39 (≠ A44), R40 (= R45), K57 (≠ H50), V91 (≠ L80), S92 (≠ I81), S93 (≠ G82), S114 (≠ A105), K116 (= K107), S141 (≠ A132), G295 (≠ A303), T300 (= T308)
5x9dA Crystal structure of homoserine dehydrogenase in complex with l- cysteine and NAD (see paper)
33% identity, 72% coverage: 5:321/443 of query aligns to 1:299/302 of 5x9dA
- active site: D196 (= D203), K200 (= K207)
- 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 (≠ A10), G7 (= G11), Y8 (≠ L12), G9 (= G13), N10 (≠ T14), V11 (= V15), T37 (≠ S43), R38 (≠ A44), V72 (= V76), S73 (≠ F77), S74 (vs. gap), P82 (≠ D85), T100 (≠ A105), N101 (= N106), K102 (= K107), G127 (≠ A132), S131 (≠ G136), N155 (= N161), G156 (= G162), T157 (= T163), Y183 (= Y190), A184 (= A191), E185 (= E192), D191 (= D198), D196 (= D203), K200 (= K207), A281 (= A303), G282 (= G304), A286 (≠ T308)
3ingA Crystal structure of homoserine dehydrogenase (np_394635.1) from thermoplasma acidophilum at 1.95 a resolution
29% identity, 52% coverage: 3:231/443 of query aligns to 1:237/319 of 3ingA
- active site: D209 (= D203), K213 (= K207)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G11), T10 (≠ L12), G11 (= G13), N12 (≠ T14), V13 (= V15), D38 (vs. gap), S39 (vs. gap), K57 (= K47), C85 (≠ L80), T86 (≠ I81), P87 (vs. gap), A112 (= A105), N113 (= N106), K114 (= K107), A139 (= A132), E198 (= E192), S199 (≠ A193)
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)
25% identity, 72% coverage: 4:320/443 of query aligns to 557:909/916 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.
3jsaA Homoserine dehydrogenase from thermoplasma volcanium complexed with NAD
28% identity, 51% coverage: 3:230/443 of query aligns to 2:239/321 of 3jsaA
- active site: D212 (= D203), K216 (= K207)
- binding nicotinamide-adenine-dinucleotide: G10 (= G11), L11 (= L12), G12 (= G13), N13 (≠ T14), V14 (= V15), D42 (≠ A44), S43 (≠ R45), A90 (≠ L80), T91 (≠ I81), P92 (vs. gap), A117 (= A105), N118 (= N106), A144 (= A132)
Sites not aligning to the query:
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 48% coverage: 4:215/443 of query aligns to 7:239/376 of O94671
- S201 (= S177) modified: Phosphoserine
P31116 Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 20% coverage: 131:220/443 of query aligns to 143:235/359 of P31116
- E208 (= E192) binding ; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D203) mutation to L: Reduces kcat 150-fold.
- K223 (= K207) mutation to V: Loss of activity.
Sites not aligning to the query:
- 11:18 binding
- 93 binding
- 117 binding
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
36% identity, 20% coverage: 131:220/443 of query aligns to 142:234/358 of 1tveA
Sites not aligning to the query:
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
36% identity, 20% coverage: 131:220/443 of query aligns to 142:234/358 of 1q7gA
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: 13, 14, 15, 39, 91, 92, 93, 97, 114, 116, 338, 343
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
36% identity, 20% coverage: 131:220/443 of query aligns to 142:234/358 of 1ebuD
Sites not aligning to the query:
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: 11, 12, 13, 14, 15, 39, 40, 91, 93, 116, 343
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
36% identity, 20% coverage: 131:220/443 of query aligns to 142:234/358 of 1ebfA
Sites not aligning to the query:
Query Sequence
>WP_068461703.1 NCBI__GCF_001541235.1:WP_068461703.1
MTKSLKLGVAGLGTVGTSLIELLATHRDRLANLGSTVDVVAVSARSKDKHRAIAETAGVT
WFDDPIALARDPAIDVFVELIGGEDGVAKEAVEAALNAGKHVVTANKALLAKHGVALAQL
AEEKGVALNFEAAVAGGIPVIKTLRESLAANSVRRVYGILNGTCNYILSTMTDEKRSFGD
ALKEAQDLGYAEADPTFDIGGFDTAHKLAILASLAFGTEINFDEIDVEGIQSITDADIEA
AEDMGYCIKLLGVATQTDSGIEMRVNPAMVPEESAIAEVWGATNGVAIDSDFCGSLLLVG
PGAGGKATASSVAGDIVDIARGIILPPLMRKAASLTPCVRSKLGSHQGAYYVRLSVYDRP
GTMAAIAKHMGDRDISIESMVQGQMRAGVPGAEARTKVRGAPAPVRIITHETTEEAIRQA
VEAIEQDGKVSERPQVIRIEKLG
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