SitesBLAST
Comparing PP_1143 FitnessBrowser__Putida:PP_1143 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)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
37% identity, 90% coverage: 8:272/295 of query aligns to 16:278/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G12), L21 (≠ I13), G22 (= G14), I23 (≠ L15), M24 (= M16), N43 (= N35), R44 (= R36), T45 (≠ S37), K48 (= K40), V77 (≠ L69), S78 (≠ A70), D82 (≠ V74), Q85 (≠ E77), V133 (= V126), F244 (≠ W238), K245 (≠ H239), H248 (≠ T242), K251 (= K245)
3ws7A The 1.18 a resolution structure of l-serine 3-dehydrogenase complexed with NADP+ and sulfate ion from the hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
37% identity, 90% coverage: 8:272/295 of query aligns to 16:275/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G12), L21 (≠ I13), G22 (= G14), I23 (≠ L15), M24 (= M16), N43 (= N35), R44 (= R36), T45 (≠ S37), K48 (= K40), M76 (≠ C68), V77 (≠ L69), S78 (≠ A70), D82 (≠ V74), Q85 (≠ E77), V133 (= V126), F241 (≠ W238), K242 (≠ H239), H245 (≠ T242), K248 (= K245)
- binding sulfate ion: T134 (≠ S127), G135 (= G128), K183 (= K176)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
33% identity, 100% coverage: 1:294/295 of query aligns to 35:332/335 of P29266
- D68 (≠ N35) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K176) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q180) mutation to Q: Decrease in activity.
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
38% identity, 89% coverage: 5:267/295 of query aligns to 1:259/287 of 3pduA
- binding glycerol: R242 (≠ D248), E246 (≠ K252), E246 (≠ K252), R250 (≠ E256)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), G10 (= G14), I11 (≠ L15), M12 (= M16), N31 (= N35), R32 (= R36), N33 (≠ S37), M64 (≠ C68), L65 (= L69), A66 (= A70), A70 (≠ V74), T96 (≠ S100), V121 (= V126), G123 (= G128), T124 (≠ G129), K171 (= K176), S231 (≠ K237), F232 (≠ W238), P233 (≠ H239), H236 (≠ T242), K239 (= K245)
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
32% identity, 97% coverage: 8:294/295 of query aligns to 3:294/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), N10 (≠ L15), M11 (= M16), Y29 (≠ W34), D30 (≠ N35), V31 (≠ R36), M63 (≠ C68), L64 (= L69), P65 (≠ A70), T95 (≠ S100), V120 (= V126), G122 (= G128), F238 (vs. gap), K245 (= K245)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
32% identity, 97% coverage: 8:294/295 of query aligns to 42:333/336 of P31937
- LP 103:104 (≠ LA 69:70) binding
- N108 (≠ V74) binding
- T134 (≠ S100) binding
- K284 (= K245) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
30% identity, 97% coverage: 7:292/295 of query aligns to 3:286/287 of 3pefA
- binding glycerol: D67 (= D71), G123 (= G128), K171 (= K176), N175 (≠ Q180), M178 (≠ V183), L203 (≠ A208), G207 (≠ A212), N213 (≠ K219), A217 (≠ I223), F232 (≠ W238), H236 (≠ T242), K239 (= K245), R242 (≠ D248), R269 (≠ G275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G14), I11 (≠ L15), M12 (= M16), N31 (= N35), R32 (= R36), S33 (= S37), K36 (= K40), M64 (≠ C68), L65 (= L69), A66 (= A70), A70 (≠ V74), E73 (= E77), T96 (≠ S100), V121 (= V126), G123 (= G128), S124 (≠ G129), A231 (≠ K237), F232 (≠ W238), H236 (≠ T242), K239 (= K245)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
34% identity, 91% coverage: 5:273/295 of query aligns to 1:262/289 of 2cvzC
- active site: S117 (= S127), K165 (= K176), N168 (= N179), N169 (≠ Q180)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), L9 (≠ I13), G10 (= G14), A11 (≠ L15), M12 (= M16), N30 (= N35), R31 (= R36), T32 (≠ S37), C62 (= C68), L63 (= L69), P64 (≠ A70), E68 (≠ V74), E71 (= E77), S91 (= S100), V116 (= V126), F227 (≠ W238), K234 (= K245)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
34% identity, 91% coverage: 7:273/295 of query aligns to 2:261/288 of 1wp4A
- active site: S116 (= S127), K164 (= K176), N167 (= N179), N168 (≠ Q180)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G12), L8 (≠ I13), G9 (= G14), A10 (≠ L15), M11 (= M16), N29 (= N35), R30 (= R36), T31 (≠ S37), K34 (= K40), C61 (= C68), L62 (= L69), P63 (≠ A70), E67 (≠ V74), S90 (= S100), V115 (= V126), T225 (≠ K237), F226 (≠ W238), K233 (= K245)
- binding sulfate ion: S116 (= S127), G117 (= G128), G118 (= G129), K164 (= K176)
2uyyA Structure of the cytokine-like nuclear factor n-pac
29% identity, 90% coverage: 8:272/295 of query aligns to 9:271/292 of 2uyyA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: G15 (= G14), L16 (= L15), M17 (= M16), N36 (= N35), R37 (= R36), T38 (≠ S37), V70 (≠ L69), S71 (≠ A70), A75 (≠ V74), T101 (≠ S100), F237 (≠ W238), Y238 (≠ H239), Y241 (≠ T242), K244 (= K245)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
27% identity, 97% coverage: 5:289/295 of query aligns to 3:287/294 of 5je8B
Q49A26 Cytokine-like nuclear factor N-PAC; NPAC; 3-hydroxyisobutyrate dehydrogenase-like protein; Glyoxylate reductase 1 homolog; Nuclear protein NP60; Nuclear protein of 60 kDa; Nucleosome-destabilizing factor; hNDF; Putative oxidoreductase GLYR1 from Homo sapiens (Human) (see 3 papers)
29% identity, 90% coverage: 8:272/295 of query aligns to 270:532/553 of Q49A26
- 271:285 (vs. 9:23, 47% identical) binding
- T362 (≠ S100) binding
- M437 (≠ K176) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (= P235) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K245) binding
Sites not aligning to the query:
- 214 D→A: Slightly reduced stimulation of KDM1B demethylase activity, but normal KDM1B-binding.
- 214:217 Interaction with histone H3
- 216 H→A: Slightly reduced stimulation of KDM1B demethylase activity, but normal KDM1B-binding.
- 216:225 Interaction with KDM1B
- 217 Required to promote KDM1B demethylase activity toward histone H3K4me1 and H3K4me2; F→A: Abolished stimulation of KDM1B demethylase activity, reduced affinity for histone H3 of the dimer with KDM1B, but normal KDM1B-binding.
- 219 H→A: Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity; when associated with A-223.
- 220:222 FLL→AAA: Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity.
- 223 S→A: Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity; when associated with A-219.
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
34% identity, 90% coverage: 5:270/295 of query aligns to 1:268/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T137), E149 (≠ Q157), A152 (≠ G160), G153 (≠ Q161), G153 (≠ Q161), K154 (≠ R162)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S127), G120 (= G128), W211 (≠ K219), F236 (≠ W238)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G10 (= G14), N11 (≠ L15), M12 (= M16), F30 (≠ W34), D31 (≠ N35), P32 (≠ R36), M64 (≠ C68), L65 (= L69), T93 (≠ S100), G121 (= G129), K168 (= K176), L240 (≠ T242), K243 (= K245)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
34% identity, 90% coverage: 5:270/295 of query aligns to 1:268/290 of 5y8kA
P0A9V8 3-sulfolactaldehyde reductase; SLA reductase; 4-hydroxybutyrate dehydrogenase; Gamma-hydroxybutyrate dehydrogenase; GHBDH; Succinic semialdehyde reductase; SSA reductase; EC 1.1.1.373; EC 1.1.1.61 from Escherichia coli (strain K12)
28% identity, 98% coverage: 5:292/295 of query aligns to 1:287/298 of P0A9V8
- QM 11:12 (≠ LM 15:16) binding
- D31 (≠ N35) binding
- L65 (= L69) binding
- T96 (≠ S100) binding
- G122 (≠ S127) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G128) binding ; mutation to G: 130-fold decrease in catalytic efficiency with SLA as substrate. 3-fold decrease in catalytic efficiency with NADH as substrate.
- T124 (≠ G129) mutation to G: 230-fold decrease in catalytic efficiency with SLA as substrate. 12-fold decrease in catalytic efficiency with NADH as substrate.
- NNYMS 174:178 (≠ CNQMI 178:182) binding
- K240 (= K245) binding
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
28% identity, 97% coverage: 7:292/295 of query aligns to 2:286/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), Q10 (≠ L15), M11 (= M16), F29 (≠ W34), D30 (≠ N35), V31 (≠ R36), M63 (≠ C68), L64 (= L69), V73 (= V78), S94 (= S99), T95 (≠ S100), R122 (≠ G128)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
28% identity, 97% coverage: 7:292/295 of query aligns to 2:286/294 of 6smyA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
34% identity, 89% coverage: 7:270/295 of query aligns to 2:267/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
34% identity, 89% coverage: 7:270/295 of query aligns to 2:267/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (= R153), E148 (≠ Q157), A151 (≠ G160), K153 (≠ R162)
- binding nicotinamide-adenine-dinucleotide: G7 (= G12), G9 (= G14), N10 (≠ L15), M11 (= M16), F29 (≠ W34), D30 (≠ N35), P31 (≠ R36), M63 (≠ C68), L64 (= L69), G120 (= G129), L239 (≠ T242), K242 (= K245)
Q9I5I6 NAD-dependent L-serine dehydrogenase; L-serine 3-dehydrogenase (NAD(+)); EC 1.1.1.387 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
35% identity, 97% coverage: 5:291/295 of query aligns to 1:292/298 of Q9I5I6
- 2:31 (vs. 6:35, 47% identical) binding
- P66 (≠ A70) binding
- T96 (≠ S100) binding ; mutation to A: Almost abolished activity.
- S122 (= S127) mutation to A: Strongly reduced activity.
- K171 (= K176) active site
- N175 (≠ Q180) mutation to A: Strongly reduced activity.
- W214 (≠ K219) mutation to A: Almost abolished activity.
- Y219 (≠ L224) mutation to A: Strongly reduced activity.
- K246 (= K245) binding ; mutation to A: Almost abolished activity.
- D247 (= D246) mutation to A: Almost abolished activity.
Query Sequence
>PP_1143 FitnessBrowser__Putida:PP_1143
MSTALPSLGFAGIGLMGLPMCRRLLAAGYPLTVWNRSPDKCAALVAAGARLASSPAELCR
DSDMVLLCLADTAVVREVVFGEQGIAQGGRSGQLLIDFSSLEPTATREMAAELAALCGMA
WLDAPVSGGTPGAEAGTLAIMVGGEAADLQRARPVLQVLGQRVTHMGAVGAGQVTKACNQ
MIVACNALVIAEVVALAEQSGVDATLIAEALAGGFADSKPLQILAPQMAESRFEPIKWHV
RTLLKDLDGAVKFSREQGSATPLSGLAAQLMRLHGSQGYLQKDPATLVELYRNKV
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