SitesBLAST
Comparing AZOBR_RS20875 FitnessBrowser__azobra:AZOBR_RS20875 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)
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)
33% identity, 91% coverage: 1:271/299 of query aligns to 14:284/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (= N30), R44 (= R31), T45 (≠ S32), K48 (= K33), M76 (= M60), V77 (≠ L61), S78 (= S62), D82 (≠ A66), Q85 (≠ E69), V133 (= V116), F241 (= F228), K242 (= K229), H245 (≠ L232), K248 (= K235)
- binding sulfate ion: T134 (≠ L117), G135 (= G118), K183 (= K167)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
33% identity, 91% coverage: 1:271/299 of query aligns to 14:287/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (= N30), R44 (= R31), T45 (≠ S32), K48 (= K33), V77 (≠ L61), S78 (= S62), D82 (≠ A66), Q85 (≠ E69), V133 (= V116), F244 (= F228), K245 (= K229), H248 (≠ L232), K251 (= K235)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
28% identity, 92% coverage: 2:275/299 of query aligns to 5:283/294 of 5je8B
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
32% identity, 92% coverage: 2:275/299 of query aligns to 3:279/287 of 3pefA
- binding glycerol: D67 (= D63), G123 (= G118), K171 (= K167), N175 (= N171), M178 (≠ I174), L203 (≠ F199), G207 (≠ L203), N213 (≠ G209), A217 (≠ E213), F232 (= F228), H236 (≠ L232), K239 (= K235), R242 (= R238), R269 (≠ V265)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (= N30), R32 (= R31), S33 (= S32), K36 (≠ T35), M64 (= M60), L65 (= L61), A66 (≠ S62), A70 (= A66), E73 (= E69), T96 (= T91), V121 (= V116), G123 (= G118), S124 (≠ R119), A231 (≠ G227), F232 (= F228), H236 (≠ L232), K239 (= K235)
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 84% coverage: 3:253/299 of query aligns to 3:260/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
33% identity, 84% coverage: 3:253/299 of query aligns to 3:260/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ E143), E148 (≠ A147), A151 (≠ S150), K153 (= K152)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), N10 (= N10), M11 (= M11), F29 (≠ W29), D30 (≠ N30), P31 (vs. gap), M63 (= M60), L64 (= L61), G120 (≠ R119), L239 (= L232), K242 (= K235)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 84% coverage: 3:253/299 of query aligns to 4:261/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ Q127), E149 (≠ A147), A152 (≠ S150), G153 (≠ K151), G153 (≠ K151), K154 (= K152)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (≠ L117), G120 (= G118), W211 (≠ Y212), F236 (= F228)
- binding nicotinamide-adenine-dinucleotide: G8 (= G7), G10 (= G9), N11 (= N10), M12 (= M11), F30 (≠ W29), D31 (≠ N30), P32 (vs. gap), M64 (= M60), L65 (= L61), T93 (= T91), G121 (≠ R119), K168 (= K167), L240 (= L232), K243 (= K235)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
33% identity, 84% coverage: 3:253/299 of query aligns to 4:261/290 of 5y8kA
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
31% identity, 91% coverage: 4:275/299 of query aligns to 5:279/287 of 3pduA
- binding glycerol: R242 (= R238), E246 (= E242), E246 (= E242), R250 (≠ E246)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (= N30), R32 (= R31), N33 (≠ S32), M64 (= M60), L65 (= L61), A66 (≠ S62), A70 (= A66), T96 (= T91), V121 (= V116), G123 (= G118), T124 (≠ R119), K171 (= K167), S231 (≠ G227), F232 (= F228), P233 (≠ K229), H236 (≠ L232), K239 (= K235)
2uyyA Structure of the cytokine-like nuclear factor n-pac
29% identity, 92% coverage: 2:275/299 of query aligns to 8:284/292 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 (= G9), L16 (≠ N10), M17 (= M11), N36 (= N30), R37 (= R31), T38 (≠ S32), V70 (≠ L61), S71 (= S62), A75 (= A66), T101 (= T91), F237 (= F228), Y238 (≠ K229), Y241 (≠ L232), K244 (= K235)
Q922P9 Cytokine-like nuclear factor N-PAC; NPAC; Glyoxylate reductase 1 homolog; Nuclear protein NP60; Putative oxidoreductase GLYR1 from Mus musculus (Mouse) (see paper)
29% identity, 92% coverage: 2:275/299 of query aligns to 268:538/546 of Q922P9
- P489 (= P226) mutation to L: Mutant animals are born at expected Mendelian ratios. 54% mutants display postnatal lethality between days 0 and 1. They show centricular septal defects.
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, 92% coverage: 2:275/299 of query aligns to 269:545/553 of Q49A26
- 271:285 (vs. 4:18, 60% identical) binding
- T362 (= T91) binding
- M437 (vs. gap) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (= P226) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K235) 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.
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
30% identity, 92% coverage: 1:275/299 of query aligns to 1:285/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), N10 (= N10), M11 (= M11), Y29 (≠ W29), D30 (≠ N30), V31 (vs. gap), M63 (= M60), L64 (= L61), P65 (≠ S62), T95 (= T91), V120 (= V116), G122 (= G118), F238 (= F228), K245 (= K235)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
29% identity, 91% coverage: 3:275/299 of query aligns to 42:324/336 of P31937
- LP 103:104 (≠ LS 61:62) binding
- N108 (≠ A66) binding
- T134 (= T91) binding
- K284 (= K235) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
28% identity, 91% coverage: 3:275/299 of query aligns to 41:323/335 of P29266
- D68 (= D37) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K167) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N171) mutation to Q: Decrease in activity.
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
30% identity, 91% coverage: 3:275/299 of query aligns to 3:279/294 of 6smyA
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)
30% identity, 91% coverage: 3:275/299 of query aligns to 4:280/298 of P0A9V8
- QM 11:12 (≠ NM 10:11) binding
- D31 (≠ N30) binding
- L65 (= L61) binding
- T96 (= T91) binding
- G122 (= G118) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (= R119) 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 (≠ P120) mutation to G: 230-fold decrease in catalytic efficiency with SLA as substrate. 12-fold decrease in catalytic efficiency with NADH as substrate.
- NNYM-S 174:178 (≠ CNMMIA 170:175) binding
- K240 (= K235) binding
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
30% identity, 91% coverage: 3:275/299 of query aligns to 3:279/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), Q10 (≠ N10), M11 (= M11), F29 (≠ W29), D30 (≠ N30), V31 (vs. gap), M63 (= M60), L64 (= L61), V73 (= V70), S94 (= S90), T95 (= T91), R122 (= R119)
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
29% identity, 92% coverage: 2:277/299 of query aligns to 2:286/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), H10 (≠ N10), M11 (= M11), F29 (≠ W29), D30 (≠ N30), L31 (≠ V34), M63 (= M60), L64 (= L61), P65 (≠ S62), T94 (= T91), V119 (= V116), G121 (= G118), F237 (= F228), K244 (= K235)
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)
29% identity, 92% coverage: 2:277/299 of query aligns to 3:288/298 of Q9I5I6
- P66 (≠ S62) binding
- T96 (= T91) binding ; mutation to A: Almost abolished activity.
- S122 (≠ L117) mutation to A: Strongly reduced activity.
- K171 (= K167) active site
- N175 (= N171) mutation to A: Strongly reduced activity.
- W214 (≠ R210) mutation to A: Almost abolished activity.
- Y219 (= Y215) mutation to A: Strongly reduced activity.
- K246 (= K235) binding ; mutation to A: Almost abolished activity.
- D247 (= D236) mutation to A: Almost abolished activity.
Sites not aligning to the query:
Query Sequence
>AZOBR_RS20875 FitnessBrowser__azobra:AZOBR_RS20875
MQIGFVGLGNMGSAMALNLVKAGHDVRAWNRSKVTQDSVPGVTLVRRAADAFQADAVFTM
LSDDPAIREVILDAGLLASARPGLTHVVTSTISVAFARELERLHEEAGLGYVSAPVLGRP
NAAASGQLNILAAGKADAVAAVEPLLASLSKKVWKLGENPARANTAKLACNMMIAMAIEA
MAEGVVLTESVGLDRADFFELILGTLFSGRAYESYSAQITERSFEPGFKAELALKDMRLA
TEASNEIGRTLPMLEAVREGLRKAVSAGFGNKDWSIMADMAVRGGDSLALSETKSEKKQ
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