SitesBLAST
Comparing GFF1376 FitnessBrowser__Marino:GFF1376 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
37% identity, 99% coverage: 2:289/290 of query aligns to 1:287/287 of 3pefA
- binding glycerol: D67 (≠ S69), G123 (= G125), K171 (= K173), N175 (= N177), M178 (≠ L180), L203 (≠ M205), G207 (≠ P209), N213 (≠ P215), A217 (≠ G219), F232 (= F234), H236 (≠ L238), K239 (= K241), R242 (≠ H244), R269 (≠ S271)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G11), I11 (= I12), M12 (= M13), N31 (= N33), R32 (= R34), S33 (= S35), K36 (≠ A38), M64 (= M66), L65 (= L67), A66 (= A68), A70 (≠ V72), E73 (≠ D75), T96 (= T98), V121 (= V123), G123 (= G125), S124 (≠ T126), A231 (≠ Q233), F232 (= F234), H236 (≠ L238), K239 (= K241)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
35% identity, 98% coverage: 4:287/290 of query aligns to 3:285/287 of 3pduA
- binding glycerol: R242 (≠ H244), E246 (≠ Q248), E246 (≠ Q248), R250 (≠ E252)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G10 (= G11), I11 (= I12), M12 (= M13), N31 (= N33), R32 (= R34), N33 (≠ S35), M64 (= M66), L65 (= L67), A66 (= A68), A70 (≠ V72), T96 (= T98), V121 (= V123), G123 (= G125), T124 (= T126), K171 (= K173), S231 (≠ Q233), F232 (= F234), P233 (= P235), H236 (≠ L238), K239 (= K241)
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
34% identity, 99% coverage: 5:290/290 of query aligns to 3:294/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), N10 (≠ I12), M11 (= M13), Y29 (≠ F32), D30 (≠ N33), V31 (≠ R34), M63 (= M66), L64 (= L67), P65 (≠ A68), T95 (= T98), V120 (= V123), G122 (= G125), F238 (= F234), K245 (= K241)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
34% identity, 99% coverage: 5:290/290 of query aligns to 42:333/336 of P31937
- LP 103:104 (≠ LA 67:68) binding
- N108 (≠ V72) binding
- T134 (= T98) binding
- K284 (= K241) 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)
33% identity, 98% coverage: 5:287/290 of query aligns to 41:329/335 of P29266
- D68 (≠ N33) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K173) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N177) mutation to Q: Decrease in activity.
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)
33% identity, 97% coverage: 5:285/290 of query aligns to 4:284/298 of P0A9V8
- QM 11:12 (≠ IM 12:13) binding
- D31 (≠ N33) binding
- L65 (= L67) binding
- T96 (= T98) binding
- G122 (≠ A124) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G125) 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 (= T126) 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 (≠ VNAML 176:180) binding
- K240 (= K241) binding
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
33% identity, 97% coverage: 5:285/290 of query aligns to 3:283/294 of 6smyA
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
33% identity, 97% coverage: 5:285/290 of query aligns to 3:283/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), Q10 (≠ I12), M11 (= M13), F29 (= F32), D30 (≠ N33), V31 (≠ R34), M63 (= M66), L64 (= L67), V73 (≠ M76), S94 (= S97), T95 (= T98), R122 (≠ G125)
Q8T079 Cytokine-like nuclear factor N-PAC; NPAC; Glyoxylate reductase 1 homolog; Nuclear protein NP60 homolog; Nucleosome-destabilizing factor; Putative oxidoreductase GLYR1 homolog from Drosophila melanogaster (Fruit fly) (see paper)
28% identity, 97% coverage: 3:284/290 of query aligns to 316:597/602 of Q8T079
Sites not aligning to the query:
- 8 modified: Phosphoserine
- 10 modified: Phosphoserine
- 224 modified: Phosphoserine
- 228 modified: Phosphoserine
- 243 modified: Phosphoserine
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)
34% identity, 94% coverage: 5:276/290 of query aligns to 16:283/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G9), L21 (= L10), G22 (= G11), I23 (= I12), M24 (= M13), N43 (= N33), R44 (= R34), T45 (≠ S35), K48 (≠ A38), M76 (= M66), V77 (≠ L67), S78 (≠ A68), D82 (≠ V72), Q85 (≠ D75), V133 (= V123), F241 (= F234), K242 (≠ P235), H245 (≠ L238), K248 (= K241)
- binding sulfate ion: T134 (≠ A124), G135 (= G125), K183 (= K173)
2uyyA Structure of the cytokine-like nuclear factor n-pac
29% identity, 98% coverage: 3:285/290 of query aligns to 7:288/292 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 (= G11), L16 (≠ I12), M17 (= M13), N36 (= N33), R37 (= R34), T38 (≠ S35), V70 (≠ L67), S71 (≠ A68), A75 (≠ V72), T101 (= T98), F237 (= F234), Y238 (≠ P235), Y241 (≠ L238), K244 (= K241)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
33% identity, 94% coverage: 5:276/290 of query aligns to 16:286/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G9), L21 (= L10), G22 (= G11), I23 (= I12), M24 (= M13), N43 (= N33), R44 (= R34), T45 (≠ S35), K48 (≠ A38), V77 (≠ L67), S78 (≠ A68), D82 (≠ V72), Q85 (≠ D75), V133 (= V123), F244 (= F234), K245 (≠ P235), H248 (≠ L238), K251 (= K241)
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, 98% coverage: 3:285/290 of query aligns to 268:549/553 of Q49A26
- 271:285 (vs. 6:20, 53% identical) binding
- T362 (= T98) binding
- M437 (≠ K173) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (≠ A232) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K241) 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.
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, 98% coverage: 3:285/290 of query aligns to 267:542/546 of Q922P9
- P489 (≠ A232) 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.
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, 99% coverage: 3:288/290 of query aligns to 2:293/298 of Q9I5I6
- 2:31 (vs. 3:33, 55% identical) binding
- P66 (≠ A68) binding
- T96 (= T98) binding ; mutation to A: Almost abolished activity.
- S122 (≠ A124) mutation to A: Strongly reduced activity.
- K171 (= K173) active site
- N175 (= N177) mutation to A: Strongly reduced activity.
- W214 (vs. gap) mutation to A: Almost abolished activity.
- Y219 (≠ T214) mutation to A: Strongly reduced activity.
- K246 (= K241) binding ; mutation to A: Almost abolished activity.
- D247 (= D242) mutation to A: Almost abolished activity.
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 98% coverage: 4:287/290 of query aligns to 3:288/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ E134), E149 (≠ Q154), A152 (≠ G157), G153 (≠ K158), G153 (≠ K158), K154 (= K159)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (≠ A124), G120 (= G125), W211 (vs. gap), F236 (= F234)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G10 (= G11), N11 (≠ I12), M12 (= M13), F30 (= F32), D31 (≠ N33), P32 (≠ R34), M64 (= M66), L65 (= L67), T93 (= T98), G121 (≠ T126), K168 (= K173), L240 (= L238), K243 (= K241)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
33% identity, 98% coverage: 4:287/290 of query aligns to 3:288/290 of 5y8kA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 98% coverage: 4:287/290 of query aligns to 2:287/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
33% identity, 98% coverage: 4:287/290 of query aligns to 2:287/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ E150), E148 (≠ Q154), A151 (≠ G157), K153 (= K159)
- binding nicotinamide-adenine-dinucleotide: G7 (= G9), G9 (= G11), N10 (≠ I12), M11 (= M13), F29 (= F32), D30 (≠ N33), P31 (≠ R34), M63 (= M66), L64 (= L67), G120 (≠ T126), L239 (= L238), K242 (= K241)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
28% identity, 98% coverage: 3:285/290 of query aligns to 4:287/294 of 5je8B
Query Sequence
>GFF1376 FitnessBrowser__Marino:GFF1376
MTQTLAFIGLGIMGSRMAANLLDKGDVNLIVFNRSTEAEKSLKDKGAKVADSAADAVRQA
DVVFSMLASPPVVQDMALGEDGFVSAMAENALWVDCSTVNPSFTEYAGEVARAQGIRFMD
APVAGTREPAASGELTFLVGADDEDFQSVEPLLQTMGKKIVHVGQVGRGTAFKMLVNAML
AQSMLAFAETTLLGEKLGFSRDFLMDTLPNLPVTPPFIGGKAELIRNGDFDAQFPLELMH
KDLHLLEQTAYEVGQPLYLANLAKEVYGSASSSGWGRKDFASVFEFLNRH
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