SitesBLAST
Comparing WP_085772173.1 NCBI__GCF_002117405.1:WP_085772173.1 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)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
37% identity, 97% coverage: 4:285/291 of query aligns to 13:293/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (= L12), G22 (= G13), I23 (≠ V14), M24 (= M15), N43 (= N34), R44 (= R35), T45 (≠ S36), K48 (= K39), V77 (= V69), S78 (≠ G70), D82 (= D74), Q85 (≠ A77), V133 (≠ I125), F244 (= F236), K245 (≠ A237), H248 (≠ W240), K251 (= K243)
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, 97% coverage: 4:285/291 of query aligns to 13:290/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (= L12), G22 (= G13), I23 (≠ V14), M24 (= M15), N43 (= N34), R44 (= R35), T45 (≠ S36), K48 (= K39), M76 (≠ C68), V77 (= V69), S78 (≠ G70), D82 (= D74), Q85 (≠ A77), V133 (≠ I125), F241 (= F236), K242 (≠ A237), H245 (≠ W240), K248 (= K243)
- binding sulfate ion: T134 (≠ S126), G135 (= G127), K183 (= K175)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
31% identity, 97% coverage: 9:290/291 of query aligns to 6:286/287 of 3pduA
- binding glycerol: R242 (≠ A246), E246 (= E250), E246 (= E250), R250 (= R254)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), G10 (= G13), I11 (≠ V14), M12 (= M15), N31 (= N34), R32 (= R35), N33 (≠ S36), M64 (≠ C68), L65 (≠ V69), A66 (≠ G70), A70 (≠ D74), T96 (= T100), V121 (≠ I125), G123 (= G127), T124 (≠ G128), K171 (= K175), S231 (≠ G235), F232 (= F236), P233 (≠ A237), H236 (≠ W240), K239 (= K243)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
35% identity, 91% coverage: 6:269/291 of query aligns to 3:260/289 of 2cvzC
- active site: S117 (= S126), K165 (= K175), N168 (= N178), N169 (≠ Q179)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), L9 (= L12), G10 (= G13), A11 (≠ V14), M12 (= M15), N30 (= N34), R31 (= R35), T32 (≠ S36), C62 (= C68), L63 (≠ V69), P64 (≠ G70), E68 (≠ A77), E71 (≠ Q80), S91 (≠ T100), V116 (≠ I125), F227 (= F236), K234 (= K243)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
35% identity, 91% coverage: 6:269/291 of query aligns to 2:259/288 of 1wp4A
- active site: S116 (= S126), K164 (= K175), N167 (= N178), N168 (≠ Q179)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G11), L8 (= L12), G9 (= G13), A10 (≠ V14), M11 (= M15), N29 (= N34), R30 (= R35), T31 (≠ S36), K34 (= K39), C61 (= C68), L62 (≠ V69), P63 (≠ G70), E67 (≠ A77), S90 (≠ T100), V115 (≠ I125), T225 (≠ G235), F226 (= F236), K233 (= K243)
- binding sulfate ion: S116 (= S126), G117 (= G127), G118 (= G128), K164 (= K175)
8z9fA Crystal structure of glyoxylate reductase from acetobacter aceti in complex with nadh
31% identity, 98% coverage: 7:291/291 of query aligns to 11:289/293 of 8z9fA
- binding 1,4-dihydronicotinamide adenine dinucleotide: F16 (≠ L12), G17 (= G13), A18 (≠ V14), M19 (= M15), P39 (≠ R35), C67 (= C68), V68 (= V69), P69 (≠ G70), A73 (≠ D74), S77 (≠ V78), S99 (≠ T100), G126 (= G127), S127 (≠ G128), Q234 (≠ G235), F235 (= F236)
8z9gA Crystal structure of glyoxylate reductase from acetobacter aceti in complex with NADPH
31% identity, 98% coverage: 7:291/291 of query aligns to 10:288/291 of 8z9gA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F15 (≠ L12), G16 (= G13), A17 (≠ V14), M18 (= M15), T37 (≠ N34), P38 (≠ R35), S39 (= S36), C66 (= C68), V67 (= V69), P68 (≠ G70), A72 (≠ D74), S76 (≠ V78), S98 (≠ T100), S126 (≠ G128), K173 (≠ T174), Q233 (≠ G235), F234 (= F236), K241 (= K243)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
29% identity, 100% coverage: 1:291/291 of query aligns to 35:331/335 of P29266
- D68 (≠ N34) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K175) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q179) mutation to Q: Decrease in activity.
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
28% identity, 98% coverage: 7:291/291 of query aligns to 3:293/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), N10 (≠ V14), M11 (= M15), Y29 (≠ F33), D30 (≠ N34), V31 (≠ R35), M63 (≠ C68), L64 (≠ V69), P65 (≠ G70), T95 (= T100), V120 (≠ I125), G122 (= G127), F238 (= F236), K245 (= K243)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
28% identity, 98% coverage: 7:291/291 of query aligns to 42:332/336 of P31937
- LP 103:104 (≠ VG 69:70) binding NAD(+)
- N108 (≠ D74) binding NAD(+)
- T134 (= T100) binding NAD(+)
- K284 (= K243) binding NAD(+)
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding NAD(+)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
28% identity, 96% coverage: 7:285/291 of query aligns to 6:285/294 of 5je8B
2uyyA Structure of the cytokine-like nuclear factor n-pac
26% identity, 97% coverage: 7:288/291 of query aligns to 9:289/292 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 (= G13), L16 (≠ V14), M17 (= M15), N36 (= N34), R37 (= R35), T38 (≠ S36), V70 (= V69), S71 (≠ G70), A75 (≠ D74), T101 (= T100), F237 (= F236), Y238 (≠ A237), Y241 (≠ W240), K244 (= K243)
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)
26% identity, 97% coverage: 6:288/291 of query aligns to 269:550/553 of Q49A26
- 271:285 (vs. 8:22, 40% identical) binding NAD(+)
- T362 (= T100) binding NAD(+)
- M437 (≠ T174) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (≠ H234) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K243) binding NAD(+)
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.
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
28% identity, 97% coverage: 9:291/291 of query aligns to 6:287/287 of 3pefA
- binding glycerol: D67 (≠ N71), G123 (= G127), K171 (= K175), N175 (≠ Q179), M178 (≠ I182), L203 (≠ V207), G207 (≠ K211), N213 (≠ S217), A217 (≠ E221), F232 (= F236), H236 (≠ W240), K239 (= K243), R242 (≠ A246), R269 (≠ E273)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G13), I11 (≠ V14), M12 (= M15), N31 (= N34), R32 (= R35), S33 (= S36), K36 (= K39), M64 (≠ C68), L65 (≠ V69), A66 (≠ G70), A70 (≠ D74), E73 (≠ A77), T96 (= T100), V121 (≠ I125), G123 (= G127), S124 (≠ G128), A231 (≠ G235), F232 (= F236), H236 (≠ W240), K239 (= K243)
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)
29% identity, 98% coverage: 7:290/291 of query aligns to 4:287/298 of P0A9V8
- QM 11:12 (≠ VM 14:15) binding NAD(+)
- D31 (≠ N34) binding NAD(+)
- L65 (≠ V69) binding NAD(+)
- T96 (= T100) binding NAD(+)
- G122 (≠ S126) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G127) binding 2,3-dihydroxypropane-1-sulfonate; mutation to G: 130-fold decrease in catalytic efficiency with SLA as substrate. 3-fold decrease in catalytic efficiency with NADH as substrate.
- T124 (≠ G128) 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 (≠ NQ--- 178:179) binding 2,3-dihydroxypropane-1-sulfonate
- K240 (= K243) binding NAD(+)
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
29% identity, 98% coverage: 7:290/291 of query aligns to 3:286/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), Q10 (≠ V14), M11 (= M15), F29 (= F33), D30 (≠ N34), V31 (≠ R35), M63 (≠ C68), L64 (≠ V69), V73 (= V78), S94 (≠ T99), T95 (= T100), R122 (≠ G127)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
29% identity, 98% coverage: 7:290/291 of query aligns to 3:286/294 of 6smyA
Q922P9 Cytokine-like nuclear factor N-PAC; NPAC; Glyoxylate reductase 1 homolog; Nuclear protein NP60; Putative oxidoreductase GLYR1 from Mus musculus (Mouse) (see paper)
25% identity, 97% coverage: 6:288/291 of query aligns to 268:543/546 of Q922P9
- P489 (≠ H234) 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)
34% identity, 83% coverage: 7:247/291 of query aligns to 4:250/298 of Q9I5I6
- P66 (≠ G70) binding NAD(+)
- T96 (= T100) binding NAD(+); mutation to A: Almost abolished activity.
- S122 (= S126) mutation to A: Strongly reduced activity.
- K171 (= K175) active site
- N175 (≠ Q179) mutation to A: Strongly reduced activity.
- W214 (= W218) mutation to A: Almost abolished activity.
- Y219 (vs. gap) mutation to A: Strongly reduced activity.
- K246 (= K243) binding NAD(+); mutation to A: Almost abolished activity.
- D247 (= D244) mutation to A: Almost abolished activity.
Sites not aligning to the query:
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
34% identity, 83% coverage: 7:247/291 of query aligns to 3:248/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), H10 (≠ V14), M11 (= M15), F29 (= F33), D30 (≠ N34), L31 (≠ R35), M63 (≠ C68), L64 (≠ V69), P65 (≠ G70), T94 (= T100), V119 (≠ I125), G121 (= G127), F237 (= F236), K244 (= K243)
Query Sequence
>WP_085772173.1 NCBI__GCF_002117405.1:WP_085772173.1
MTQNCNVAFIGLGVMGYPMAGHLARAGHRLAVFNRSAAKAQRFASEFAARAAASPREAAE
GADFVFSCVGNDDDLRAVTQGDKGAFAGMGKGAIFTDHTTASAEVARELFTAAREQGLGF
LDAPISGGQAGAEKGQLTVMCGGDSHDFAKAQPVIAAYAKACRLMGPTGAGQLTKMVNQI
AIAGLIQSLSEALNFATRAGLDAAAVVDLIKNGAAQSWQMENRAATMLRGEFDHGFAVEW
MRKDLAICLEEARRNGAELPVAALVDQFYARVEQMGGARWDTSSLIAALRR
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