SitesBLAST
Comparing GFF2806 FitnessBrowser__WCS417:GFF2806 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
49% identity, 95% coverage: 23:520/523 of query aligns to 7:502/504 of 1eyyA
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
31% identity, 51% coverage: 57:325/523 of query aligns to 55:308/485 of 4u3wA
Sites not aligning to the query:
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
26% identity, 58% coverage: 17:320/523 of query aligns to 2:284/456 of 3rhdA
- active site: N133 (= N159), H156 (≠ K184), E233 (= E265), C267 (= C302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (≠ S158), T130 (vs. gap), F132 (vs. gap), H156 (≠ K184), S158 (≠ H186), S159 (≠ G187), K160 (≠ A188), G193 (= G221), E194 (≠ R222), G197 (= G225), D198 (≠ I226), F211 (= F239), S214 (= S242), V217 (≠ G245)
Sites not aligning to the query:
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
26% identity, 84% coverage: 54:492/523 of query aligns to 521:945/959 of 5ur2B
Sites not aligning to the query:
- binding N-propargylglycine-modified flavin adenine dinucleotide: 174, 215, 216, 249, 278, 279, 280, 281, 283, 300, 301, 302, 303, 306, 329, 330, 331, 332, 356, 357, 358, 379, 398, 403, 405
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
27% identity, 77% coverage: 6:409/523 of query aligns to 12:402/484 of Q8NMB0
- N157 (= N159) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K184) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (≠ A206) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (≠ M266) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C302) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
29% identity, 62% coverage: 2:326/523 of query aligns to 1:304/488 of 5u0mA
- active site: N148 (= N159), K171 (= K184), E246 (= E265), C280 (= C302)
- binding nicotinamide-adenine-dinucleotide: F144 (= F155), Y147 (≠ S158), N148 (= N159), K171 (= K184), S173 (≠ H186), E174 (≠ G187), G207 (= G225), T222 (= T240), G223 (= G241), S224 (= S242), V227 (≠ G245), E246 (= E265), M247 (= M266), G248 (≠ S267), C280 (= C302)
Sites not aligning to the query:
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
29% identity, 62% coverage: 2:326/523 of query aligns to 1:304/488 of 5u0lA
Sites not aligning to the query:
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
35% identity, 31% coverage: 145:304/523 of query aligns to 139:288/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 156:159) binding
- K162 (≠ D170) active site, Charge relay system
- KPSE 176:179 (≠ KAHG 184:187) binding
- G209 (= G221) binding
- GTST 230:233 (≠ SRSG 242:245) binding
- E252 (= E265) active site, Proton acceptor
- C286 (= C302) binding covalent; modified: Cysteine sulfenic acid (-SOH)
Sites not aligning to the query:
- 387 binding
- 464 active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
35% identity, 31% coverage: 145:304/523 of query aligns to 138:287/489 of 4cazA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (≠ F155), G149 (= G156), W151 (≠ S158), N152 (= N159), K175 (= K184), E178 (≠ G187), G208 (= G221), G212 (= G225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249), E251 (= E265), L252 (≠ M266), C285 (= C302)
Sites not aligning to the query:
- active site: 386, 463
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: 386, 388
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
35% identity, 31% coverage: 145:304/523 of query aligns to 138:287/489 of 2woxA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F155), G149 (= G156), W151 (≠ S158), N152 (= N159), K175 (= K184), S177 (≠ H186), E178 (≠ G187), G208 (= G221), G212 (= G225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249), E251 (= E265), L252 (≠ M266), C285 (= C302)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
35% identity, 31% coverage: 145:304/523 of query aligns to 138:287/489 of 2wmeA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G156), W151 (≠ S158), K175 (= K184), S177 (≠ H186), E178 (≠ G187), G208 (= G221), G212 (= G225), F226 (= F239), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249)
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
32% identity, 45% coverage: 38:274/523 of query aligns to 35:254/486 of 3ju8A
- active site: N147 (= N159), K170 (= K184), E245 (= E265)
- binding nicotinamide-adenine-dinucleotide: G144 (= G156), Y146 (≠ S158), N147 (= N159), L152 (≠ V166), K170 (= K184), S172 (≠ H186), F220 (= F239), T221 (= T240), G222 (= G241), S223 (= S242), T226 (≠ G245), E245 (= E265), M246 (= M266), G247 (≠ S267)
Sites not aligning to the query:
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
24% identity, 83% coverage: 17:450/523 of query aligns to 21:445/497 of P17202
- I28 (≠ V24) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ --S 158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G169) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KP-------SE 182:185 (≠ KAHGAHPGTSE 184:194) binding
- L186 (= L195) binding
- SSAT 236:239 (≠ SR-S 242:244) binding
- V251 (≠ R256) binding in other chain
- L258 (≠ M266) binding
- W285 (≠ Q296) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E391) binding
- A441 (≠ R446) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
Sites not aligning to the query:
- 450 C→S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- 456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
- 460 binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
29% identity, 50% coverage: 17:275/523 of query aligns to 19:265/495 of 4v37A
- active site: N157 (= N159), K180 (= K184), E255 (= E265)
- binding nicotinamide-adenine-dinucleotide: I153 (vs. gap), S154 (vs. gap), P155 (vs. gap), W156 (≠ S158), N157 (= N159), M162 (≠ V166), K180 (= K184), S182 (= S193), E183 (= E194), G213 (= G221), G217 (= G225), A218 (≠ I226), T232 (= T240), G233 (= G241), S234 (= S242), T237 (≠ S244), E255 (= E265), L256 (≠ M266)
Sites not aligning to the query:
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 40% coverage: 66:275/523 of query aligns to 74:270/503 of Q84LK3
- N162 (= N159) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ G169) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
C0P9J6 Aminoaldehyde dehydrogenase 1a; ZmAMADH1a; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a; Aminobutyraldehyde dehydrogenase AMADH1a; Betaine aldehyde dehydrogenase AMADH1a; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Zea mays (Maize) (see paper)
30% identity, 40% coverage: 66:275/523 of query aligns to 76:272/505 of C0P9J6
Sites not aligning to the query:
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
30% identity, 40% coverage: 66:275/523 of query aligns to 71:267/500 of 4i8pA
- active site: N159 (= N159), K182 (= K184), E257 (= E265)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F155), T156 (≠ G156), P157 (≠ A157), W158 (≠ S158), N159 (= N159), M164 (≠ V166), K182 (= K184), S184 (= S193), E185 (= E194), G215 (= G221), G219 (= G225), A220 (≠ I226), T234 (= T240), G235 (= G241), S236 (= S242), T239 (≠ G245), E257 (= E265), L258 (≠ M266)
Sites not aligning to the query:
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
25% identity, 61% coverage: 7:325/523 of query aligns to 30:327/515 of 2d4eC
- active site: N173 (= N159), K196 (= K184), E271 (= E265), C305 (= C302)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F155), T170 (≠ G156), P171 (≠ A157), W172 (≠ S158), K196 (= K184), A198 (≠ H186), G229 (= G221), G233 (= G225), A234 (≠ I226), T248 (= T240), G249 (= G241), E250 (vs. gap), T253 (≠ S244), E271 (= E265), L272 (≠ M266), C305 (= C302)
Sites not aligning to the query:
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
28% identity, 58% coverage: 2:305/523 of query aligns to 3:286/476 of 5x5uA
- active site: N151 (= N159), K174 (= K184), E249 (= E265), C283 (= C302)
- binding glycerol: D15 (≠ T14), A16 (≠ T15), A17 (≠ G16), G19 (≠ R18)
- binding nicotinamide-adenine-dinucleotide: P149 (≠ A157), P207 (≠ G221), A208 (≠ R222), S211 (≠ G225), G227 (= G241), S228 (= S242), V231 (≠ G245)
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
28% identity, 58% coverage: 2:305/523 of query aligns to 3:286/476 of 5x5tA
Sites not aligning to the query:
Query Sequence
>GFF2806 FitnessBrowser__WCS417:GFF2806
MTLTGKMLIGQHATTGNREAIRAVNPATDTPMEPAYPGGDREHVAQACALAWAAFDGYRE
TSLEARAAFLEAIAAHIEALGDELIERAVAETGLPRARIQGERGRTCGQLRTFARTVRAG
EWLDVRVDPAQPQRQPLPRPDLRQRHIALGPVAVFGASNFPLAFSVAGGDTASALAAGCP
VVVKAHGAHPGTSELVGRAVAQAIQACGLPEGVFSLLYGSGREVGIALVTDPRIKAVGFT
GSRSGGVALTQAAQARPEPIPVYAEMSSINPVYLFPAALAARGEGLAKGFVGSLTQGAGQ
FCTNPGLVIGVQGPALDRFISTASELLPTCAAQTMLTPGIFKAFDSGVTALTEHARVSAK
GLAAEGPNQGQAHLFVTPAKDFLANEQLQAEVFGAASLIVVCASNEEMHQVSEHLEGQLT
ATLHLDDDDLPSAKALLPVLERKAGRLLVNGWPTGVEVCDAMVHGGPFPATSDSRSTSVG
TAAIQRFLRPVCYQDFPDALLPDALQHGNPLLLRRLLDGQREA
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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