SitesBLAST
Comparing Ga0059261_1896 Ga0059261_1896 NAD-dependent aldehyde dehydrogenases 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
46% identity, 87% coverage: 66:520/524 of query aligns to 50:501/504 of 1eyyA
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
30% identity, 62% coverage: 2:325/524 of query aligns to 1:304/488 of 5u0mA
- active site: N148 (= N158), K171 (= K183), E246 (= E264), C280 (= C301)
- binding nicotinamide-adenine-dinucleotide: F144 (= F154), Y147 (≠ S157), N148 (= N158), K171 (= K183), S173 (≠ H185), E174 (≠ R186), G207 (= G224), T222 (= T239), G223 (= G240), S224 (= S241), V227 (≠ G244), E246 (= E264), M247 (= M265), G248 (≠ A266), C280 (= C301)
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)
30% identity, 62% coverage: 2:325/524 of query aligns to 1:304/488 of 5u0lA
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
30% identity, 58% coverage: 20:321/524 of query aligns to 19:299/486 of 3ju8A
- active site: N147 (= N158), K170 (= K183), E245 (= E264), C279 (= C301)
- binding nicotinamide-adenine-dinucleotide: G144 (= G155), Y146 (≠ S157), N147 (= N158), L152 (≠ F163), K170 (= K183), S172 (≠ H185), F220 (= F238), T221 (= T239), G222 (= G240), S223 (= S241), T226 (≠ G244), E245 (= E264), M246 (= M265), G247 (≠ A266), C279 (= C301)
Sites not aligning to the query:
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
26% identity, 52% coverage: 8:277/524 of query aligns to 13:266/487 of Q9H2A2
- R109 (= R105) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N158) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
26% identity, 61% coverage: 8:327/524 of query aligns to 9:305/454 of 3ty7B
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)
28% identity, 57% coverage: 7:303/524 of query aligns to 9:288/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 155:158) binding
- K162 (≠ D169) active site, Charge relay system
- KPSE 176:179 (≠ KGHR 183:186) binding
- G209 (≠ S220) binding
- GTST 230:233 (≠ SRGG 241:244) binding
- E252 (= E264) active site, Proton acceptor
- C286 (= C301) binding covalent; modified: Cysteine sulfenic acid (-SOH)
Sites not aligning to the query:
- 387 binding
- 464 active site, Charge relay system
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
29% identity, 56% coverage: 8:302/524 of query aligns to 30:306/515 of 2d4eC
- active site: N173 (= N158), K196 (= K183), E271 (= E264), C305 (= C301)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F154), T170 (≠ G155), P171 (≠ A156), W172 (≠ S157), K196 (= K183), A198 (≠ H185), G229 (≠ S220), G233 (= G224), A234 (≠ E225), T248 (= T239), G249 (= G240), E250 (≠ S241), T253 (≠ G244), E271 (= E264), L272 (≠ M265), C305 (= C301)
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
28% identity, 57% coverage: 7:303/524 of query aligns to 8:287/489 of 4cazA
- active site: N152 (= N158), K175 (= K183), E251 (= E264), C285 (= C301)
- 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 (≠ F154), G149 (= G155), W151 (≠ S157), N152 (= N158), K175 (= K183), E178 (≠ R186), G208 (≠ S220), G212 (= G224), F226 (= F238), T227 (= T239), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248), E251 (= E264), L252 (≠ M265), C285 (= C301)
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)
28% identity, 57% coverage: 7:303/524 of query aligns to 8:287/489 of 2woxA
- active site: N152 (= N158), K175 (= K183), E251 (= E264), C285 (= C301)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F154), G149 (= G155), W151 (≠ S157), N152 (= N158), K175 (= K183), S177 (≠ H185), E178 (≠ R186), G208 (≠ S220), G212 (= G224), F226 (= F238), T227 (= T239), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248), E251 (= E264), L252 (≠ M265), C285 (= C301)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
28% identity, 57% coverage: 7:303/524 of query aligns to 8:287/489 of 2wmeA
- active site: N152 (= N158), K175 (= K183), E251 (= E264), C285 (= C301)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G155), W151 (≠ S157), K175 (= K183), S177 (≠ H185), E178 (≠ R186), G208 (≠ S220), G212 (= G224), F226 (= F238), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248)
Sites not aligning to the query:
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
24% identity, 53% coverage: 40:319/524 of query aligns to 24:284/456 of 3rhdA
- active site: N133 (= N158), H156 (≠ K183), E233 (= E264), C267 (= C301)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (≠ S157), T130 (vs. gap), F132 (vs. gap), H156 (≠ K183), S158 (≠ H185), S159 (≠ R186), K160 (≠ A187), G193 (≠ S220), E194 (≠ R221), G197 (= G224), D198 (≠ E225), F211 (= F238), S214 (= S241), V217 (≠ G244)
Sites not aligning to the query:
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
27% identity, 57% coverage: 6:302/524 of query aligns to 11:297/505 of O24174
- N164 (= N158) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ G168) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
29% identity, 61% coverage: 8:327/524 of query aligns to 14:315/485 of 2w8rA
Sites not aligning to the query:
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
29% identity, 61% coverage: 8:327/524 of query aligns to 14:315/485 of 2w8qA
Sites not aligning to the query:
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
29% identity, 61% coverage: 8:327/524 of query aligns to 64:365/535 of P51649
- C93 (≠ A34) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (≠ A130) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ R134) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P136) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ A166) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C178) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KGHR 183:186) binding
- T233 (≠ H188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A192) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ G214) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G224) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSRGGG 240:245) binding
- R334 (≠ V290) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ A291) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (≠ Q299) modified: Disulfide link with 342, In inhibited form
- C342 (= C301) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 372 natural variant: N -> S
- 382 P → L: in SSADHD; 2% of activity
- 406 V → I: in dbSNP:rs143741652
- 409 G → D: in SSADHD; <1% of activity; dbSNP:rs118203984
- 498 binding ; S→A: Reduces catalytic activity to less than 15% of wild-type.
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
28% identity, 51% coverage: 7:274/524 of query aligns to 8:265/495 of 4v37A
- active site: N157 (= N158), K180 (= K183), E255 (= E264)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ F154), S154 (≠ G155), P155 (≠ A156), W156 (≠ S157), N157 (= N158), M162 (≠ F163), K180 (= K183), S182 (≠ A192), E183 (= E193), G213 (≠ S220), G217 (= G224), A218 (≠ E225), T232 (= T239), G233 (= G240), S234 (= S241), T237 (≠ G244), E255 (= E264), L256 (≠ M265)
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)
28% identity, 51% coverage: 7:274/524 of query aligns to 10:267/497 of P17202
- I28 (≠ Y23) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ GAS 155:157) binding
- Y160 (≠ F159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G168) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- K-------PSE 182:185 (≠ KGHRAHPGTAE 183:193) binding
- L186 (= L194) binding
- SSAT 236:239 (≠ SRGG 241:244) binding
- V251 (≠ P256) binding in other chain
- L258 (≠ M265) binding
Sites not aligning to the query:
- 285 W→A: Decreases binding affinity for betaine aldehyde.
- 390 binding
- 441 A→I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- 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
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
29% identity, 60% coverage: 7:321/524 of query aligns to 8:303/489 of 6wsbA
- active site: N152 (= N158), E250 (= E264), C284 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F154), G149 (= G155), A150 (= A156), W151 (≠ S157), N152 (= N158), K175 (= K183), E178 (≠ R186), G208 (≠ S220), G211 (= G224), A212 (≠ E225), F225 (= F238), T226 (= T239), G227 (= G240), G228 (≠ S241), T231 (≠ G244), V235 (≠ L248), E250 (= E264), L251 (≠ M265), G252 (≠ A266), C284 (= C301)
Sites not aligning to the query:
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
25% identity, 85% coverage: 8:452/524 of query aligns to 8:433/475 of Q59931
- R103 (≠ L112) binding
- S151 (≠ G155) binding
- K177 (= K183) binding
- T180 (≠ R186) binding
- D215 (≠ E225) binding
- 230:251 (vs. 240:265, 35% identical) binding
- E377 (vs. gap) binding
Sites not aligning to the query:
Query Sequence
>Ga0059261_1896 Ga0059261_1896 NAD-dependent aldehyde dehydrogenases
MELTGGLFIGGERRQSDARFHAYDPAAGADIADAGFASASEQDVADACAAAEAAFLPYST
KPLEARARFLETIADEIEALGDVLIERACRESGLPAARITGERGRTVGQLRLFAKEVRDG
AWQKLRIDHADRERTPPRPDLRLRMVPLGPVAVFGASNFPLAFSTAGGDTASAFAAGCPV
VVKGHRAHPGTAELIATAIIRAVETCGMPAGTFGMVNGTSRKVGETLVADPRIQAVGFTG
SRGGGEALMRIAAARPRPIPVYAEMAAINPVILMPQALKARGPALAEAFVASLAMGAGQF
CTNPGLVMGIDGPELDAFVARAGEVLSGQAAQVMLTDGIWEAFESGKAKLAGSAFVTKVA
EGVEADGPNRGRAALFSVAGKDFLADPVHLHEVFGVSSVVVRCASLEELKAVLGELEGQL
TATLQVDEGDYPEAQALLPVLERTVGRVIANGWPTGVEVTHAMVHGGPYPSTSDPRSTSV
GTLAIDRFLRPVSYQDLPEALLPAALRENAQAGTVARIDGSWTI
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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