SitesBLAST
Comparing BWI76_RS13210 FitnessBrowser__Koxy:BWI76_RS13210 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)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
88% identity, 100% coverage: 1:479/479 of query aligns to 1:479/479 of P25553
- M1 (= M1) modified: Initiator methionine, Removed
- L150 (= L150) binding
- R161 (= R161) binding
- KPSE 176:179 (= KPSE 176:179) binding
- F180 (= F180) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (= Q214) binding
- S230 (= S230) binding
- E251 (= E251) binding
- N286 (= N286) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (= R336) binding
- E443 (= E443) binding
- H449 (= H449) binding
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
89% identity, 99% coverage: 4:479/479 of query aligns to 2:477/477 of 2opxA
- active site: N151 (= N153), K174 (= K176), E249 (= E251), C283 (= C285), E381 (= E383), A458 (= A460)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (= F107), F152 (= F154), N284 (= N286), F312 (= F314), G313 (= G315), R318 (= R320), D320 (= D322), I321 (= I323), A322 (= A324), Y362 (≠ F364), F440 (= F442), F440 (= F442), E441 (= E443)
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
88% identity, 99% coverage: 4:479/479 of query aligns to 2:477/477 of 2impA
- active site: N151 (= N153), K174 (= K176), E249 (= E251), C283 (= C285), E381 (= E383), A458 (= A460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I149), L148 (= L150), P149 (= P151), W150 (= W152), K174 (= K176), E177 (= E179), F178 (= F180), G207 (= G209), G211 (= G213), Q212 (= Q214), S228 (= S230), A231 (= A233), K234 (= K236), R334 (= R336)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
88% identity, 99% coverage: 4:479/479 of query aligns to 2:477/477 of 2iluA
- active site: N151 (= N153), K174 (= K176), E249 (= E251), C283 (= C285), E381 (= E383), A458 (= A460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I149), L148 (= L150), P149 (= P151), W150 (= W152), K174 (= K176), S176 (= S178), E177 (= E179), R206 (= R208), G207 (= G209), G211 (= G213), Q212 (= Q214), S228 (= S230), A231 (= A233), K234 (= K236), I235 (= I237), N328 (= N330), R334 (= R336), F383 (= F385)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
43% identity, 99% coverage: 6:477/479 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N153), E246 (= E251), C280 (= C285), E458 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I149), T145 (≠ L150), A146 (≠ P151), W147 (= W152), N148 (= N153), K171 (= K176), T173 (≠ S178), S174 (≠ E179), G204 (= G209), G208 (= G213), T223 (= T228), G224 (= G229), S225 (= S230), A228 (= A233), S231 (≠ K236), I232 (= I237), E246 (= E251), L247 (= L252), C280 (= C285), E381 (= E383), F383 (= F385), H447 (= H449)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
38% identity, 98% coverage: 9:477/479 of query aligns to 5:475/494 of 5izdA
- active site: N149 (= N153), K172 (= K176), E247 (= E251), C281 (= C285), E381 (= E383), E458 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I149), T146 (≠ L150), W148 (= W152), K172 (= K176), P173 (= P177), S174 (= S178), S175 (≠ E179), R204 (= R208), G205 (= G209), G209 (= G213), D210 (≠ Q214), G225 (= G229), S226 (= S230), T229 (≠ A233)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
40% identity, 97% coverage: 11:477/479 of query aligns to 14:479/481 of 3jz4A
- active site: N156 (= N153), K179 (= K176), E254 (= E251), C288 (= C285), E385 (= E383), E462 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P151), W155 (= W152), K179 (= K176), A181 (≠ S178), S182 (≠ E179), A212 (≠ G209), G216 (= G213), G232 (= G229), S233 (= S230), I236 (≠ A233), C288 (= C285), K338 (≠ R336), E385 (= E383), F387 (= F385)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
40% identity, 97% coverage: 11:477/479 of query aligns to 15:480/482 of P25526
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
37% identity, 97% coverage: 10:475/479 of query aligns to 21:491/505 of 4neaA
- active site: N166 (= N153), K189 (= K176), E264 (= E251), C298 (= C285), E399 (= E383), E476 (≠ A460)
- binding nicotinamide-adenine-dinucleotide: P164 (= P151), K189 (= K176), E192 (= E179), G222 (= G209), G226 (= G213), G242 (= G229), G243 (≠ S230), T246 (≠ A233), H249 (≠ K236), I250 (= I237), C298 (= C285), E399 (= E383), F401 (= F385)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
36% identity, 96% coverage: 10:468/479 of query aligns to 4:460/482 of 5ek6A
- active site: N147 (= N153), K170 (= K176), E245 (= E251), C279 (= C285), E374 (= E383), E452 (≠ A460)
- binding 2-methylpropanal: I152 (≠ L158), K155 (≠ R161), T222 (= T228), E245 (= E251), F441 (≠ H449)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I149), T144 (≠ L150), W146 (= W152), N147 (= N153), I152 (≠ L158), K170 (= K176), A172 (≠ S178), S173 (≠ E179), P202 (≠ R208), G203 (= G209), G207 (= G213), F221 (≠ M227), T222 (= T228), G223 (= G229), E224 (≠ S230), T227 (≠ A233), I231 (= I237), E245 (= E251), L246 (= L252), C279 (= C285), E374 (= E383)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
36% identity, 96% coverage: 10:468/479 of query aligns to 4:460/482 of 4h73A
- active site: N147 (= N153), K170 (= K176), E245 (= E251), C279 (= C285), E374 (= E383), E452 (≠ A460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I149), T144 (≠ L150), P145 (= P151), W146 (= W152), K170 (= K176), A172 (≠ S178), S173 (≠ E179), G203 (= G209), G207 (= G213), F221 (≠ M227), G223 (= G229), E224 (≠ S230), T227 (≠ A233)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
36% identity, 96% coverage: 10:468/479 of query aligns to 11:467/490 of 5ekcE
- active site: N154 (= N153), K177 (= K176), E252 (= E251), C286 (= C285), E381 (= E383), E459 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I149), T151 (≠ L150), P152 (= P151), W153 (= W152), K177 (= K176), S180 (≠ E179), G210 (= G209), G214 (= G213), F228 (≠ M227), G230 (= G229), E231 (≠ S230), T234 (≠ A233), N331 (= N330), R333 (≠ A332), Q334 (≠ A333)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
40% identity, 97% coverage: 5:469/479 of query aligns to 1:464/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
40% identity, 97% coverage: 5:469/479 of query aligns to 1:464/474 of 1wndA
- active site: N149 (= N153), K172 (= K176), E246 (= E251), C280 (= C285), E378 (= E383), D455 (≠ A460)
- binding calcium ion: G249 (= G254), K250 (= K255), A251 (= A256), G405 (= G410), L406 (= L411), A407 (≠ T412), Y427 (≠ F432)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
40% identity, 97% coverage: 5:469/479 of query aligns to 1:464/474 of 1wnbB
- active site: N149 (= N153), K172 (= K176), E246 (= E251), C280 (= C285), E378 (= E383), D455 (≠ A460)
- binding betaine aldehyde: D279 (≠ V284), F436 (≠ N441), L438 (≠ E443)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I149), A146 (≠ L150), W148 (= W152), K172 (= K176), G204 (= G209), G208 (= G213), D209 (≠ Q214), T223 (= T228), G224 (= G229), S225 (= S230), T228 (≠ A233), H231 (≠ K236), G248 (= G253), E378 (= E383)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
40% identity, 97% coverage: 5:469/479 of query aligns to 1:464/474 of 1wnbA
- active site: N149 (= N153), K172 (= K176), E246 (= E251), C280 (= C285), E378 (= E383), D455 (≠ A460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I149), A146 (≠ L150), W148 (= W152), K172 (= K176), G204 (= G209), G208 (= G213), D209 (≠ Q214), G224 (= G229), S225 (= S230), T228 (≠ A233), H231 (≠ K236), G248 (= G253), F380 (= F385)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 98% coverage: 9:478/479 of query aligns to 25:496/503 of O14293
- S248 (= S230) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
38% identity, 98% coverage: 9:478/479 of query aligns to 6:474/476 of 4f3xA
- active site: N150 (= N153), K173 (= K176), E247 (= E251), C281 (= C285), E379 (= E383), D456 (≠ A460)
- binding nicotinamide-adenine-dinucleotide: I146 (= I149), A147 (≠ L150), P148 (= P151), W149 (= W152), K173 (= K176), E176 (= E179), G205 (= G209), G209 (= G213), I213 (≠ A217), I223 (≠ M227), G225 (= G229), D226 (≠ S230), T229 (≠ A233), G249 (= G253), C281 (= C285), Q328 (≠ A333), R331 (= R336), E379 (= E383), F381 (= F385)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
35% identity, 99% coverage: 6:478/479 of query aligns to 5:481/489 of 4cazA
- active site: N152 (= N153), K175 (= K176), E251 (= E251), C285 (= C285), E386 (= E383), E463 (≠ A460)
- 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 (= I149), G149 (≠ L150), W151 (= W152), N152 (= N153), K175 (= K176), E178 (= E179), G208 (= G209), G212 (= G213), F226 (≠ M227), T227 (= T228), G228 (= G229), G229 (≠ S230), T232 (≠ A233), V236 (≠ I237), E251 (= E251), L252 (= L252), C285 (= C285), E386 (= E383), F388 (= F385)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
35% identity, 99% coverage: 6:478/479 of query aligns to 5:481/489 of 2woxA
- active site: N152 (= N153), K175 (= K176), E251 (= E251), C285 (= C285), E386 (= E383), E463 (≠ A460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I149), G149 (≠ L150), W151 (= W152), N152 (= N153), K175 (= K176), S177 (= S178), E178 (= E179), G208 (= G209), G212 (= G213), F226 (≠ M227), T227 (= T228), G228 (= G229), G229 (≠ S230), T232 (≠ A233), V236 (≠ I237), E251 (= E251), L252 (= L252), C285 (= C285), E386 (= E383), F388 (= F385)
Query Sequence
>BWI76_RS13210 FitnessBrowser__Koxy:BWI76_RS13210
MTAPVQHPMYIDGQFEPGRGDAWIDVINPATEALLSRIPDGSAEDARRAILAAERAQPGW
EALPAIERARWLRKIAAGIRERAEEIAALIVAEGGKIQQLAAVEVSFTADYLDYMAEWAR
RYEGEIVQSDRTGENILVFKRALGVTTGILPWNFPFFLIARKLAPALITGNTIVIKPSEF
TPNNAIAFAQIVHDIGLPKGVFNLVLGRGETVGQELASNPKVAMVSMTGSVAAGEKIMAA
AAKNITKVCLELGGKAPAIVMDDADLELAVKAVVDSRVINSGQVCNCVERVYVQKGIYDR
FVNRLGEALKAVQFGDPASRDDIAMGPLINAAALARVEQKVAKAVAQGARVALGGKAVTG
RGYFYPPTLLLDVRQEMDIVHEETFGPVLPVVAFDTLEEALAMANDSDYGLTSSIYTRDL
NVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGRHGLNEYLQTQVVYLQA
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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