SitesBLAST
Comparing AO356_26145 FitnessBrowser__pseudo5_N2C3_1:AO356_26145 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)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
62% identity, 98% coverage: 10:477/477 of query aligns to 8:477/477 of 2opxA
- active site: N151 (= N151), K174 (= K174), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (= F105), F152 (= F152), N284 (= N283), F312 (≠ Y311), G313 (= G312), R318 (≠ E317), D320 (= D319), I321 (≠ V320), A322 (≠ E321), Y362 (≠ H362), F440 (= F440), F440 (= F440), E441 (= E441)
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)
61% identity, 100% coverage: 3:477/477 of query aligns to 2:479/479 of P25553
- L150 (= L148) binding
- R161 (= R159) binding
- KPSE 176:179 (= KPSE 174:177) binding
- F180 (≠ E178) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A211) binding
- S230 (= S227) binding
- E251 (= E248) binding
- N286 (= N283) 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 (≠ S333) binding
- E443 (= E441) binding
- H449 (= H447) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
62% identity, 98% coverage: 10:477/477 of query aligns to 8:477/477 of 2impA
- active site: N151 (= N151), K174 (= K174), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I147), L148 (= L148), P149 (= P149), W150 (= W150), K174 (= K174), E177 (= E177), F178 (≠ E178), G207 (= G207), G211 (= G210), Q212 (≠ A211), S228 (= S227), A231 (≠ T230), K234 (≠ R233), R334 (≠ S333)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
62% identity, 98% coverage: 10:477/477 of query aligns to 8:477/477 of 2iluA
- active site: N151 (= N151), K174 (= K174), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I147), L148 (= L148), P149 (= P149), W150 (= W150), K174 (= K174), S176 (= S176), E177 (= E177), R206 (≠ D206), G207 (= G207), G211 (= G210), Q212 (≠ A211), S228 (= S227), A231 (≠ T230), K234 (≠ R233), I235 (= I234), N328 (= N327), R334 (≠ S333), F383 (= F383)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
40% identity, 98% coverage: 7:475/477 of query aligns to 2:475/477 of 6j76A
- active site: N148 (= N151), E246 (= E248), C280 (= C282), E458 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I147), T145 (≠ L148), A146 (≠ P149), W147 (= W150), N148 (= N151), K171 (= K174), T173 (≠ S176), S174 (≠ E177), G204 (= G207), G208 (= G210), T223 (= T225), G224 (= G226), S225 (= S227), A228 (≠ T230), S231 (≠ R233), I232 (= I234), E246 (= E248), L247 (= L249), C280 (= C282), E381 (= E381), F383 (= F383), H447 (= H447)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
38% identity, 98% coverage: 10:475/477 of query aligns to 6:475/494 of 5izdA
- active site: N149 (= N151), K172 (= K174), E247 (= E248), C281 (= C282), E381 (= E381), E458 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I147), T146 (≠ L148), W148 (= W150), K172 (= K174), P173 (= P175), S174 (= S176), S175 (≠ E177), R204 (≠ D206), G205 (= G207), G209 (= G210), D210 (≠ A211), G225 (= G226), S226 (= S227), T229 (= T230)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
41% identity, 95% coverage: 22:476/477 of query aligns to 23:480/489 of 6wsbA
- active site: N152 (= N151), E250 (= E248), C284 (= C282), E462 (≠ A458)
- binding nicotinamide-adenine-dinucleotide: I148 (= I147), G149 (≠ L148), A150 (≠ P149), W151 (= W150), N152 (= N151), K175 (= K174), E178 (= E177), G208 (= G207), G211 (= G210), A212 (= A211), F225 (= F224), T226 (= T225), G227 (= G226), G228 (≠ S227), T231 (= T230), V235 (≠ I234), E250 (= E248), L251 (= L249), G252 (= G250), C284 (= C282), E385 (= E381), F387 (= F383)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
39% identity, 96% coverage: 8:467/477 of query aligns to 11:471/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E248), C288 (= C282), E385 (= E381), E462 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P149), W155 (= W150), K179 (= K174), A181 (≠ S176), S182 (≠ E177), A212 (vs. gap), G216 (= G210), G232 (= G226), S233 (= S227), I236 (≠ T230), C288 (= C282), K338 (≠ S333), E385 (= E381), F387 (= F383)
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)
39% identity, 96% coverage: 8:467/477 of query aligns to 12:472/482 of P25526
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)
35% identity, 99% coverage: 4:473/477 of query aligns to 5:482/497 of P17202
- I28 (≠ F25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ LPW 148:150) binding
- Y160 (≠ F152) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 174:177) binding
- L186 (≠ E178) binding
- SSAT 236:239 (≠ SVAT 227:230) binding
- V251 (≠ I242) binding in other chain
- L258 (= L249) binding
- W285 (≠ I276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E381) binding
- A441 (≠ E432) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ E441) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ H447) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R451) binding
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
37% identity, 98% coverage: 10:476/477 of query aligns to 26:496/503 of O14293
- S248 (= S227) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 99% coverage: 4:473/477 of query aligns to 3:480/495 of 4v37A
- active site: N157 (= N151), K180 (= K174), E255 (= E248), A289 (≠ C282), E388 (= E381), E465 (≠ A458)
- binding 3-aminopropan-1-ol: C448 (≠ E441), W454 (≠ H447)
- binding nicotinamide-adenine-dinucleotide: I153 (= I147), S154 (≠ L148), P155 (= P149), W156 (= W150), N157 (= N151), M162 (≠ L156), K180 (= K174), S182 (= S176), E183 (= E177), G213 (= G207), G217 (= G210), A218 (= A211), T232 (= T225), G233 (= G226), S234 (= S227), T237 (= T230), E255 (= E248), L256 (= L249), A289 (≠ C282), E388 (= E381), F390 (= F383)
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
37% identity, 97% coverage: 8:468/477 of query aligns to 5:466/476 of 4f3xA
- active site: N150 (= N151), K173 (= K174), E247 (= E248), C281 (= C282), E379 (= E381), D456 (≠ A458)
- binding nicotinamide-adenine-dinucleotide: I146 (= I147), A147 (≠ L148), P148 (= P149), W149 (= W150), K173 (= K174), E176 (= E177), G205 (= G207), G209 (= G210), I213 (≠ S214), I223 (≠ F224), G225 (= G226), D226 (≠ S227), T229 (= T230), G249 (= G250), C281 (= C282), Q328 (≠ G330), R331 (≠ S333), E379 (= E381), F381 (= F383)
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)
35% identity, 96% coverage: 8:467/477 of query aligns to 19:485/505 of 4neaA
- active site: N166 (= N151), K189 (= K174), E264 (= E248), C298 (= C282), E399 (= E381), E476 (≠ A458)
- binding nicotinamide-adenine-dinucleotide: P164 (= P149), K189 (= K174), E192 (= E177), G222 (= G207), G226 (= G210), G242 (= G226), G243 (≠ S227), T246 (= T230), H249 (≠ R233), I250 (= I234), C298 (= C282), E399 (= E381), F401 (= F383)
7radA Crystal structure analysis of aldh1b1
35% identity, 99% coverage: 4:476/477 of query aligns to 10:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ L148), P160 (= P149), W161 (= W150), N162 (= N151), M167 (≠ L156), K185 (= K174), E188 (= E177), G218 (= G207), G222 (= G210), A223 (= A211), T237 (= T225), G238 (= G226), S239 (= S227), V242 (≠ T230), E261 (= E248), L262 (= L249), C295 (= C282), E392 (= E381), F394 (= F383)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ V101), E117 (≠ F105), F163 (= F152), E285 (≠ D272), F289 (≠ I276), N450 (= N439), V452 (≠ E441)
7mjdA Crystal structure analysis of aldh1b1
35% identity, 99% coverage: 4:476/477 of query aligns to 10:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ L148), P160 (= P149), W161 (= W150), N162 (= N151), M167 (≠ L156), K185 (= K174), E188 (= E177), G218 (= G207), G222 (= G210), F236 (= F224), T237 (= T225), G238 (= G226), S239 (= S227), V242 (≠ T230), E261 (= E248), L262 (= L249), C295 (= C282), E392 (= E381), F394 (= F383)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ F105), E285 (≠ D272), F289 (≠ I276), N450 (= N439), V452 (≠ E441)
7mjcA Crystal structure analysis of aldh1b1
35% identity, 99% coverage: 4:476/477 of query aligns to 10:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ L148), P160 (= P149), W161 (= W150), N162 (= N151), K185 (= K174), E188 (= E177), G218 (= G207), G222 (= G210), T237 (= T225), G238 (= G226), S239 (= S227), V242 (≠ T230), E261 (= E248), L262 (= L249), C295 (= C282), E392 (= E381), F394 (= F383)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 98% coverage: 8:476/477 of query aligns to 5:478/489 of 4o6rA
- active site: N150 (= N151), K173 (= K174), E248 (= E248), C282 (= C282), E383 (= E381), E460 (≠ A458)
- binding adenosine monophosphate: I146 (= I147), V147 (≠ L148), K173 (= K174), G206 (= G207), G210 (= G210), Q211 (≠ A211), F224 (= F224), G226 (= G226), S227 (= S227), T230 (= T230), R233 (= R233)
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
36% identity, 95% coverage: 25:476/477 of query aligns to 31:485/493 of 6vr6D
- active site: N156 (= N151), E253 (= E248), C287 (= C282), E467 (≠ A458)
- binding nicotinamide-adenine-dinucleotide: I152 (= I147), G153 (≠ L148), W155 (= W150), K179 (= K174), A212 (≠ G207), G215 (= G210), Q216 (≠ A211), F229 (= F224), G231 (= G226), S232 (= S227), T235 (= T230), I239 (= I234)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
36% identity, 95% coverage: 25:476/477 of query aligns to 32:486/494 of P49189
- C116 (≠ Y109) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
Query Sequence
>AO356_26145 FitnessBrowser__pseudo5_N2C3_1:AO356_26145
MSSVPVFQNFINGQFTHSEAHLDVFNPATGALLSRVPASNAADVDQALATARAAQKDWSA
KPAIERAGYLRRIAAKLRENVAHLAHTITLEQGKISALAEVEVHFTADYLDYMAEWARRI
EGEIITSDRPGENIFLFRKPLGVVAGILPWNFPFFLIARKMAPALLTGNTIVIKPSEETP
NNCFEFARLVAATDLPPGVFNVVCGDGQVGAALSGHKGVDMISFTGSVATGSRIMTAAAP
NITKLNLELGGKAPAIVLADADLALAVKAIRDSRIINTGQVCNCAERVYVERKVADQFIE
RISAAMSATRYGDPIAEADVEMGPLINRQGLDSVEHKVRTALSQGASLVSGGSVADRSSG
FHFQPTVLAGCNASMDIMREEIFGPVLPIQIIDDLDEAIALANDCDYGLTSSIYTRDLSR
AMHAIRGLDFGETYVNRENFEAMQGFHAGVRKSGIGGADGKHGLYEYTHTHAVYLQS
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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