SitesBLAST
Comparing BWI76_RS11680 FitnessBrowser__Koxy:BWI76_RS11680 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)
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
59% identity, 99% coverage: 2:486/492 of query aligns to 5:488/488 of 5u0mA
- active site: N148 (= N145), K171 (= K168), E246 (= E243), C280 (= C277), E377 (= E375), P455 (= P453)
- binding nicotinamide-adenine-dinucleotide: F144 (= F141), Y147 (= Y144), N148 (= N145), K171 (= K168), S173 (= S170), E174 (= E171), G207 (= G204), T222 (= T219), G223 (= G220), S224 (= S221), V227 (≠ T224), E246 (= E243), M247 (= M244), G248 (= G245), C280 (= C277), E377 (= E375), F379 (= F377)
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
59% identity, 99% coverage: 2:486/492 of query aligns to 5:488/488 of 5u0lA
- active site: N148 (= N145), K171 (= K168), E246 (= E243), C280 (= C277), E377 (= E375), P455 (= P453)
- binding decanal: K107 (= K104), H152 (= H149), L153 (= L150), G156 (= G153), H157 (= H154), S456 (≠ G454), A457 (= A455)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
61% identity, 98% coverage: 4:484/492 of query aligns to 6:486/486 of 3ju8A
- active site: N147 (= N145), K170 (= K168), E245 (= E243), C279 (= C277), E377 (= E375), P455 (= P453)
- binding nicotinamide-adenine-dinucleotide: G144 (= G142), Y146 (= Y144), N147 (= N145), L152 (= L150), K170 (= K168), S172 (= S170), F220 (= F218), T221 (= T219), G222 (= G220), S223 (= S221), T226 (= T224), E245 (= E243), M246 (= M244), G247 (= G245), C279 (= C277), E377 (= E375), F379 (= F377), F444 (= F442)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
33% identity, 92% coverage: 14:464/492 of query aligns to 26:495/511 of 6fkuA
- active site: N159 (= N145), E261 (= E243), C295 (= C277), E483 (≠ R452)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (≠ F141), T156 (≠ G142), N159 (= N145), K182 (= K168), S184 (= S170), E185 (= E171), G214 (= G200), G215 (= G204), K216 (≠ E205), G220 (= G209), Q221 (= Q210), F237 (= F218), T238 (= T219), G239 (= G220), S240 (= S221), V243 (≠ T224), E261 (= E243), L262 (≠ M244), C295 (= C277), R342 (≠ Q325), F343 (≠ A326), E404 (= E375), F406 (= F377)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 93% coverage: 3:461/492 of query aligns to 12:481/505 of O24174
- N164 (= N145) 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 (≠ G153) 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.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
31% identity, 93% coverage: 2:460/492 of query aligns to 12:476/494 of 4pz2B
- active site: N159 (= N145), K182 (= K168), E258 (= E243), C292 (= C277), E392 (= E375), D469 (≠ P453)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F141), I156 (≠ G142), P157 (= P143), W158 (≠ Y144), N159 (= N145), M164 (≠ L150), K182 (= K168), A184 (≠ S170), E185 (= E171), G215 (= G200), G219 (= G204), F233 (= F218), T234 (= T219), G235 (= G220), S236 (= S221), V239 (≠ T224), E258 (= E243), L259 (≠ M244), C292 (= C277), E392 (= E375), F394 (= F377)
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)
32% identity, 93% coverage: 3:461/492 of query aligns to 10:476/497 of P17202
- I28 (vs. gap) binding
- D96 (≠ E86) binding
- SPW 156:158 (≠ GPY 142:144) binding
- Y160 (≠ F146) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G153) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 168:171) binding
- L186 (= L172) binding
- SSAT 236:239 (= SSAT 221:224) binding
- V251 (≠ E237) binding in other chain
- L258 (≠ M244) binding
- W285 (≠ I271) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E375) binding
- A441 (= A424) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A436) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F442) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G446) binding
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)
33% identity, 93% coverage: 5:461/492 of query aligns to 15:472/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 93% coverage: 5:461/492 of query aligns to 14:471/481 of 3jz4A
- active site: N156 (= N145), K179 (= K168), E254 (= E243), C288 (= C277), E385 (= E375), E462 (≠ P453)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P143), W155 (≠ Y144), K179 (= K168), A181 (≠ S170), S182 (≠ E171), A212 (≠ R201), G216 (= G204), G232 (= G220), S233 (= S221), I236 (≠ T224), C288 (= C277), K338 (= K329), E385 (= E375), F387 (= F377)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
32% identity, 93% coverage: 3:461/492 of query aligns to 8:474/495 of 4v37A
- active site: N157 (= N145), K180 (= K168), E255 (= E243), A289 (≠ C277), E388 (= E375), E465 (≠ P453)
- binding 3-aminopropan-1-ol: C448 (≠ A436), W454 (≠ F442)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ F141), S154 (≠ G142), P155 (= P143), W156 (≠ Y144), N157 (= N145), M162 (≠ L150), K180 (= K168), S182 (= S170), E183 (= E171), G213 (= G200), G217 (= G204), A218 (≠ E205), T232 (= T219), G233 (= G220), S234 (= S221), T237 (= T224), E255 (= E243), L256 (≠ M244), A289 (≠ C277), E388 (= E375), F390 (= F377)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
34% identity, 89% coverage: 21:460/492 of query aligns to 39:483/495 of 5iuwA
- active site: N166 (= N145), K189 (= K168), E265 (= E243), C300 (= C277), E399 (= E375), D476 (≠ P453)
- binding 1h-indol-3-ylacetic acid: F167 (= F146), M170 (≠ H149), C300 (= C277), D457 (≠ T434), F465 (= F442)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ F141), V163 (≠ G142), P164 (= P143), W165 (≠ Y144), N166 (= N145), K189 (= K168), G222 (= G200), G226 (= G204), K227 (≠ E205), F240 (= F218), T241 (= T219), G242 (= G220), S243 (= S221), I246 (≠ T224), Y253 (≠ Q231), E265 (= E243), A266 (≠ M244), C300 (= C277), E399 (= E375), F401 (= F377)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
34% identity, 89% coverage: 21:460/492 of query aligns to 39:483/495 of 5iuvA
- active site: N166 (= N145), K189 (= K168), E265 (= E243), C300 (= C277), E399 (= E375), D476 (≠ P453)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ F141), V163 (≠ G142), P164 (= P143), W165 (≠ Y144), N166 (= N145), K189 (= K168), S191 (= S170), G222 (= G200), G226 (= G204), K227 (≠ E205), F240 (= F218), T241 (= T219), G242 (= G220), S243 (= S221), I246 (≠ T224), Y253 (≠ Q231), E265 (= E243), A266 (≠ M244), C300 (= C277), E399 (= E375), F401 (= F377)
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)
30% identity, 90% coverage: 20:461/492 of query aligns to 28:476/487 of Q9H2A2
- R109 (≠ A100) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N145) mutation to A: Complete loss of activity.
- R451 (≠ A436) mutation to A: Complete loss of activity.
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)
34% identity, 81% coverage: 53:452/492 of query aligns to 68:471/505 of C0P9J6
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
34% identity, 81% coverage: 53:452/492 of query aligns to 63:466/500 of 4i8pA
- active site: N159 (= N145), K182 (= K168), E257 (= E243), C291 (= C277), E390 (= E375)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F141), T156 (≠ G142), P157 (= P143), W158 (≠ Y144), N159 (= N145), M164 (≠ L150), K182 (= K168), S184 (= S170), E185 (= E171), G215 (= G200), G219 (= G204), A220 (≠ E205), T234 (= T219), G235 (= G220), S236 (= S221), T239 (= T224), E257 (= E243), L258 (≠ M244), C291 (= C277), E390 (= E375), F392 (= F377), W456 (≠ F442)
Sites not aligning to the query:
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
34% identity, 89% coverage: 21:460/492 of query aligns to 39:483/495 of 7jsoA
- active site: N166 (= N145), E265 (= E243), A300 (≠ C277), D476 (≠ P453)
- binding 1h-indol-3-ylacetic acid: F167 (= F146), W174 (≠ G153), V299 (≠ R276), A300 (≠ C277), T301 (= T278), D457 (≠ T434), F465 (= F442)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (≠ F141), V163 (≠ G142), P164 (= P143), W165 (≠ Y144), K189 (= K168), E192 (= E171), G222 (= G200), G226 (= G204), K227 (≠ E205), F240 (= F218), G242 (= G220), S243 (= S221), I246 (≠ T224), A266 (≠ M244), G267 (= G245), A300 (≠ C277), E399 (= E375), F401 (= F377)
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
33% identity, 81% coverage: 53:452/492 of query aligns to 66:469/503 of Q84LK3
- N162 (= N145) 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 (≠ G153) 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).
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 90% coverage: 21:461/492 of query aligns to 25:469/489 of 4o6rA
- active site: N150 (= N145), K173 (= K168), E248 (= E243), C282 (= C277), E383 (= E375), E460 (≠ P453)
- binding adenosine monophosphate: I146 (≠ F141), V147 (≠ G142), K173 (= K168), G206 (= G200), G210 (= G204), Q211 (≠ E205), F224 (= F218), G226 (= G220), S227 (= S221), T230 (= T224), R233 (≠ Q227)
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
33% identity, 83% coverage: 50:455/492 of query aligns to 87:499/516 of 2eiwA
- active site: N184 (= N145), K207 (= K168), E288 (= E243), C322 (= C277), E417 (= E375), T497 (≠ P453)
- binding proline: E137 (≠ A100), F185 (= F146), S323 (≠ T278), G477 (= G435), A478 (= A436), F485 (= F442)
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
33% identity, 83% coverage: 50:455/492 of query aligns to 87:499/516 of 2j5nA
- active site: N184 (= N145), K207 (= K168), E288 (= E243), C322 (= C277), E417 (= E375), T497 (≠ P453)
- binding glycine: S323 (≠ T278), G477 (= G435), A478 (= A436), F485 (= F442)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ F141), A181 (≠ G142), P182 (= P143), W183 (≠ Y144), N184 (= N145), I189 (≠ L150), K207 (= K168), E210 (= E171), G240 (= G200), F258 (= F218), T259 (= T219), G260 (= G220), S261 (= S221), V264 (≠ T224), E288 (= E243), T289 (≠ M244), C322 (= C277), E417 (= E375), F419 (= F377)
Query Sequence
>BWI76_RS11680 FitnessBrowser__Koxy:BWI76_RS11680
MSLWINGDWQSGRGPARSKHNPVSQTLLWQGNDADADQVALAVSAARAAFPAWARQPFAA
RKAIAEKFASLLEANKSELTAVIARETGKPRWEAATEITAMINKIAISVNAYHSRTGEAQ
TAMADGEATLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPQSGEAV
VKLWAEAGLPPGVLNLLQGGRETGEALSGQADIDGLLFTGSSATGFQLHRQLAGQPEKIL
ALEMGGNNPLIVDDPQDIDAAVHLTIQSAFITAGQRCTCARRLLVKRGEAGDAFLQRLVT
VSQTLIPAAWDAEPQPFIGGLISAQAAQKVHQAWLAHVASGGKTLLEPRLLQAGTSLLTP
GIIEMSAVAQVADEEVFGPLLCVWRYDHFDEAIALANATRFGLSCGLISAERDKFDQLLL
EARAGIVNWNKPLTGAASTAPFGGTGASGNHRPGAWYAADYCAWPMASLESPELSLPATL
SPGLNFRQETSQ
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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