SitesBLAST
Comparing AO353_24855 FitnessBrowser__pseudo3_N2E3:AO353_24855 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
49% identity, 99% coverage: 2:469/471 of query aligns to 9:477/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (≠ N144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (≠ Q173), G210 (= G203), P211 (≠ S204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E378), F388 (= F380), F451 (= F443)
- binding octanal: W155 (≠ Y148), S285 (≠ T278)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
46% identity, 99% coverage: 4:469/471 of query aligns to 5:475/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E378), E460 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ N144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ S204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (≠ R230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E378), F386 (= F380)
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)
38% identity, 98% coverage: 7:469/471 of query aligns to 10:482/497 of P17202
- I28 (= I25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ NPW 144:146) binding
- Y160 (= Y148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSQ 170:173) binding
- L186 (≠ E174) binding
- SSAT 236:239 (≠ STGA 224:227) binding
- V251 (= V239) binding in other chain
- L258 (= L246) binding
- W285 (≠ I273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E378) binding
- A441 (≠ Q429) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ N438) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F443) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K447) binding
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 7:471/471 of query aligns to 19:488/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E378), E471 (= E454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (≠ Q173), Q192 (≠ E174), G221 (= G203), G225 (= G207), G241 (= G223), S242 (= S224), T245 (≠ A227), L264 (= L246), C297 (= C279), E394 (= E378), F396 (= F380)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 7:471/471 of query aligns to 19:488/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E378), E471 (= E454)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ N144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (≠ Q173), G221 (= G203), G225 (= G207), A226 (≠ E208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ R230), L264 (= L246), C297 (= C279), Q344 (= Q326), R347 (≠ T329), E394 (= E378), F396 (= F380)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
37% identity, 98% coverage: 7:469/471 of query aligns to 8:480/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E378), E465 (= E454)
- binding 3-aminopropan-1-ol: C448 (≠ N438), W454 (≠ F443)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), S154 (≠ N144), P155 (= P145), W156 (= W146), N157 (= N147), M162 (≠ Q152), K180 (= K170), S182 (= S172), E183 (≠ Q173), G213 (= G203), G217 (= G207), A218 (≠ E208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E378), F390 (= F380)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 98% coverage: 7:469/471 of query aligns to 12:487/505 of O24174
- N164 (= N147) 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 (≠ G155) 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.
7radA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 4:471/471 of query aligns to 12:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ N144), P160 (= P145), W161 (= W146), N162 (= N147), M167 (≠ Q152), K185 (= K170), E188 (≠ Q173), G218 (= G203), G222 (= G207), A223 (≠ E208), T237 (= T222), G238 (= G223), S239 (= S224), V242 (≠ A227), E261 (= E245), L262 (= L246), C295 (= C279), E392 (= E378), F394 (= F380)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ V102), E117 (≠ G106), F163 (≠ Y148), E285 (≠ Q269), F289 (≠ I273), N450 (= N438), V452 (≠ L440)
7mjdA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 4:471/471 of query aligns to 12:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ N144), P160 (= P145), W161 (= W146), N162 (= N147), M167 (≠ Q152), K185 (= K170), E188 (≠ Q173), G218 (= G203), G222 (= G207), F236 (= F221), T237 (= T222), G238 (= G223), S239 (= S224), V242 (≠ A227), E261 (= E245), L262 (= L246), C295 (= C279), E392 (= E378), F394 (= F380)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ G106), E285 (≠ Q269), F289 (≠ I273), N450 (= N438), V452 (≠ L440)
7mjcA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 4:471/471 of query aligns to 12:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ N144), P160 (= P145), W161 (= W146), N162 (= N147), K185 (= K170), E188 (≠ Q173), G218 (= G203), G222 (= G207), T237 (= T222), G238 (= G223), S239 (= S224), V242 (≠ A227), E261 (= E245), L262 (= L246), C295 (= C279), E392 (= E378), F394 (= F380)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 100% coverage: 3:471/471 of query aligns to 12:487/489 of 7a6qB
- active site: N163 (= N147), E262 (= E245), C296 (= C279), E470 (= E454)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), W162 (= W146), K186 (= K170), E189 (≠ Q173), G219 (= G203), G223 (= G207), S240 (= S224), V243 (≠ A227), K342 (≠ A325)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (= A22), T33 (≠ V24), C34 (≠ I25), P36 (= P27), D103 (≠ E91), E189 (≠ Q173), Q190 (≠ E174), F218 (≠ P202), I339 (≠ C322), D340 (≠ S323)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G106), D141 (≠ G128), N143 (≠ S130), N451 (= N438), L453 (= L440), A455 (vs. gap)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 100% coverage: 3:471/471 of query aligns to 12:487/489 of 7a6qA
- active site: N163 (= N147), E262 (= E245), C296 (= C279), E470 (= E454)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), T160 (≠ N144), W162 (= W146), K186 (= K170), A188 (≠ S172), E189 (≠ Q173), G219 (= G203), G223 (= G207), S240 (= S224), V243 (≠ A227), K342 (≠ A325), K346 (≠ T329)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G106), D141 (≠ G128), N143 (≠ S130), N451 (= N438), L453 (= L440), Y454 (vs. gap)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
39% identity, 100% coverage: 3:471/471 of query aligns to 12:487/489 of 5fhzA
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E378), E470 (= E454)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), T160 (≠ N144), W162 (= W146), K186 (= K170), E189 (≠ Q173), G219 (= G203), G223 (= G207), F237 (= F221), G239 (= G223), S240 (= S224), T241 (= T225), V243 (≠ A227), G264 (= G247), Q343 (= Q326), E393 (= E378)
- binding retinoic acid: G118 (= G106), R121 (≠ T109), F164 (≠ Y148), M168 (≠ Q152), W171 (≠ G155), C295 (≠ T278), C296 (= C279), L453 (= L440)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
39% identity, 100% coverage: 3:471/471 of query aligns to 30:505/512 of P47895
- R89 (≠ S59) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K170) binding
- E207 (≠ Q173) binding
- GSTEVG 257:262 (≠ GSTGAG 223:228) binding
- Q361 (= Q326) binding
- E411 (= E378) binding
- A493 (≠ G459) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
39% identity, 100% coverage: 3:471/471 of query aligns to 11:486/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I143), T159 (≠ N144), P160 (= P145), W161 (= W146), K185 (= K170), E188 (≠ Q173), G218 (= G203), G222 (= G207), F236 (= F221), S239 (= S224), V242 (≠ A227)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
40% identity, 99% coverage: 7:471/471 of query aligns to 16:488/497 of 8skfA
- binding calcium ion: T33 (≠ V24), I34 (= I25), D100 (≠ E91), V187 (≠ E174)
- binding nicotinamide-adenine-dinucleotide: I156 (= I143), G157 (≠ N144), A158 (≠ P145), W159 (= W146), K183 (= K170), E186 (≠ Q173), G216 (= G203), G220 (= G207), T235 (= T222), G236 (= G223), G237 (≠ S224), S240 (≠ A227), K243 (≠ R230), E259 (= E245), C293 (= C279), F396 (= F380)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
40% identity, 99% coverage: 7:471/471 of query aligns to 7:479/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
40% identity, 99% coverage: 7:471/471 of query aligns to 7:479/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
40% identity, 99% coverage: 7:471/471 of query aligns to 7:479/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
40% identity, 99% coverage: 7:471/471 of query aligns to 7:479/488 of 8vqwC
- binding coenzyme a: I147 (= I143), W150 (= W146), K174 (= K170), S176 (= S172), E177 (≠ Q173), G207 (= G203), G211 (= G207), F225 (= F221), G227 (= G223), G228 (≠ S224), S231 (≠ A227), H331 (≠ Q326), F387 (= F380)
Query Sequence
>AO353_24855 FitnessBrowser__pseudo3_N2E3:AO353_24855
MHNYTALFIDGRWQTPSGQGIAEVINPATEEVAGSVPLGDERDVENAVAAARRAFGPWSR
TPSSVRAGYIRALAEQLRARADEMAALITAELGMPVQWCRSVQVDGPITGLEQYVELASL
MDEVREVGNSLVIREPVGVCAFINPWNYPLHQLIGKLAPALAAGCTVVVKPSQETPLHAF
LLAQMIEAIGLPAGVFNLVSGPGSKVGEALAKHPDVDMVSFTGSTGAGVRVAQAAAPSVK
RVCLELGGKSPLLIAEDADLAAAVRYGVQDVMINSGQTCTALTRMLLPASRYAEVVELAL
AETLSLRMGDPLDPQSFLGPMCSAAQRRTVRDYIQVGQQEGARLVCGGDTAQAFERGYYV
SPTLFADVDNRMRIAQEEIFGPVLCLIPYTDEAQAIQIANDSPFGLSSGVWAGSPDRALQ
LARQLRAGQCFLNGAAFNYLAPFGGYKQSGNGREWGEEGLNEFVEVKAIQV
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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