SitesBLAST
Comparing WP_018125680.1 NCBI__GCF_000375485.1:WP_018125680.1 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)
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)
60% identity, 99% coverage: 2:489/491 of query aligns to 16:503/505 of 4neaA
- active site: N166 (= N152), K189 (= K175), E264 (= E250), C298 (= C284), E399 (= E385), E476 (= E462)
- binding nicotinamide-adenine-dinucleotide: P164 (= P150), K189 (= K175), E192 (= E178), G222 (= G208), G226 (= G212), G242 (= G228), G243 (= G229), T246 (= T232), H249 (≠ T235), I250 (= I236), C298 (= C284), E399 (= E385), F401 (= F387)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
48% identity, 97% coverage: 5:480/491 of query aligns to 18:489/491 of 5gtlA
- active site: N165 (= N152), K188 (= K175), E263 (= E250), C297 (= C284), E394 (= E385), E471 (= E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I148), P163 (= P150), K188 (= K175), A190 (≠ S177), E191 (= E178), Q192 (≠ I179), G221 (= G208), G225 (= G212), G241 (= G228), S242 (≠ G229), T245 (= T232), L264 (= L251), C297 (= C284), E394 (= E385), F396 (= F387)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
48% identity, 97% coverage: 5:480/491 of query aligns to 18:489/491 of 5gtkA
- active site: N165 (= N152), K188 (= K175), E263 (= E250), C297 (= C284), E394 (= E385), E471 (= E462)
- binding nicotinamide-adenine-dinucleotide: I161 (= I148), I162 (≠ S149), P163 (= P150), W164 (= W151), K188 (= K175), E191 (= E178), G221 (= G208), G225 (= G212), A226 (= A213), F239 (= F226), G241 (= G228), S242 (≠ G229), T245 (= T232), Y248 (≠ T235), L264 (= L251), C297 (= C284), Q344 (≠ H331), R347 (≠ K334), E394 (= E385), F396 (= F387)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
46% identity, 98% coverage: 2:480/491 of query aligns to 2:478/489 of 4o6rA
- active site: N150 (= N152), K173 (= K175), E248 (= E250), C282 (= C284), E383 (= E385), E460 (= E462)
- binding adenosine monophosphate: I146 (= I148), V147 (≠ S149), K173 (= K175), G206 (= G208), G210 (= G212), Q211 (≠ A213), F224 (= F226), G226 (= G228), S227 (≠ G229), T230 (= T232), R233 (≠ T235)
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)
42% identity, 99% coverage: 4:489/491 of query aligns to 8:494/497 of P17202
- I28 (≠ L24) binding K(+)
- D96 (= D92) binding K(+)
- SPW 156:158 (= SPW 149:151) binding NAD(+)
- Y160 (= Y153) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 175:178) binding NAD(+)
- L186 (≠ I179) binding K(+)
- SSAT 236:239 (≠ GIET 229:232) binding NAD(+)
- V251 (= V244) binding in other chain
- L258 (= L251) binding NAD(+)
- W285 (≠ F278) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding NAD(+)
- A441 (≠ T436) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ Y445) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (= W451) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K455) binding K(+)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 5l13A
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ Y153), M168 (≠ Q157), W171 (= W160), F290 (= F278), C295 (≠ I283), C296 (= C284), C297 (≠ S285), D451 (≠ N443), F453 (≠ Y445)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 4kwgA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ Y153), M168 (≠ Q157), C295 (≠ I283), C296 (= C284), C297 (≠ S285), D451 (≠ N443), F453 (≠ Y445)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 4kwfA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ Y153), M168 (≠ Q157), W171 (= W160), E262 (= E250), C295 (≠ I283), C296 (= C284), C297 (≠ S285), D451 (≠ N443), F453 (≠ Y445), F459 (≠ W451)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 3sz9A
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ Y153), C295 (≠ I283), C296 (= C284), D451 (≠ N443), F453 (≠ Y445), F459 (≠ W451)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 3injA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ D106), F164 (≠ Y153), L167 (= L156), F286 (≠ N274), F290 (= F278), D451 (≠ N443), F453 (≠ Y445)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 2vleA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding daidzin: M118 (≠ D106), F164 (≠ Y153), M168 (≠ Q157), W171 (= W160), F286 (≠ N274), F290 (= F278), C295 (≠ I283), C296 (= C284), D451 (≠ N443), V452 (= V444), F453 (≠ Y445)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 1o01B
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding (2e)-but-2-enal: C296 (= C284), C297 (≠ S285), F453 (≠ Y445)
- binding nicotinamide-adenine-dinucleotide: I159 (= I148), I160 (≠ S149), P161 (= P150), W162 (= W151), K186 (= K175), E189 (= E178), G219 (= G208), G223 (= G212), A224 (= A213), F237 (= F226), G239 (= G228), S240 (≠ G229), I243 (≠ T232), L263 (= L251), G264 (= G252), C296 (= C284), Q343 (≠ H331), E393 (= E385), F395 (= F387)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 1cw3A
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E385), E470 (= E462)
- binding magnesium ion: V34 (≠ L24), D103 (= D92), Q190 (≠ I179)
- binding nicotinamide-adenine-dinucleotide: I159 (= I148), I160 (≠ S149), P161 (= P150), W162 (= W151), K186 (= K175), G219 (= G208), G223 (= G212), A224 (= A213), F237 (= F226), G239 (= G228), S240 (≠ G229), I243 (≠ T232), L263 (= L251), G264 (= G252), C296 (= C284), Q343 (≠ H331), K346 (= K334), E393 (= E385), F395 (= F387)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 16:487/496 of 4fr8C
- active site: N165 (= N152), K188 (= K175), Q264 (≠ E250), C298 (= C284), E395 (= E385), E472 (= E462)
- binding nicotinamide-adenine-dinucleotide: I161 (= I148), I162 (≠ S149), W164 (= W151), K188 (= K175), G221 (= G208), G225 (= G212), A226 (= A213), F239 (= F226), G241 (= G228), S242 (≠ G229), I245 (≠ T232), Q345 (≠ H331), E395 (= E385), F397 (= F387)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 13:484/493 of 4fr8A
- active site: N162 (= N152), K185 (= K175), Q261 (≠ E250), C295 (= C284), E392 (= E385), E469 (= E462)
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ S149), W161 (= W151), K185 (= K175), G218 (= G208), G222 (= G212), A223 (= A213), F236 (= F226), G238 (= G228), S239 (≠ G229), I242 (≠ T232), Q342 (≠ H331), K345 (= K334), E392 (= E385), F394 (= F387)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ Y153), L166 (= L156), W170 (= W160), F289 (= F278), S294 (≠ I283), C295 (= C284), D450 (≠ N443), F452 (≠ Y445)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
48% identity, 97% coverage: 1:477/491 of query aligns to 37:511/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
43% identity, 99% coverage: 3:489/491 of query aligns to 9:499/505 of O24174
- N164 (= N152) 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 (= W160) 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.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
42% identity, 99% coverage: 4:489/491 of query aligns to 6:492/495 of 4v37A
- active site: N157 (= N152), K180 (= K175), E255 (= E250), A289 (≠ C284), E388 (= E385), E465 (= E462)
- binding 3-aminopropan-1-ol: C448 (≠ Y445), W454 (= W451)
- binding nicotinamide-adenine-dinucleotide: I153 (= I148), S154 (= S149), P155 (= P150), W156 (= W151), N157 (= N152), M162 (≠ Q157), K180 (= K175), S182 (= S177), E183 (= E178), G213 (= G208), G217 (= G212), A218 (= A213), T232 (= T227), G233 (= G228), S234 (≠ G229), T237 (= T232), E255 (= E250), L256 (= L251), A289 (≠ C284), E388 (= E385), F390 (= F387)
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
48% identity, 97% coverage: 4:477/491 of query aligns to 14:485/494 of 1nzwA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), S296 (≠ C284), E393 (= E385), E470 (= E462)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I148), I160 (≠ S149), P161 (= P150), K186 (= K175), E189 (= E178), G219 (= G208), P220 (≠ A209), G223 (= G212), A224 (= A213), F237 (= F226), G239 (= G228), S240 (≠ G229), I243 (≠ T232), E262 (= E250), G264 (= G252), S296 (≠ C284), Q343 (≠ H331), E393 (= E385), F395 (= F387)
7radA Crystal structure analysis of aldh1b1
46% identity, 96% coverage: 5:477/491 of query aligns to 14:484/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ S149), P160 (= P150), W161 (= W151), N162 (= N152), M167 (≠ Q157), K185 (= K175), E188 (= E178), G218 (= G208), G222 (= G212), A223 (= A213), T237 (= T227), G238 (= G228), S239 (≠ G229), V242 (≠ T232), E261 (= E250), L262 (= L251), C295 (= C284), E392 (= E385), F394 (= F387)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ W102), E117 (≠ D106), F163 (≠ Y153), E285 (≠ N274), F289 (= F278), N450 (= N443), V452 (≠ Y445)
Query Sequence
>WP_018125680.1 NCBI__GCF_000375485.1:WP_018125680.1
MIRKKMYIDGEWVAADSGKEREILNPFDSSVIASVPEAGRGETRRAIAAARRAFDEGGWP
QTPAAERARLVFKLAELIERDHEELARLESLDTGKTVEESRWDMDDIAGIFRYFAGLADK
DGGEVIESPVPDTTSYVMREPVGVCGQISPWNYPLLQASWKMAPALAAGCTVVMKPSEIT
PLTTIKVTELAEEAGFPKGVVNTVLGPGAEVGAELSESHDVDLISFTGGIETGKTIMRAA
TGNVKKVALELGGKNPNIIFDDADFDLAVDYALNGVFFHAGQICSAGARILVQEGIHDRF
VEELRKRMERIKLGNGFDDDTQMGPLTSAEHLAKVEAYGEIGKKEGAKLLLGGCRPDDEA
LKDGYFYMPTLFSDCENDMRIVQEETFGPIITIEKFSTEEEAVTRANSTVYGLSAGFWTN
DPNRIERVSKALRFGTVWINDFNVYFVQAPWGGYKQSGLGRELGRMGLEEYTEVKHVYRN
HATKALNWFGA
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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