SitesBLAST
Comparing AO356_28685 AO356_28685 betaine-aldehyde dehydrogenase 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
50% identity, 99% coverage: 4:495/496 of query aligns to 3:490/491 of 5gtlA
- active site: N165 (= N168), K188 (= K191), E263 (= E266), C297 (= C300), E394 (= E399), E471 (= E476)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I164), P163 (= P166), K188 (= K191), A190 (= A193), E191 (= E194), Q192 (= Q195), G221 (= G224), G225 (= G228), G241 (= G244), S242 (= S245), T245 (≠ V248), L264 (= L267), C297 (= C300), E394 (= E399), F396 (= F401)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
50% identity, 99% coverage: 4:495/496 of query aligns to 3:490/491 of 5gtkA
- active site: N165 (= N168), K188 (= K191), E263 (= E266), C297 (= C300), E394 (= E399), E471 (= E476)
- binding nicotinamide-adenine-dinucleotide: I161 (= I164), I162 (≠ V165), P163 (= P166), W164 (= W167), K188 (= K191), E191 (= E194), G221 (= G224), G225 (= G228), A226 (= A229), F239 (= F242), G241 (= G244), S242 (= S245), T245 (≠ V248), Y248 (≠ L251), L264 (= L267), C297 (= C300), Q344 (= Q347), R347 (≠ T350), E394 (= E399), F396 (= F401)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 5l13A
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F169), M168 (= M173), W171 (= W176), F290 (≠ Y294), C295 (≠ V299), C296 (= C300), C297 (≠ T301), D451 (≠ N457), F453 (≠ V459)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 4kwgA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F169), M168 (= M173), C295 (≠ V299), C296 (= C300), C297 (≠ T301), D451 (≠ N457), F453 (≠ V459)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 4kwfA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F169), M168 (= M173), W171 (= W176), E262 (= E266), C295 (≠ V299), C296 (= C300), C297 (≠ T301), D451 (≠ N457), F453 (≠ V459), F459 (= F465)
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)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 3sz9A
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F169), C295 (≠ V299), C296 (= C300), D451 (≠ N457), F453 (≠ V459), F459 (= F465)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 3injA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ S119), F164 (= F169), L167 (≠ T172), F286 (≠ D290), F290 (≠ Y294), D451 (≠ N457), F453 (≠ V459)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 2vleA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding daidzin: M118 (≠ S119), F164 (= F169), M168 (= M173), W171 (= W176), F286 (≠ D290), F290 (≠ Y294), C295 (≠ V299), C296 (= C300), D451 (≠ N457), V452 (= V458), F453 (≠ V459)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 1o01B
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding (2e)-but-2-enal: C296 (= C300), C297 (≠ T301), F453 (≠ V459)
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (≠ V165), P161 (= P166), W162 (= W167), K186 (= K191), E189 (= E194), G219 (= G224), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), L263 (= L267), G264 (= G268), C296 (= C300), Q343 (= Q347), E393 (= E399), F395 (= F401)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 1cw3A
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding magnesium ion: V34 (≠ E38), D103 (≠ E105), Q190 (= Q195)
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (≠ V165), P161 (= P166), W162 (= W167), K186 (= K191), G219 (= G224), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), L263 (= L267), G264 (= G268), C296 (= C300), Q343 (= Q347), K346 (≠ T350), E393 (= E399), F395 (= F401)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 12:491/496 of 4fr8C
- active site: N165 (= N168), K188 (= K191), Q264 (≠ E266), C298 (= C300), E395 (= E399), E472 (= E476)
- binding nicotinamide-adenine-dinucleotide: I161 (= I164), I162 (≠ V165), W164 (= W167), K188 (= K191), G221 (= G224), G225 (= G228), A226 (= A229), F239 (= F242), G241 (= G244), S242 (= S245), I245 (≠ V248), Q345 (= Q347), E395 (= E399), F397 (= F401)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 9:488/493 of 4fr8A
- active site: N162 (= N168), K185 (= K191), Q261 (≠ E266), C295 (= C300), E392 (= E399), E469 (= E476)
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ V165), W161 (= W167), K185 (= K191), G218 (= G224), G222 (= G228), A223 (= A229), F236 (= F242), G238 (= G244), S239 (= S245), I242 (≠ V248), Q342 (= Q347), K345 (≠ T350), E392 (= E399), F394 (= F401)
- binding propane-1,2,3-triyl trinitrate: F163 (= F169), L166 (≠ T172), W170 (= W176), F289 (≠ Y294), S294 (≠ V299), C295 (= C300), D450 (≠ N457), F452 (≠ V459)
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
47% identity, 98% coverage: 11:495/496 of query aligns to 10:489/494 of 1nzwA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), S296 (≠ C300), E393 (= E399), E470 (= E476)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I164), I160 (≠ V165), P161 (= P166), K186 (= K191), E189 (= E194), G219 (= G224), P220 (≠ A225), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), E262 (= E266), G264 (= G268), S296 (≠ C300), Q343 (= Q347), E393 (= E399), F395 (= F401)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
48% identity, 96% coverage: 19:493/496 of query aligns to 41:513/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
2onmA Human mitochondrial aldehyde dehydrogenase asian variant, aldh2 2, Complexed with NAD+ (see paper)
47% identity, 96% coverage: 11:485/496 of query aligns to 10:479/494 of 2onmA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E399), E470 (= E476)
- binding adenosine-5'-diphosphate: E189 (= E194), G219 (= G224), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248)
7radA Crystal structure analysis of aldh1b1
47% identity, 96% coverage: 19:495/496 of query aligns to 14:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ V165), P160 (= P166), W161 (= W167), N162 (= N168), M167 (= M173), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), A223 (= A229), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), E261 (= E266), L262 (= L267), C295 (= C300), E392 (= E399), F394 (= F401)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ S119), F163 (= F169), E285 (≠ D290), F289 (≠ Y294), N450 (= N457), V452 (= V459)
7mjdA Crystal structure analysis of aldh1b1
47% identity, 96% coverage: 19:495/496 of query aligns to 14:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ V165), P160 (= P166), W161 (= W167), N162 (= N168), M167 (= M173), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), F236 (= F242), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), E261 (= E266), L262 (= L267), C295 (= C300), E392 (= E399), F394 (= F401)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ S119), E285 (≠ D290), F289 (≠ Y294), N450 (= N457), V452 (= V459)
7mjcA Crystal structure analysis of aldh1b1
47% identity, 96% coverage: 19:495/496 of query aligns to 14:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ V165), P160 (= P166), W161 (= W167), N162 (= N168), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), E261 (= E266), L262 (= L267), C295 (= C300), E392 (= E399), F394 (= F401)
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
44% identity, 97% coverage: 16:496/496 of query aligns to 19:497/501 of P00352
- N121 (≠ G115) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ VPWN 165:168) binding
- I177 (≠ V175) to F: in dbSNP:rs8187929
- KPAE 193:196 (= KPAE 191:194) binding
- GP 226:227 (≠ GA 224:225) binding
- GS 246:247 (= GS 244:245) binding
- E269 (= E266) active site, Proton acceptor
- ELG 269:271 (= ELG 266:268) binding
- C302 (≠ V299) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C300) active site, Nucleophile
- EQYDK 349:353 (≠ RQLGT 346:350) binding
- EIF 400:402 (= EIF 399:401) binding
- G458 (≠ N457) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
7um9A Human aldh1a1 with bound compound cm38 (see paper)
44% identity, 97% coverage: 16:496/496 of query aligns to 12:490/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (≠ V165), P161 (= P166), W162 (= W167), N163 (= N168), K186 (= K191), E189 (= E194), G219 (= G224), G223 (= G228), F237 (= F242), T238 (= T243), G239 (= G244), S240 (= S245), V243 (= V248), E262 (= E266), G264 (= G268), Q343 (= Q347), K346 (≠ T350), E393 (= E399), F395 (= F401)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (= W176), H286 (≠ D290), Y290 (= Y294), I297 (≠ T301), G451 (≠ N457)
Query Sequence
>AO356_28685 AO356_28685 betaine-aldehyde dehydrogenase
MNPIQLLPAVEKFLSQPGRLFIGGTWQDAANGRRFAVENPATEHTLAEVAEGGERDVDAA
VAAARAAFTGTWAQQSPAQRGLLLFRLAELLDQHREELAQLITLENGKPIGAARGEAASA
ANIIRYFAGWPTKIEGSTLPVSPSSGAPMLNYTLREPVGVCALIVPWNFPLTMCVWKLGP
VLATGCVAVLKPAEQTPLVAIRLVQLIEAAGFPAGVVNLLTGLGAQTGAPLAQHPDVDKI
AFTGSTQVGRLIAQAATGNMKKVSLELGGKSPNIILPDADIVRAAKGAADGIFYNQGQVC
TAGSRLYVHASVLDQVLEELQRHAAAHVLGPGLDPASSMGPLVSARQLGTVRGYLQRGQE
EGAELICGGDRPAHLERGHFIRPSVFLDRAERACVAREEIFGPVLTVMSWTEIDELVLRA
NDSPYGLAAGLWTRDLRSAHRVAAQLKAGSVWINCWNVVDPASPFGGYKQSGWGREMGKN
VIDAYTETKSVYVDLA
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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