SitesBLAST
Comparing Pf1N1B4_4355 Gamma-glutamyl-aminobutyraldehyde dehydrogenase (EC 1.2.1.-) 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)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
76% identity, 100% coverage: 2:496/496 of query aligns to 1:495/495 of 5iuwA
- active site: N166 (= N167), K189 (= K190), E265 (= E266), C300 (= C301), E399 (= E400), D476 (= D477)
- binding 1h-indol-3-ylacetic acid: F167 (= F168), M170 (≠ I171), C300 (= C301), D457 (= D458), F465 (= F466)
- binding nicotinamide-adenine-dinucleotide: I162 (= I163), V163 (= V164), P164 (= P165), W165 (= W166), N166 (= N167), K189 (= K190), G222 (= G223), G226 (= G227), K227 (= K228), F240 (= F241), T241 (= T242), G242 (= G243), S243 (= S244), I246 (= I247), Y253 (= Y254), E265 (= E266), A266 (= A267), C300 (= C301), E399 (= E400), F401 (= F402)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
76% identity, 100% coverage: 2:496/496 of query aligns to 1:495/495 of 5iuvA
- active site: N166 (= N167), K189 (= K190), E265 (= E266), C300 (= C301), E399 (= E400), D476 (= D477)
- binding nicotinamide-adenine-dinucleotide: I162 (= I163), V163 (= V164), P164 (= P165), W165 (= W166), N166 (= N167), K189 (= K190), S191 (= S192), G222 (= G223), G226 (= G227), K227 (= K228), F240 (= F241), T241 (= T242), G242 (= G243), S243 (= S244), I246 (= I247), Y253 (= Y254), E265 (= E266), A266 (= A267), C300 (= C301), E399 (= E400), F401 (= F402)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
75% identity, 100% coverage: 2:496/496 of query aligns to 1:495/495 of 7jsoA
- active site: N166 (= N167), E265 (= E266), A300 (≠ C301), D476 (= D477)
- binding 1h-indol-3-ylacetic acid: F167 (= F168), W174 (= W175), V299 (= V300), A300 (≠ C301), T301 (= T302), D457 (= D458), F465 (= F466)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I163), V163 (= V164), P164 (= P165), W165 (= W166), K189 (= K190), E192 (= E193), G222 (= G223), G226 (= G227), K227 (= K228), F240 (= F241), G242 (= G243), S243 (= S244), I246 (= I247), A266 (= A267), G267 (= G268), A300 (≠ C301), E399 (= E400), F401 (= F402)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
44% identity, 97% coverage: 15:496/496 of query aligns to 13:490/491 of 5gtlA
- active site: N165 (= N167), K188 (= K190), E263 (= E266), C297 (= C301), E394 (= E400), E471 (≠ D477)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I163), P163 (= P165), K188 (= K190), A190 (≠ S192), E191 (= E193), Q192 (≠ K194), G221 (= G223), G225 (= G227), G241 (= G243), S242 (= S244), T245 (≠ I247), L264 (≠ A267), C297 (= C301), E394 (= E400), F396 (= F402)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
44% identity, 97% coverage: 15:496/496 of query aligns to 13:490/491 of 5gtkA
- active site: N165 (= N167), K188 (= K190), E263 (= E266), C297 (= C301), E394 (= E400), E471 (≠ D477)
- binding nicotinamide-adenine-dinucleotide: I161 (= I163), I162 (≠ V164), P163 (= P165), W164 (= W166), K188 (= K190), E191 (= E193), G221 (= G223), G225 (= G227), A226 (≠ K228), F239 (= F241), G241 (= G243), S242 (= S244), T245 (≠ I247), Y248 (≠ Q250), L264 (≠ A267), C297 (= C301), Q344 (= Q348), R347 (≠ N351), E394 (= E400), F396 (= F402)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
45% identity, 98% coverage: 9:496/496 of query aligns to 2:480/486 of 4pxlA
- active site: N154 (= N167), K177 (= K190), E253 (= E266), C287 (= C301), E384 (= E400), D461 (= D477)
- binding nicotinamide-adenine-dinucleotide: I150 (= I163), V151 (= V164), P152 (= P165), W153 (= W166), K177 (= K190), E180 (= E193), G210 (= G223), G214 (= G227), A215 (≠ K228), F228 (= F241), G230 (= G243), S231 (= S244), V234 (≠ I247), E253 (= E266), G255 (= G268), C287 (= C301), Q334 (= Q348), K337 (≠ N351), E384 (= E400), F386 (= F402)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
46% identity, 99% coverage: 4:494/496 of query aligns to 6:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I163), L166 (≠ V164), P167 (= P165), W168 (= W166), K192 (= K190), G225 (= G223), G229 (= G227), F243 (= F241), G245 (= G243), S246 (= S244), T249 (≠ I247), L252 (≠ Q250), F253 (≠ L251), Y256 (= Y254), C269 (≠ A267), G270 (= G268), C303 (= C301), H350 (≠ Q348), K353 (≠ N351), F400 (= F402)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
45% identity, 98% coverage: 9:496/496 of query aligns to 7:488/494 of 4pz2B
- active site: N159 (= N167), K182 (= K190), E258 (= E266), C292 (= C301), E392 (= E400), D469 (= D477)
- binding nicotinamide-adenine-dinucleotide: I155 (= I163), I156 (≠ V164), P157 (= P165), W158 (= W166), N159 (= N167), M164 (= M172), K182 (= K190), A184 (≠ S192), E185 (= E193), G215 (= G223), G219 (= G227), F233 (= F241), T234 (= T242), G235 (= G243), S236 (= S244), V239 (≠ I247), E258 (= E266), L259 (≠ A267), C292 (= C301), E392 (= E400), F394 (= F402)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 96% coverage: 20:496/496 of query aligns to 21:495/501 of Q56YU0
- G152 (= G150) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A417) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
43% identity, 97% coverage: 17:496/496 of query aligns to 1:477/487 of 4go4A
- active site: N149 (= N167), K172 (= K190), E247 (= E266), C281 (= C301), E381 (= E400), E458 (≠ D477)
- binding nicotinamide-adenine-dinucleotide: I145 (= I163), V146 (= V164), W148 (= W166), N149 (= N167), F154 (≠ M172), K172 (= K190), G205 (= G223), G209 (= G227), Q210 (≠ K228), F223 (= F241), T224 (= T242), G225 (= G243), S226 (= S244), T229 (≠ I247), E247 (= E266), G249 (= G268), C281 (= C301), E381 (= E400), F383 (= F402)
7radA Crystal structure analysis of aldh1b1
43% identity, 96% coverage: 22:496/496 of query aligns to 16:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I163), I159 (≠ V164), P160 (= P165), W161 (= W166), N162 (= N167), M167 (= M172), K185 (= K190), E188 (= E193), G218 (= G223), G222 (= G227), A223 (≠ K228), T237 (= T242), G238 (= G243), S239 (= S244), V242 (≠ I247), E261 (= E266), L262 (≠ A267), C295 (= C301), E392 (= E400), F394 (= F402)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ I118), E117 (≠ A122), F163 (= F168), E285 (≠ S291), F289 (= F295), N450 (≠ D458), V452 (≠ G460)
7mjdA Crystal structure analysis of aldh1b1
43% identity, 96% coverage: 22:496/496 of query aligns to 16:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I163), I159 (≠ V164), P160 (= P165), W161 (= W166), N162 (= N167), M167 (= M172), K185 (= K190), E188 (= E193), G218 (= G223), G222 (= G227), F236 (= F241), T237 (= T242), G238 (= G243), S239 (= S244), V242 (≠ I247), E261 (= E266), L262 (≠ A267), C295 (= C301), E392 (= E400), F394 (= F402)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ A122), E285 (≠ S291), F289 (= F295), N450 (≠ D458), V452 (≠ G460)
7mjcA Crystal structure analysis of aldh1b1
43% identity, 96% coverage: 22:496/496 of query aligns to 16:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I163), I159 (≠ V164), P160 (= P165), W161 (= W166), N162 (= N167), K185 (= K190), E188 (= E193), G218 (= G223), G222 (= G227), T237 (= T242), G238 (= G243), S239 (= S244), V242 (≠ I247), E261 (= E266), L262 (≠ A267), C295 (= C301), E392 (= E400), F394 (= F402)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
42% identity, 96% coverage: 20:496/496 of query aligns to 39:513/518 of O94788
- E50 (≠ L31) to G: in dbSNP:rs34266719
- A110 (= A90) to V: in dbSNP:rs35365164
- Q182 (≠ A162) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 164:166) binding
- KPAE 210:213 (≠ KPSE 190:193) binding
- STE 264:266 (≠ STA 244:246) binding
- C320 (= C301) active site, Nucleophile
- R347 (≠ W328) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K329) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RQLDN 347:351) binding
- A383 (= A364) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E400) binding
- E436 (≠ Q419) to K: in dbSNP:rs34744827
- S461 (≠ A444) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
42% identity, 96% coverage: 20:496/496 of query aligns to 13:487/492 of 6b5hA
- active site: N161 (= N167), E260 (= E266), C294 (= C301), E468 (≠ D477)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ I118), G116 (≠ A122), F162 (= F168), W169 (= W175), Q284 (≠ S291), F288 (= F295), T295 (= T302), N449 (≠ D458), L451 (≠ G460), N452 (≠ D461), F457 (= F466)
- binding nicotinamide-adenine-dinucleotide: I157 (= I163), I158 (≠ V164), W160 (= W166), N161 (= N167), K184 (= K190), G217 (= G223), G221 (= G227), F235 (= F241), T236 (= T242), G237 (= G243), S238 (= S244), V241 (≠ I247), E260 (= E266), L261 (≠ A267), C294 (= C301), F393 (= F402)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
42% identity, 96% coverage: 20:496/496 of query aligns to 13:487/492 of 6b5gA
- active site: N161 (= N167), E260 (= E266), C294 (= C301), E468 (≠ D477)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F168), L165 (≠ I171), W169 (= W175), F288 (= F295), C293 (≠ V300), C294 (= C301), T295 (= T302), N449 (≠ D458), L451 (≠ G460)
- binding nicotinamide-adenine-dinucleotide: I157 (= I163), I158 (≠ V164), P159 (= P165), W160 (= W166), N161 (= N167), M166 (= M172), K184 (= K190), E187 (= E193), G217 (= G223), G221 (= G227), F235 (= F241), T236 (= T242), G237 (= G243), S238 (= S244), V241 (≠ I247), E260 (= E266), L261 (≠ A267), C294 (= C301), E391 (= E400), F393 (= F402)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
42% identity, 96% coverage: 20:496/496 of query aligns to 13:487/492 of 6aljA
- active site: N161 (= N167), E260 (= E266), C294 (= C301), E468 (≠ D477)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A122), F162 (= F168), L165 (≠ I171), M166 (= M172), W169 (= W175), E260 (= E266), C293 (≠ V300), C294 (= C301), L451 (≠ G460), N452 (≠ D461), A453 (≠ M462)
- binding nicotinamide-adenine-dinucleotide: I157 (= I163), I158 (≠ V164), P159 (= P165), W160 (= W166), N161 (= N167), K184 (= K190), E187 (= E193), G217 (= G223), G221 (= G227), F235 (= F241), G237 (= G243), S238 (= S244), V241 (≠ I247), Q341 (= Q348), K344 (≠ N351), E391 (= E400), F393 (= F402)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
42% identity, 96% coverage: 20:496/496 of query aligns to 39:513/518 of Q63639
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
42% identity, 98% coverage: 13:496/496 of query aligns to 34:515/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
5l13A Structure of aldh2 in complex with 2p3 (see paper)
43% identity, 96% coverage: 22:496/496 of query aligns to 17:489/494 of 5l13A
- active site: N163 (= N167), K186 (= K190), E262 (= E266), C296 (= C301), E393 (= E400), E470 (≠ D477)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F168), M168 (= M172), W171 (= W175), F290 (= F295), C295 (≠ V300), C296 (= C301), C297 (≠ T302), D451 (= D458), F453 (≠ G460)
Query Sequence
>Pf1N1B4_4355 Gamma-glutamyl-aminobutyraldehyde dehydrogenase (EC 1.2.1.-)
MTNTRSDWEQRFQSLTLEGRAFIDGQYCPALSGDTFECISPVDGRFLANIASTDEADANA
AVQVARRTFESGIWAKLPPAERKRVLIRFADLILQNQEELALLETLDMGKPISDSMSIDI
PATANAIRWSAEAIDKIYDEVAATPHDQLGLITREPAGVVAAIVPWNFPLIMASWKFAPA
LAAGNSFILKPSEKSPLTAIRIAQLALEAGIPKGVFNVLPGFGHTVGKALALHMDVDVLA
FTGSTAIAKQLLIYAGQSNMKRVWLEAGGKSPNVVFADAPDLRAAARAAVSAIAFNQGEV
CTAGSRLLVERSIREQFIPLLVEALQAWKPGHALDPETTVGAVVDQRQLDNVLRYIQVGK
DQGAQLIAGGNRTLADTGGLYVEPAIFDGVTNAMTIAREEIFGPVLSLITFDTAEEALQI
ANDSIFGLAAGVWTSNLSKAHTFARGLRAGSVWVNQYDGGDMTAPFGGFKQSGNGRDKSL
HAFDKYTELKATWIKL
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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