SitesBLAST
Comparing Pf1N1B4_2132 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2132 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
90% identity, 100% coverage: 3:497/497 of query aligns to 1:495/495 of 5iuwA
- active site: N166 (= N168), K189 (= K191), E265 (= E267), C300 (= C302), E399 (= E401), D476 (= D478)
- binding 1h-indol-3-ylacetic acid: F167 (= F169), M170 (= M172), C300 (= C302), D457 (= D459), F465 (= F467)
- binding nicotinamide-adenine-dinucleotide: I162 (= I164), V163 (= V165), P164 (= P166), W165 (= W167), N166 (= N168), K189 (= K191), G222 (= G224), G226 (= G228), K227 (= K229), F240 (= F242), T241 (= T243), G242 (= G244), S243 (= S245), I246 (= I248), Y253 (= Y255), E265 (= E267), A266 (= A268), C300 (= C302), E399 (= E401), F401 (= F403)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
90% identity, 100% coverage: 3:497/497 of query aligns to 1:495/495 of 5iuvA
- active site: N166 (= N168), K189 (= K191), E265 (= E267), C300 (= C302), E399 (= E401), D476 (= D478)
- binding nicotinamide-adenine-dinucleotide: I162 (= I164), V163 (= V165), P164 (= P166), W165 (= W167), N166 (= N168), K189 (= K191), S191 (= S193), G222 (= G224), G226 (= G228), K227 (= K229), F240 (= F242), T241 (= T243), G242 (= G244), S243 (= S245), I246 (= I248), Y253 (= Y255), E265 (= E267), A266 (= A268), C300 (= C302), E399 (= E401), F401 (= F403)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
90% identity, 100% coverage: 3:497/497 of query aligns to 1:495/495 of 7jsoA
- active site: N166 (= N168), E265 (= E267), A300 (≠ C302), D476 (= D478)
- binding 1h-indol-3-ylacetic acid: F167 (= F169), W174 (= W176), V299 (= V301), A300 (≠ C302), T301 (= T303), D457 (= D459), F465 (= F467)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I164), V163 (= V165), P164 (= P166), W165 (= W167), K189 (= K191), E192 (= E194), G222 (= G224), G226 (= G228), K227 (= K229), F240 (= F242), G242 (= G244), S243 (= S245), I246 (= I248), A266 (= A268), G267 (= G269), A300 (≠ C302), E399 (= E401), F401 (= F403)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
46% identity, 96% coverage: 21:497/497 of query aligns to 12:488/494 of 4pz2B
- active site: N159 (= N168), K182 (= K191), E258 (= E267), C292 (= C302), E392 (= E401), D469 (= D478)
- binding nicotinamide-adenine-dinucleotide: I155 (= I164), I156 (≠ V165), P157 (= P166), W158 (= W167), N159 (= N168), M164 (= M173), K182 (= K191), A184 (≠ S193), E185 (= E194), G215 (= G224), G219 (= G228), F233 (= F242), T234 (= T243), G235 (= G244), S236 (= S245), V239 (≠ I248), E258 (= E267), L259 (≠ A268), C292 (= C302), E392 (= E401), F394 (= F403)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
45% identity, 99% coverage: 4:495/497 of query aligns to 5:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I164), L166 (≠ V165), P167 (= P166), W168 (= W167), K192 (= K191), G225 (= G224), G229 (= G228), F243 (= F242), G245 (= G244), S246 (= S245), T249 (≠ I248), L252 (≠ Q251), F253 (≠ L252), Y256 (= Y255), C269 (≠ A268), G270 (= G269), C303 (= C302), H350 (≠ Q349), K353 (≠ T352), F400 (= F403)
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)
43% identity, 96% coverage: 21:497/497 of query aligns to 39:513/518 of Q63639
7radA Crystal structure analysis of aldh1b1
45% identity, 96% coverage: 23:497/497 of query aligns to 16:488/493 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 (≠ K229), T237 (= T243), G238 (= G244), S239 (= S245), V242 (≠ I248), E261 (= E267), L262 (≠ A268), C295 (= C302), E392 (= E401), F394 (= F403)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ I119), E117 (≠ G123), F163 (= F169), E285 (≠ G292), F289 (= F296), N450 (≠ D459), V452 (≠ G461)
7mjdA Crystal structure analysis of aldh1b1
45% identity, 96% coverage: 23:497/497 of query aligns to 16:488/493 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 (≠ I248), E261 (= E267), L262 (≠ A268), C295 (= C302), E392 (= E401), F394 (= F403)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ G123), E285 (≠ G292), F289 (= F296), N450 (≠ D459), V452 (≠ G461)
7mjcA Crystal structure analysis of aldh1b1
45% identity, 96% coverage: 23:497/497 of query aligns to 16:488/493 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 (≠ I248), E261 (= E267), L262 (≠ A268), C295 (= C302), E392 (= E401), F394 (= F403)
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: 21:497/497 of query aligns to 13:487/492 of 6b5hA
- active site: N161 (= N168), E260 (= E267), C294 (= C302), E468 (≠ D478)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ I119), G116 (= G123), F162 (= F169), W169 (= W176), Q284 (≠ G292), F288 (= F296), T295 (= T303), N449 (≠ D459), L451 (≠ G461), N452 (≠ D462), F457 (= F467)
- binding nicotinamide-adenine-dinucleotide: I157 (= I164), I158 (≠ V165), W160 (= W167), N161 (= N168), K184 (= K191), G217 (= G224), G221 (= G228), F235 (= F242), T236 (= T243), G237 (= G244), S238 (= S245), V241 (≠ I248), E260 (= E267), L261 (≠ A268), C294 (= C302), F393 (= F403)
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: 21:497/497 of query aligns to 13:487/492 of 6b5gA
- active site: N161 (= N168), E260 (= E267), C294 (= C302), E468 (≠ D478)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F169), L165 (≠ M172), W169 (= W176), F288 (= F296), C293 (≠ V301), C294 (= C302), T295 (= T303), N449 (≠ D459), L451 (≠ G461)
- binding nicotinamide-adenine-dinucleotide: I157 (= I164), I158 (≠ V165), P159 (= P166), W160 (= W167), N161 (= N168), M166 (= M173), K184 (= K191), E187 (= E194), G217 (= G224), G221 (= G228), F235 (= F242), T236 (= T243), G237 (= G244), S238 (= S245), V241 (≠ I248), E260 (= E267), L261 (≠ A268), C294 (= C302), E391 (= E401), F393 (= F403)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
42% identity, 96% coverage: 21:497/497 of query aligns to 13:487/492 of 6aljA
- active site: N161 (= N168), E260 (= E267), C294 (= C302), E468 (≠ D478)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G123), F162 (= F169), L165 (≠ M172), M166 (= M173), W169 (= W176), E260 (= E267), C293 (≠ V301), C294 (= C302), L451 (≠ G461), N452 (≠ D462), A453 (≠ M463)
- binding nicotinamide-adenine-dinucleotide: I157 (= I164), I158 (≠ V165), P159 (= P166), W160 (= W167), N161 (= N168), K184 (= K191), E187 (= E194), G217 (= G224), G221 (= G228), F235 (= F242), G237 (= G244), S238 (= S245), V241 (≠ I248), Q341 (= Q349), K344 (≠ T352), E391 (= E401), F393 (= F403)
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: 21:497/497 of query aligns to 39:513/518 of O94788
- E50 (≠ V32) to G: in dbSNP:rs34266719
- A110 (= A91) to V: in dbSNP:rs35365164
- Q182 (≠ A163) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 165:167) binding
- KPAE 210:213 (≠ KPSE 191:194) binding
- STE 264:266 (≠ STK 245:247) binding
- C320 (= C302) active site, Nucleophile
- R347 (≠ W329) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K330) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ QQMNT 348:352) binding
- A383 (= A365) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E401) binding
- E436 (≠ Q420) to K: in dbSNP:rs34744827
- S461 (≠ A445) to Y: in DIH4; decreased retinoic acid biosynthetic process
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
45% identity, 96% coverage: 23:497/497 of query aligns to 43:515/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
5l13A Structure of aldh2 in complex with 2p3 (see paper)
44% identity, 96% coverage: 23:497/497 of query aligns to 17:489/494 of 5l13A
- active site: N163 (= N168), K186 (= K191), E262 (= E267), C296 (= C302), E393 (= E401), E470 (≠ D478)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F169), M168 (= M173), W171 (= W176), F290 (= F296), C295 (≠ V301), C296 (= C302), C297 (≠ T303), D451 (= D459), F453 (≠ G461)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
44% identity, 96% coverage: 23:497/497 of query aligns to 17:489/494 of 4kwgA
- active site: N163 (= N168), K186 (= K191), E262 (= E267), C296 (= C302), E393 (= E401), E470 (≠ D478)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F169), M168 (= M173), C295 (≠ V301), C296 (= C302), C297 (≠ T303), D451 (= D459), F453 (≠ G461)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
44% identity, 96% coverage: 23:497/497 of query aligns to 17:489/494 of 4kwfA
- active site: N163 (= N168), K186 (= K191), E262 (= E267), C296 (= C302), E393 (= E401), E470 (≠ D478)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F169), M168 (= M173), W171 (= W176), E262 (= E267), C295 (≠ V301), C296 (= C302), C297 (≠ T303), D451 (= D459), F453 (≠ G461), F459 (= F467)
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)
44% identity, 96% coverage: 23:497/497 of query aligns to 17:489/494 of 3sz9A
- active site: N163 (= N168), K186 (= K191), E262 (= E267), C296 (= C302), E393 (= E401), E470 (≠ D478)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F169), C295 (≠ V301), C296 (= C302), D451 (= D459), F453 (≠ G461), F459 (= F467)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
44% identity, 96% coverage: 23:497/497 of query aligns to 17:489/494 of 3injA
- active site: N163 (= N168), K186 (= K191), E262 (= E267), C296 (= C302), E393 (= E401), E470 (≠ D478)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ G123), F164 (= F169), L167 (≠ M172), F286 (≠ G292), F290 (= F296), D451 (= D459), F453 (≠ G461)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
44% identity, 96% coverage: 23:497/497 of query aligns to 17:489/494 of 2vleA
- active site: N163 (= N168), K186 (= K191), E262 (= E267), C296 (= C302), E393 (= E401), E470 (≠ D478)
- binding daidzin: M118 (≠ G123), F164 (= F169), M168 (= M173), W171 (= W176), F286 (≠ G292), F290 (= F296), C295 (≠ V301), C296 (= C302), D451 (= D459), V452 (≠ G460), F453 (≠ G461)
Query Sequence
>Pf1N1B4_2132 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2132
MTTLTRADWEQRARDLKIEGRAYINGEYTDAVSGETFECISPVDGRLLGKIASCDAADAQ
RAVDNARATFNSGAWSRLAPTKRKATMIRFAGLLKQHAEELALLETLDMGKPISDSLYID
VPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGP
ALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVLNVLPGYGHTVGKALALHNDVDTL
VFTGSTKIAKQLLIYSGESNMKRVWLEAGGKSPNIVFADAPDLQAAAEAAAGAIAFNQGE
VCTAGSRLLVERSIKDKFLPLVIEALKTWKPGNPLDPATNVGALVDTQQMNTVLSYIESG
HTDGAKLVAGGKRILQETGGTYVEPTIFDGVSNAMKIAQEEIFGPVLSVITFDSAEEAIQ
IANDTPYGLAAAVWTADISKAHLTAKALRAGSVWVNQYDGGDMTAPFGGFKQSGNGRDKS
LHAFDKYTELKATWIKL
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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