SitesBLAST
Comparing PP_3151 FitnessBrowser__Putida:PP_3151 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)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
65% identity, 98% coverage: 8:460/461 of query aligns to 4:458/459 of 3efvA
- active site: N134 (= N136), E231 (= E233), C265 (= C267), E439 (= E441)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ V132), M131 (= M133), P132 (= P134), W133 (= W135), N134 (= N136), Q139 (= Q141), R142 (= R144), K157 (= K159), A159 (= A161), N190 (≠ P192), V193 (= V195), T208 (= T210), G209 (= G211), S210 (= S212), A213 (= A215), E231 (= E233), L232 (= L234), G233 (= G235), C265 (= C267), E362 (= E364), F364 (= F366), F428 (= F430)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
43% identity, 97% coverage: 12:458/461 of query aligns to 4:452/453 of 4itbA
- active site: N130 (= N136), K153 (= K159), E227 (= E233), C261 (= C267), E358 (= E364), E435 (= E441)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (= V132), M127 (= M133), P128 (= P134), W129 (= W135), N130 (= N136), K153 (= K159), A155 (= A161), S156 (≠ P162), A186 (≠ P192), V189 (= V195), G205 (= G211), S206 (= S212), A209 (= A215), S212 (≠ A218), L228 (= L234), C261 (= C267), E358 (= E364), F360 (= F366)
- binding 4-oxobutanoic acid: E227 (= E233), C261 (= C267), S418 (= S424)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
43% identity, 97% coverage: 12:458/461 of query aligns to 4:452/453 of 3vz3A
- active site: N130 (= N136), K153 (= K159), E227 (= E233), A261 (≠ C267), E358 (= E364), E435 (= E441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (= V132), M127 (= M133), W129 (= W135), N130 (= N136), Q135 (= Q141), R138 (= R144), K153 (= K159), A155 (= A161), S156 (≠ P162), A186 (≠ P192), V189 (= V195), T204 (= T210), G205 (= G211), S206 (= S212), A209 (= A215), E227 (= E233), L228 (= L234), G229 (= G235), A261 (≠ C267), F360 (= F366)
- binding 4-oxobutanoic acid: F131 (= F137), W134 (= W140), S260 (≠ V266), A261 (≠ C267), I262 (≠ A268), S418 (= S424)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
36% identity, 96% coverage: 15:458/461 of query aligns to 7:453/455 of 4ywuA
- active site: N131 (= N136), K154 (= K159), E228 (= E233), C262 (= C267), E359 (= E364), E436 (= E441)
- binding 4-oxobutanoic acid: N131 (= N136), Q136 (= Q141), R139 (= R144), E228 (= E233), V261 (= V266), C262 (= C267), F425 (= F430)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
36% identity, 96% coverage: 15:458/461 of query aligns to 7:453/455 of 4ohtA
- active site: N131 (= N136), K154 (= K159), E228 (= E233), C262 (= C267), E359 (= E364), E436 (= E441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (= V132), E128 (≠ M133), P129 (= P134), W130 (= W135), K154 (= K159), H155 (= H160), A156 (= A161), S157 (≠ P162), Y187 (≠ P192), S207 (= S212), I214 (= I219)
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
37% identity, 96% coverage: 16:456/461 of query aligns to 46:493/505 of 3u4jA
Sites not aligning to the query:
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
34% identity, 95% coverage: 14:450/461 of query aligns to 32:472/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
34% identity, 95% coverage: 14:450/461 of query aligns to 31:471/481 of 3jz4A
- active site: N156 (= N136), K179 (= K159), E254 (= E233), C288 (= C267), E385 (= E364), E462 (= E441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P134), W155 (= W135), K179 (= K159), A181 (= A161), S182 (≠ P162), A212 (≠ P192), G216 (≠ T196), G232 (= G211), S233 (= S212), I236 (≠ A215), C288 (= C267), K338 (≠ E317), E385 (= E364), F387 (= F366)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
33% identity, 97% coverage: 12:459/461 of query aligns to 31:486/494 of P49189
- C116 (≠ L97) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
33% identity, 97% coverage: 12:459/461 of query aligns to 30:485/493 of 6vr6D
- active site: N156 (= N136), E253 (= E233), C287 (= C267), E467 (= E441)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ V132), G153 (≠ M133), W155 (= W135), K179 (= K159), A212 (≠ P192), G215 (≠ V195), Q216 (≠ T196), F229 (≠ L209), G231 (= G211), S232 (= S212), T235 (≠ A215), I239 (= I219)
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)
31% identity, 96% coverage: 13:456/461 of query aligns to 28:482/497 of P17202
- I28 (≠ L13) binding
- D96 (≠ E79) binding
- SPW 156:158 (≠ MPW 133:135) binding
- Y160 (≠ F137) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R144) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAP 159:162) binding
- L186 (≠ N163) binding
- SSAT 236:239 (≠ SVRA 212:215) binding
- V251 (≠ L227) binding in other chain
- L258 (= L234) binding
- W285 (≠ Q261) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E364) binding
- A441 (≠ G415) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S424) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F430) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K434) binding
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
35% identity, 97% coverage: 14:458/461 of query aligns to 31:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ V132), T153 (≠ M133), P154 (= P134), K179 (= K159), A212 (≠ V190), K213 (≠ T191), F230 (≠ L209), T231 (= T210), G232 (= G211), S233 (= S212), V236 (≠ A215), W239 (≠ A218), G256 (= G235)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
31% identity, 96% coverage: 13:456/461 of query aligns to 26:480/495 of 4v37A
- active site: N157 (= N136), K180 (= K159), E255 (= E233), A289 (≠ C267), E388 (= E364), E465 (= E441)
- binding 3-aminopropan-1-ol: C448 (≠ S424), W454 (≠ F430)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V132), S154 (≠ M133), P155 (= P134), W156 (= W135), N157 (= N136), M162 (≠ Q141), K180 (= K159), S182 (≠ A161), E183 (≠ P162), G213 (≠ T191), G217 (≠ V195), A218 (≠ T196), T232 (= T210), G233 (= G211), S234 (= S212), T237 (≠ A215), E255 (= E233), L256 (= L234), A289 (≠ C267), E388 (= E364), F390 (= F366)
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)
35% identity, 96% coverage: 14:456/461 of query aligns to 59:509/518 of O94788
- A110 (= A62) to V: in dbSNP:rs35365164
- Q182 (≠ A131) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ MPW 133:135) binding
- KPAE 210:213 (≠ KHAP 159:162) binding
- STE 264:266 (≠ SVR 212:214) binding
- C320 (= C267) active site, Nucleophile
- R347 (≠ L294) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K295) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ DLRDE 313:317) binding
- A383 (= A330) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E364) binding
- E436 (= E383) to K: in dbSNP:rs34744827
- S461 (≠ T408) to Y: in DIH4; decreased retinoic acid biosynthetic process
Sites not aligning to the query:
- 50 E → G: in dbSNP:rs34266719
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
35% identity, 96% coverage: 14:456/461 of query aligns to 33:483/492 of 6b5hA
- active site: N161 (= N136), E260 (= E233), C294 (= C267), E468 (= E441)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G89), G116 (≠ K93), F162 (= F137), W169 (≠ R144), Q284 (≠ I257), F288 (≠ Q261), T295 (≠ A268), N449 (≠ C422), L451 (≠ S424), N452 (≠ D425), F457 (= F430)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V132), I158 (≠ M133), W160 (= W135), N161 (= N136), K184 (= K159), G217 (≠ T191), G221 (≠ V195), F235 (≠ L209), T236 (= T210), G237 (= G211), S238 (= S212), V241 (≠ A215), E260 (= E233), L261 (= L234), C294 (= C267), F393 (= F366)
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)
35% identity, 96% coverage: 14:456/461 of query aligns to 33:483/492 of 6b5gA
- active site: N161 (= N136), E260 (= E233), C294 (= C267), E468 (= E441)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F137), L165 (≠ W140), W169 (≠ R144), F288 (≠ Q261), C293 (≠ V266), C294 (= C267), T295 (≠ A268), N449 (≠ C422), L451 (≠ S424)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V132), I158 (≠ M133), P159 (= P134), W160 (= W135), N161 (= N136), M166 (≠ Q141), K184 (= K159), E187 (≠ P162), G217 (≠ T191), G221 (≠ V195), F235 (≠ L209), T236 (= T210), G237 (= G211), S238 (= S212), V241 (≠ A215), E260 (= E233), L261 (= L234), C294 (= C267), E391 (= E364), F393 (= F366)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
35% identity, 96% coverage: 14:456/461 of query aligns to 33:483/492 of 6aljA
- active site: N161 (= N136), E260 (= E233), C294 (= C267), E468 (= E441)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ K93), F162 (= F137), L165 (≠ W140), M166 (≠ Q141), W169 (≠ R144), E260 (= E233), C293 (≠ V266), C294 (= C267), L451 (≠ S424), N452 (≠ D425), A453 (≠ P426)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V132), I158 (≠ M133), P159 (= P134), W160 (= W135), N161 (= N136), K184 (= K159), E187 (≠ P162), G217 (≠ T191), G221 (≠ V195), F235 (≠ L209), G237 (= G211), S238 (= S212), V241 (≠ A215), Q341 (≠ L314), K344 (≠ E317), E391 (= E364), F393 (= F366)
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)
35% identity, 96% coverage: 14:456/461 of query aligns to 59:509/518 of Q63639
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 90% coverage: 46:459/461 of query aligns to 79:496/503 of O14293
- S248 (= S212) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
35% identity, 93% coverage: 13:441/461 of query aligns to 25:457/476 of 5x5uA
- active site: N151 (= N136), K174 (= K159), E249 (= E233), C283 (= C267), E380 (= E364), E457 (= E441)
- binding nicotinamide-adenine-dinucleotide: P149 (= P134), P207 (= P192), A208 (≠ D193), S211 (≠ T196), G227 (= G211), S228 (= S212), V231 (≠ A215), R329 (≠ D313), R330 (≠ L314), E380 (= E364), F382 (= F366)
Sites not aligning to the query:
Query Sequence
>PP_3151 FitnessBrowser__Putida:PP_3151
MSAISSLTHAISLDPYSGEQIGTYPFDTDAALEAALQRAKVGYRQWRQVSLGQRSEYLLA
LADTLEAKAEAFAHMISREIGKPIAQARGEVSKCVGLCRWYAEHGPAMLAAEPTQVEKAR
IEYRPLGPILAVMPWNFPVWQVLRGAVPAILAGNTYVLKHAPNVMGSAYLMAELFKDAGL
PEGVFEVLNVTPDGVTRAINDPRIAAVTLTGSVRAGMAIGAQAGAALKKCVLELGGSDPF
IVLADADLDAAVQAAVIGRYQNTGQVCAAAKRLIVEASIVDAFTHKFVEATRQLKVGNPL
EDDTYIGPMARYDLRDELDGQVQATLAEGATLLLGGNKVEGVANFYAPTVFANVTPDMTA
FKQELFGPVAAIITARDADHAVELANDSEFGLASTIYTADYALAERMTAALDTGGVFING
YCASDPRVAFGGVKKSGFGRELSHFGVREFTNAQTVWLDRN
Or try a new SitesBLAST search
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