SitesBLAST
Comparing 15646 FitnessBrowser__Keio:15646 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)
82% identity, 99% coverage: 6:462/462 of query aligns to 3:459/459 of 3efvA
- active site: N134 (= N137), E231 (= E234), C265 (= C268), E439 (= E442)
- binding nicotinamide-adenine-dinucleotide: I130 (= I133), M131 (= M134), P132 (= P135), W133 (= W136), N134 (= N137), Q139 (= Q142), R142 (= R145), K157 (= K160), A159 (= A162), N190 (= N193), V193 (= V196), T208 (= T211), G209 (= G212), S210 (= S213), A213 (= A216), E231 (= E234), L232 (= L235), G233 (= G236), C265 (= C268), E362 (= E365), F364 (= F367), F428 (= F431)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
43% identity, 97% coverage: 11:458/462 of query aligns to 4:451/453 of 4itbA
- active site: N130 (= N137), K153 (= K160), E227 (= E234), C261 (= C268), E358 (= E365), E435 (= E442)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (≠ I133), M127 (= M134), P128 (= P135), W129 (= W136), N130 (= N137), K153 (= K160), A155 (= A162), S156 (≠ P163), A186 (≠ N193), V189 (= V196), G205 (= G212), S206 (= S213), A209 (= A216), S212 (≠ A219), L228 (= L235), C261 (= C268), E358 (= E365), F360 (= F367)
- binding 4-oxobutanoic acid: E227 (= E234), C261 (= C268), S418 (= S425)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
42% identity, 97% coverage: 11:458/462 of query aligns to 4:451/453 of 3vz3A
- active site: N130 (= N137), K153 (= K160), E227 (= E234), A261 (≠ C268), E358 (= E365), E435 (= E442)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (≠ I133), M127 (= M134), W129 (= W136), N130 (= N137), Q135 (= Q142), R138 (= R145), K153 (= K160), A155 (= A162), S156 (≠ P163), A186 (≠ N193), V189 (= V196), T204 (= T211), G205 (= G212), S206 (= S213), A209 (= A216), E227 (= E234), L228 (= L235), G229 (= G236), A261 (≠ C268), F360 (= F367)
- binding 4-oxobutanoic acid: F131 (= F138), W134 (= W141), S260 (≠ V267), A261 (≠ C268), I262 (≠ A269), S418 (= S425)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
36% identity, 97% coverage: 11:458/462 of query aligns to 4:452/455 of 4ywuA
- active site: N131 (= N137), K154 (= K160), E228 (= E234), C262 (= C268), E359 (= E365), E436 (= E442)
- binding 4-oxobutanoic acid: N131 (= N137), Q136 (= Q142), R139 (= R145), E228 (= E234), V261 (= V267), C262 (= C268), F425 (= F431)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
36% identity, 97% coverage: 11:458/462 of query aligns to 4:452/455 of 4ohtA
- active site: N131 (= N137), K154 (= K160), E228 (= E234), C262 (= C268), E359 (= E365), E436 (= E442)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (≠ I133), E128 (≠ M134), P129 (= P135), W130 (= W136), K154 (= K160), H155 (= H161), A156 (= A162), S157 (≠ P163), Y187 (≠ N193), S207 (= S213), I214 (= I220)
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)
32% identity, 96% coverage: 13:455/462 of query aligns to 32:476/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
32% identity, 96% coverage: 13:455/462 of query aligns to 31:475/481 of 3jz4A
- active site: N156 (= N137), K179 (= K160), E254 (= E234), C288 (= C268), E385 (= E365), E462 (= E442)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P135), W155 (= W136), K179 (= K160), A181 (= A162), S182 (≠ P163), A212 (≠ N193), G216 (vs. gap), G232 (= G212), S233 (= S213), I236 (≠ A216), C288 (= C268), K338 (≠ E318), E385 (= E365), F387 (= F367)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
34% identity, 97% coverage: 12:458/462 of query aligns to 25:474/477 of 2opxA
- active site: N151 (= N137), K174 (= K160), E249 (= E234), C283 (= C268), E381 (= E365), A458 (≠ E442)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ K92), F152 (= F138), N284 (≠ A269), F312 (≠ M297), G313 (= G298), R318 (≠ E303), D320 (≠ N305), I321 (vs. gap), A322 (= A306), Y362 (= Y346), F440 (≠ A424), F440 (≠ A424), E441 (≠ S425)
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
34% identity, 97% coverage: 12:458/462 of query aligns to 25:474/477 of 2impA
- active site: N151 (= N137), K174 (= K160), E249 (= E234), C283 (= C268), E381 (= E365), A458 (≠ E442)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I133), L148 (≠ M134), P149 (= P135), W150 (= W136), K174 (= K160), E177 (≠ P163), F178 (≠ N164), G207 (≠ N193), G211 (≠ S197), Q212 (= Q198), S228 (= S213), A231 (= A216), K234 (≠ A219), R334 (≠ E318)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
34% identity, 97% coverage: 12:458/462 of query aligns to 25:474/477 of 2iluA
- active site: N151 (= N137), K174 (= K160), E249 (= E234), C283 (= C268), E381 (= E365), A458 (≠ E442)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I133), L148 (≠ M134), P149 (= P135), W150 (= W136), K174 (= K160), S176 (≠ A162), E177 (≠ P163), R206 (≠ D192), G207 (≠ N193), G211 (≠ S197), Q212 (= Q198), S228 (= S213), A231 (= A216), K234 (≠ A219), I235 (= I220), N328 (≠ R312), R334 (≠ E318), F383 (= F367)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 97% coverage: 12:458/462 of query aligns to 27:476/479 of P25553
- L150 (≠ M134) binding
- R161 (= R145) binding
- KPSE 176:179 (≠ KHAP 160:163) binding
- F180 (≠ N164) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (= Q198) binding
- S230 (= S213) binding
- E251 (= E234) binding
- N286 (≠ A269) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ E318) binding
- E443 (≠ S425) binding
- H449 (≠ F431) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
35% identity, 97% coverage: 12:457/462 of query aligns to 25:472/476 of 5x5uA
- active site: N151 (= N137), K174 (= K160), E249 (= E234), C283 (= C268), E380 (= E365), E457 (= E442)
- binding nicotinamide-adenine-dinucleotide: P149 (= P135), P207 (≠ N193), A208 (≠ D194), S211 (= S197), G227 (= G212), S228 (= S213), V231 (≠ A216), R329 (≠ D314), R330 (≠ L315), E380 (= E365), F382 (= F367)
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
35% identity, 97% coverage: 12:457/462 of query aligns to 25:472/476 of 5x5tA
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
33% identity, 97% coverage: 11:457/462 of query aligns to 25:478/489 of 4cazA
- active site: N152 (= N137), K175 (= K160), E251 (= E234), C285 (= C268), E386 (= E365), E463 (= E442)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I133), G149 (≠ M134), W151 (= W136), N152 (= N137), K175 (= K160), E178 (≠ P163), G208 (≠ N193), G212 (≠ S197), F226 (≠ V210), T227 (= T211), G228 (= G212), G229 (≠ S213), T232 (≠ A216), V236 (≠ I220), E251 (= E234), L252 (= L235), C285 (= C268), E386 (= E365), F388 (= F367)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
33% identity, 97% coverage: 11:457/462 of query aligns to 25:478/489 of 2woxA
- active site: N152 (= N137), K175 (= K160), E251 (= E234), C285 (= C268), E386 (= E365), E463 (= E442)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I133), G149 (≠ M134), W151 (= W136), N152 (= N137), K175 (= K160), S177 (≠ A162), E178 (≠ P163), G208 (≠ N193), G212 (≠ S197), F226 (≠ V210), T227 (= T211), G228 (= G212), G229 (≠ S213), T232 (≠ A216), V236 (≠ I220), E251 (= E234), L252 (= L235), C285 (= C268), E386 (= E365), F388 (= F367)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
33% identity, 97% coverage: 11:457/462 of query aligns to 25:478/489 of 2wmeA
- active site: N152 (= N137), K175 (= K160), E251 (= E234), C285 (= C268), E386 (= E365), E463 (= E442)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ M134), W151 (= W136), K175 (= K160), S177 (≠ A162), E178 (≠ P163), G208 (≠ N193), G212 (≠ S197), F226 (≠ V210), G228 (= G212), G229 (≠ S213), T232 (≠ A216), V236 (≠ I220)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
33% identity, 97% coverage: 11:457/462 of query aligns to 26:479/490 of Q9HTJ1
- GAWN 150:153 (≠ MPWN 134:137) binding
- K162 (≠ G146) active site, Charge relay system
- KPSE 176:179 (≠ KHAP 160:163) binding
- G209 (≠ N193) binding
- GTST 230:233 (≠ SVRA 213:216) binding
- E252 (= E234) active site, Proton acceptor
- C286 (= C268) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E365) binding
- E464 (= E442) active site, Charge relay system
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
35% identity, 95% coverage: 17:457/462 of query aligns to 48:493/505 of 3u4jA
Sites not aligning to the query:
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)
31% identity, 97% coverage: 11:457/462 of query aligns to 31:483/494 of P49189
- C116 (≠ L96) 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)
31% identity, 97% coverage: 11:457/462 of query aligns to 30:482/493 of 6vr6D
- active site: N156 (= N137), E253 (= E234), C287 (= C268), E467 (= E442)
- binding nicotinamide-adenine-dinucleotide: I152 (= I133), G153 (≠ M134), W155 (= W136), K179 (= K160), A212 (≠ N193), G215 (≠ V196), Q216 (≠ S197), F229 (≠ V210), G231 (= G212), S232 (= S213), T235 (≠ A216), I239 (= I220)
Query Sequence
>15646 FitnessBrowser__Keio:15646
MTITPATHAISINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDI
GKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQA
VIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAG
IPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP
FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDP
RDEENALGPMARFDLRDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMT
AFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN
GYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI
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