SitesBLAST
Comparing N515DRAFT_2488 N515DRAFT_2488 succinate-semialdehyde dehydrogenase / glutarate-semialdehyde dehydrogenase 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)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
45% identity, 98% coverage: 2:456/463 of query aligns to 1:453/455 of 4ywuA
- active site: N131 (= N134), K154 (= K157), E228 (= E231), C262 (= C265), E359 (= E362), E436 (= E439)
- binding 4-oxobutanoic acid: N131 (= N134), Q136 (= Q139), R139 (= R142), E228 (= E231), V261 (= V264), C262 (= C265), F425 (= F428)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
45% identity, 98% coverage: 2:456/463 of query aligns to 1:453/455 of 4ohtA
- active site: N131 (= N134), K154 (= K157), E228 (= E231), C262 (= C265), E359 (= E362), E436 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (= V130), E128 (= E131), P129 (= P132), W130 (= W133), K154 (= K157), H155 (= H158), A156 (= A159), S157 (= S160), Y187 (≠ R190), S207 (= S210), I214 (≠ V217)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
44% identity, 97% coverage: 4:454/463 of query aligns to 3:450/453 of 4itbA
- active site: N130 (= N134), K153 (= K157), E227 (= E231), C261 (= C265), E358 (= E362), E435 (= E439)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (= V130), M127 (≠ E131), P128 (= P132), W129 (= W133), N130 (= N134), K153 (= K157), A155 (= A159), S156 (= S160), A186 (≠ R190), V189 (≠ L193), G205 (= G209), S206 (= S210), A209 (= A213), S212 (≠ V216), L228 (= L232), C261 (= C265), E358 (= E362), F360 (= F364)
- binding 4-oxobutanoic acid: E227 (= E231), C261 (= C265), S418 (≠ V422)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
43% identity, 97% coverage: 4:454/463 of query aligns to 3:450/453 of 3vz3A
- active site: N130 (= N134), K153 (= K157), E227 (= E231), A261 (≠ C265), E358 (= E362), E435 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (= V130), M127 (≠ E131), W129 (= W133), N130 (= N134), Q135 (= Q139), R138 (= R142), K153 (= K157), A155 (= A159), S156 (= S160), A186 (≠ R190), V189 (≠ L193), T204 (= T208), G205 (= G209), S206 (= S210), A209 (= A213), E227 (= E231), L228 (= L232), G229 (= G233), A261 (≠ C265), F360 (= F364)
- binding 4-oxobutanoic acid: F131 (= F135), W134 (≠ Y138), S260 (≠ V264), A261 (≠ C265), I262 (≠ C266), S418 (≠ V422)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
40% identity, 97% coverage: 5:454/463 of query aligns to 8:454/459 of 3efvA
- active site: N134 (= N134), E231 (= E231), C265 (= C265), E439 (= E439)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ V130), M131 (≠ E131), P132 (= P132), W133 (= W133), N134 (= N134), Q139 (= Q139), R142 (= R142), K157 (= K157), A159 (= A159), N190 (≠ R190), V193 (≠ L193), T208 (= T208), G209 (= G209), S210 (= S210), A213 (= A213), E231 (= E231), L232 (= L232), G233 (= G233), C265 (= C265), E362 (= E362), F364 (= F364), F428 (= F428)
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)
33% identity, 97% coverage: 7:456/463 of query aligns to 32:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 97% coverage: 7:456/463 of query aligns to 31:479/481 of 3jz4A
- active site: N156 (= N134), K179 (= K157), E254 (= E231), C288 (= C265), E385 (= E362), E462 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P132), W155 (= W133), K179 (= K157), A181 (= A159), S182 (= S160), A212 (≠ R190), G216 (vs. gap), G232 (= G209), S233 (= S210), I236 (≠ A213), C288 (= C265), K338 (≠ D315), E385 (= E362), F387 (= F364)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
31% identity, 97% coverage: 7:457/463 of query aligns to 7:464/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (≠ V130), L137 (≠ E131), F139 (≠ W133), K163 (= K157), S165 (≠ A159), I166 (≠ S160), S196 (≠ R190), G200 (vs. gap), G216 (= G209), S217 (= S210), T220 (≠ A213), I224 (≠ V217)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
31% identity, 97% coverage: 7:457/463 of query aligns to 7:464/466 of 8hapA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: I136 (≠ V130), L137 (≠ E131), F139 (≠ W133), K163 (= K157), S165 (≠ A159), I166 (≠ S160), S196 (≠ R190), G200 (vs. gap), G216 (= G209), S217 (= S210), T220 (≠ A213), I224 (≠ V217), L239 (= L232), C272 (= C265), E368 (= E362), F370 (= F364)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 97% coverage: 7:457/463 of query aligns to 44:496/503 of O14293
- S248 (= S210) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
31% identity, 98% coverage: 8:463/463 of query aligns to 33:493/493 of 6vr6D
- active site: N156 (= N134), E253 (= E231), C287 (= C265), E467 (= E439)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ V130), G153 (≠ E131), W155 (= W133), K179 (= K157), A212 (≠ R190), G215 (≠ L193), Q216 (≠ K194), F229 (≠ L207), G231 (= G209), S232 (= S210), T235 (≠ A213), I239 (≠ V217)
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, 98% coverage: 8:463/463 of query aligns to 34:494/494 of P49189
- C116 (≠ I90) 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
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
31% identity, 97% coverage: 7:456/463 of query aligns to 24:475/494 of 5izdA
- active site: N149 (= N134), K172 (= K157), E247 (= E231), C281 (= C265), E381 (= E362), E458 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ V130), T146 (≠ E131), W148 (= W133), K172 (= K157), P173 (≠ H158), S174 (≠ A159), S175 (= S160), R204 (≠ T189), G205 (≠ R190), G209 (vs. gap), D210 (≠ K194), G225 (= G209), S226 (= S210), T229 (≠ A213)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
30% identity, 98% coverage: 3:456/463 of query aligns to 49:505/512 of P47895
- R89 (≠ K40) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K157) binding
- E207 (≠ S160) binding
- GSTEVG 257:262 (≠ GSEGAG 209:214) binding
- Q361 (≠ A312) binding
- E411 (= E362) binding
- A493 (≠ G444) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
30% identity, 98% coverage: 3:456/463 of query aligns to 31:487/489 of 7a6qB
- active site: N163 (= N134), E262 (= E231), C296 (= C265), E470 (= E439)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V130), W162 (= W133), K186 (= K157), E189 (≠ S160), G219 (≠ T184), G223 (≠ A188), S240 (= S210), V243 (≠ A213), K342 (≠ G311)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (= A4), T33 (= T5), C34 (≠ I6), P36 (= P8), D103 (≠ E72), E189 (≠ S160), Q190 (≠ N161), F218 (= F183), I339 (≠ S308), D340 (≠ S309)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ L86), D141 (≠ S109), N143 (≠ H111), N451 (≠ T420), L453 (≠ V422), A455 (= A424)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
30% identity, 98% coverage: 3:456/463 of query aligns to 31:487/489 of 7a6qA
- active site: N163 (= N134), E262 (= E231), C296 (= C265), E470 (= E439)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V130), T160 (≠ E131), W162 (= W133), K186 (= K157), A188 (= A159), E189 (≠ S160), G219 (≠ T184), G223 (≠ A188), S240 (= S210), V243 (≠ A213), K342 (≠ G311), K346 (≠ D315)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ L86), D141 (≠ S109), N143 (≠ H111), N451 (≠ T420), L453 (≠ V422), Y454 (≠ A423)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
30% identity, 98% coverage: 3:456/463 of query aligns to 31:487/489 of 5fhzA
- active site: N163 (= N134), K186 (= K157), E262 (= E231), C296 (= C265), E393 (= E362), E470 (= E439)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V130), T160 (≠ E131), W162 (= W133), K186 (= K157), E189 (≠ S160), G219 (≠ T184), G223 (≠ A188), F237 (≠ L207), G239 (= G209), S240 (= S210), T241 (≠ E211), V243 (≠ A213), G264 (= G233), Q343 (≠ A312), E393 (= E362)
- binding retinoic acid: G118 (≠ L86), R121 (≠ Q89), F164 (= F135), M168 (≠ Q139), W171 (≠ R142), C295 (≠ V264), C296 (= C265), L453 (≠ V422)
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
30% identity, 98% coverage: 3:456/463 of query aligns to 30:486/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (≠ V130), T159 (≠ E131), P160 (= P132), W161 (= W133), K185 (= K157), E188 (≠ S160), G218 (≠ T184), G222 (≠ A188), F236 (≠ L207), S239 (= S210), V242 (≠ A213)
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)
32% identity, 97% coverage: 6:454/463 of query aligns to 28:482/497 of P17202
- I28 (= I6) binding
- D96 (≠ E72) binding
- SPW 156:158 (≠ EPW 131:133) binding
- Y160 (≠ F135) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R142) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAS 157:160) binding
- L186 (≠ N161) binding
- SSAT 236:239 (≠ SEGA 210:213) binding
- V251 (≠ L225) binding in other chain
- L258 (= L232) binding
- W285 (= W259) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E362) binding
- A441 (≠ M413) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V422) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F428) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R432) binding
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
32% identity, 98% coverage: 2:456/463 of query aligns to 30:488/497 of 8skfA
- binding calcium ion: T33 (= T5), I34 (= I6), D100 (≠ E72), V187 (≠ N161)
- binding nicotinamide-adenine-dinucleotide: I156 (≠ V130), G157 (≠ E131), A158 (≠ P132), W159 (= W133), K183 (= K157), E186 (≠ S160), G216 (≠ R190), G220 (vs. gap), T235 (= T208), G236 (= G209), G237 (≠ S210), S240 (≠ A213), K243 (vs. gap), E259 (= E231), C293 (= C265), F396 (= F364)
Query Sequence
>N515DRAFT_2488 N515DRAFT_2488 succinate-semialdehyde dehydrogenase / glutarate-semialdehyde dehydrogenase
MSYATINPYTGETVKTFPSATDAEVTQALDQAQAMFEAWKDVGVAARVKVLQKAADLLRE
SHTQYAKVLTLEMGKVIGEAEGEVELCAQILEYYADHAEQLLAPEKLSSRHPSYTQSWVE
HVPQGILLAVEPWNFPYYQIVRIAAPQLAAGNVLILKHASNVPQCAAAFERLFREAGLPQ
GGFTNLYATRDQLKAIIEDPRVQGVALTGSEGAGAVVAAQAGQALKKSTMELGGADAFVV
LADADLDKAVQWAVTGRHWNAGQVCCSSKRIIVVDEIYDAFLEKYKAGVARLRAGDPMEP
STTLAPMSSRGAVDDLKKQLEQAVAHGAKVEVIGAEVPSRGAFFRPVLLSHVSDDNPARY
WEFFGPVSQVIRARDEADAIRIANDSPFGLGGSVFTTDIKHGIEVAKKISTGMVYINHPT
GVAADLPFGGVRRSGYGRELTGLGIKEFVNHKLIAVTDIDGAF
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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