SitesBLAST
Comparing Pf1N1B4_5616 Succinate-semialdehyde dehydrogenase [NAD] (EC 1.2.1.24); Succinate-semialdehyde dehydrogenase [NAD(P)+] (EC 1.2.1.16) 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)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
65% identity, 98% coverage: 8:462/463 of query aligns to 4:458/459 of 3efvA
- active site: N134 (= N138), E231 (= E235), C265 (= C269), E439 (= E443)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ V134), M131 (= M135), P132 (= P136), W133 (= W137), N134 (= N138), Q139 (= Q143), R142 (= R146), K157 (= K161), A159 (= A163), N190 (≠ P194), V193 (= V197), T208 (= T212), G209 (= G213), S210 (= S214), A213 (= A217), E231 (= E235), L232 (= L236), G233 (= G237), C265 (= C269), E362 (= E366), F364 (= F368), F428 (= F432)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
43% identity, 97% coverage: 12:460/463 of query aligns to 4:452/453 of 4itbA
- active site: N130 (= N138), K153 (= K161), E227 (= E235), C261 (= C269), E358 (= E366), E435 (= E443)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (= V134), M127 (= M135), P128 (= P136), W129 (= W137), N130 (= N138), K153 (= K161), A155 (= A163), S156 (≠ P164), A186 (≠ P194), V189 (= V197), G205 (= G213), S206 (= S214), A209 (= A217), S212 (≠ A220), L228 (= L236), C261 (= C269), E358 (= E366), F360 (= F368)
- binding 4-oxobutanoic acid: E227 (= E235), C261 (= C269), S418 (≠ T426)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
43% identity, 97% coverage: 12:460/463 of query aligns to 4:452/453 of 3vz3A
- active site: N130 (= N138), K153 (= K161), E227 (= E235), A261 (≠ C269), E358 (= E366), E435 (= E443)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (= V134), M127 (= M135), W129 (= W137), N130 (= N138), Q135 (= Q143), R138 (= R146), K153 (= K161), A155 (= A163), S156 (≠ P164), A186 (≠ P194), V189 (= V197), T204 (= T212), G205 (= G213), S206 (= S214), A209 (= A217), E227 (= E235), L228 (= L236), G229 (= G237), A261 (≠ C269), F360 (= F368)
- binding 4-oxobutanoic acid: F131 (= F139), W134 (= W142), S260 (≠ V268), A261 (≠ C269), I262 (≠ A270), S418 (≠ T426)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
36% identity, 97% coverage: 12:460/463 of query aligns to 4:453/455 of 4ywuA
- active site: N131 (= N138), K154 (= K161), E228 (= E235), C262 (= C269), E359 (= E366), E436 (= E443)
- binding 4-oxobutanoic acid: N131 (= N138), Q136 (= Q143), R139 (= R146), E228 (= E235), V261 (= V268), C262 (= C269), F425 (= F432)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
36% identity, 97% coverage: 12:460/463 of query aligns to 4:453/455 of 4ohtA
- active site: N131 (= N138), K154 (= K161), E228 (= E235), C262 (= C269), E359 (= E366), E436 (= E443)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (= V134), E128 (≠ M135), P129 (= P136), W130 (= W137), K154 (= K161), H155 (= H162), A156 (= A163), S157 (≠ P164), Y187 (≠ P194), S207 (= S214), I214 (= I221)
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)
36% identity, 95% coverage: 14:452/463 of query aligns to 32:472/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 95% coverage: 14:452/463 of query aligns to 31:471/481 of 3jz4A
- active site: N156 (= N138), K179 (= K161), E254 (= E235), C288 (= C269), E385 (= E366), E462 (= E443)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P136), W155 (= W137), K179 (= K161), A181 (= A163), S182 (≠ P164), A212 (≠ P194), G216 (≠ S198), G232 (= G213), S233 (= S214), I236 (≠ A217), C288 (= C269), K338 (≠ E319), E385 (= E366), F387 (= F368)
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)
35% identity, 97% coverage: 12:461/463 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)
35% identity, 97% coverage: 12:461/463 of query aligns to 30:485/493 of 6vr6D
- active site: N156 (= N138), E253 (= E235), C287 (= C269), E467 (= E443)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ V134), G153 (≠ M135), W155 (= W137), K179 (= K161), A212 (≠ V197), G215 (≠ A200), Q216 (vs. gap), F229 (≠ L211), G231 (= G213), S232 (= S214), T235 (≠ A217), I239 (= I221)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
35% identity, 97% coverage: 14:460/463 of query aligns to 31:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ V134), T153 (≠ M135), P154 (= P136), K179 (= K161), A212 (≠ V192), K213 (≠ T193), F230 (≠ L211), T231 (= T212), G232 (= G213), S233 (= S214), V236 (≠ A217), W239 (≠ A220), G256 (= G237)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
36% identity, 96% coverage: 14:458/463 of query aligns to 33:483/492 of 6b5hA
- active site: N161 (= N138), E260 (= E235), C294 (= C269), E468 (= E443)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (vs. gap), G116 (= G89), F162 (= F139), W169 (≠ R146), Q284 (≠ I259), F288 (≠ Q263), T295 (≠ A270), N449 (≠ C424), L451 (≠ T426), N452 (≠ D427), F457 (= F432)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V134), I158 (≠ M135), W160 (= W137), N161 (= N138), K184 (= K161), G217 (≠ P194), G221 (≠ S198), F235 (≠ L211), T236 (= T212), G237 (= G213), S238 (= S214), V241 (≠ A217), E260 (= E235), L261 (= L236), C294 (= C269), F393 (= F368)
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)
36% identity, 96% coverage: 14:458/463 of query aligns to 33:483/492 of 6b5gA
- active site: N161 (= N138), E260 (= E235), C294 (= C269), E468 (= E443)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F139), L165 (≠ W142), W169 (≠ R146), F288 (≠ Q263), C293 (≠ V268), C294 (= C269), T295 (≠ A270), N449 (≠ C424), L451 (≠ T426)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V134), I158 (≠ M135), P159 (= P136), W160 (= W137), N161 (= N138), M166 (≠ Q143), K184 (= K161), E187 (≠ P164), G217 (≠ P194), G221 (≠ S198), F235 (≠ L211), T236 (= T212), G237 (= G213), S238 (= S214), V241 (≠ A217), E260 (= E235), L261 (= L236), C294 (= C269), E391 (= E366), F393 (= F368)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
36% identity, 96% coverage: 14:458/463 of query aligns to 33:483/492 of 6aljA
- active site: N161 (= N138), E260 (= E235), C294 (= C269), E468 (= E443)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G89), F162 (= F139), L165 (≠ W142), M166 (≠ Q143), W169 (≠ R146), E260 (= E235), C293 (≠ V268), C294 (= C269), L451 (≠ T426), N452 (≠ D427), A453 (≠ P428)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V134), I158 (≠ M135), P159 (= P136), W160 (= W137), N161 (= N138), K184 (= K161), E187 (≠ P164), G217 (≠ P194), G221 (≠ S198), F235 (≠ L211), G237 (= G213), S238 (= S214), V241 (≠ A217), Q341 (≠ L316), K344 (≠ E319), E391 (= E366), F393 (= F368)
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)
36% identity, 96% coverage: 14:458/463 of query aligns to 59:509/518 of O94788
- A110 (= A62) to V: in dbSNP:rs35365164
- Q182 (≠ A133) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ MPW 135:137) binding
- KPAE 210:213 (≠ KHAP 161:164) binding
- STE 264:266 (≠ SVR 214:216) binding
- C320 (= C269) active site, Nucleophile
- R347 (≠ L296) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (= V297) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ DLRDE 315:319) binding
- A383 (= A332) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E366) binding
- E436 (= E385) to K: in dbSNP:rs34744827
- S461 (≠ A410) to Y: in DIH4; decreased retinoic acid biosynthetic process
Sites not aligning to the query:
- 50 E → G: in dbSNP:rs34266719
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)
36% identity, 96% coverage: 14:458/463 of query aligns to 59:509/518 of Q63639
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
33% identity, 93% coverage: 32:461/463 of query aligns to 60:495/503 of 1bpwA
- active site: N166 (= N138), K189 (= K161), E263 (= E235), C297 (= C269), E400 (= E366), E477 (= E443)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V134), L163 (≠ M135), W165 (= W137), N166 (= N138), K189 (= K161), G221 (≠ T193), G225 (≠ V197), T240 (= T212), G241 (= G213), S242 (= S214), T245 (≠ A217), E263 (= E235), L264 (= L236), C297 (= C269), E400 (= E366), F402 (= F368), F466 (= F432)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
33% identity, 93% coverage: 32:461/463 of query aligns to 60:495/503 of P56533
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
36% identity, 93% coverage: 13:443/463 of query aligns to 25:457/476 of 5x5uA
- active site: N151 (= N138), K174 (= K161), E249 (= E235), C283 (= C269), E380 (= E366), E457 (= E443)
- binding nicotinamide-adenine-dinucleotide: P149 (= P136), P207 (= P194), A208 (≠ D195), S211 (= S198), G227 (= G213), S228 (= S214), V231 (≠ A217), R329 (≠ D315), R330 (≠ L316), E380 (= E366), F382 (= F368)
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
36% identity, 93% coverage: 13:443/463 of query aligns to 25:457/476 of 5x5tA
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
34% identity, 97% coverage: 12:458/463 of query aligns to 32:484/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (≠ V134), T159 (≠ M135), P160 (= P136), W161 (= W137), K185 (= K161), E188 (≠ P164), G218 (≠ P194), G222 (≠ S198), F236 (≠ L211), S239 (= S214), V242 (≠ A217)
Query Sequence
>Pf1N1B4_5616 Succinate-semialdehyde dehydrogenase [NAD] (EC 1.2.1.24); Succinate-semialdehyde dehydrogenase [NAD(P)+] (EC 1.2.1.16)
MTNVSSLTHAISINPANGEQIGYYPFESESALEAALSRAVAGFSLWRSKPAEERSQSLIT
LAKVLRGNAETMANMITLEMGKPTTQARGEIEKCAQLCEWYAEHGPAMLTAEPTQVEGGK
ARIEYRPLGPILAVMPWNFPIWQVLRGAVPALIAGNTYVLKHAPNVMGCAYLLREAFKQA
DFPEGVFEVINVTPDGVSTAIADPRIAAVTLTGSVRAGMAIGAQAGAALKKCVLELGGSD
PFIVLNDADLDEAVKAAVIGRYQNTGQVCAAAKRLIVEQGIVEAFTRKFVEATRELVVGD
PLATDTYIGPMARFDLRDELDRQVQQTLEEGATLLMGGKKAEGSGNFFEPTVFADVTDRM
TSFKQELFGPVASIITARDAAHALELANDSEFGLASTIYTRDVELAHKLAGELETGGVFI
NGYCATDPRVTFGGVKKSGFGRELSHFGVREFCNAQTVWLDRR
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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