SitesBLAST
Comparing GFF2285 PGA1_c23170 succinate-semialdehyde dehdyrogenase GabD 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
45% identity, 98% coverage: 8:470/474 of query aligns to 14:477/481 of 3jz4A
- active site: N156 (= N148), K179 (= K171), E254 (= E247), C288 (= C281), E385 (= E378), E462 (= E455)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P146), W155 (= W147), K179 (= K171), A181 (= A173), S182 (= S174), A212 (≠ T205), G216 (≠ V209), G232 (= G225), S233 (= S226), I236 (≠ V229), C288 (= C281), K338 (= K331), E385 (= E378), F387 (= F380)
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)
45% identity, 98% coverage: 8:470/474 of query aligns to 15:478/482 of P25526
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
44% identity, 98% coverage: 7:471/474 of query aligns to 13:478/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ V144), T153 (= T145), P154 (= P146), K179 (= K171), A212 (≠ T205), K213 (≠ G206), F230 (= F223), T231 (= T224), G232 (= G225), S233 (= S226), V236 (= V229), W239 (≠ K232), G256 (= G249)
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
44% identity, 99% coverage: 4:471/474 of query aligns to 61:531/535 of P51649
- C93 (≠ A36) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G119) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (= H123) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P125) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R156) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C166) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 171:174) binding
- T233 (= T176) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ M180) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N198) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (vs. gap) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTGVG 225:230) binding
- R334 (= R275) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N276) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C281) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A283) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D312) natural variant: N -> S
- P382 (= P322) to L: in SSADHD; 2% of activity
- V406 (= V346) to I: in dbSNP:rs143741652
- G409 (= G349) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S438) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
44% identity, 99% coverage: 4:470/474 of query aligns to 11:480/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
44% identity, 99% coverage: 4:470/474 of query aligns to 11:480/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 98% coverage: 6:471/474 of query aligns to 4:476/477 of 6j76A
- active site: N148 (= N148), E246 (= E247), C280 (= C281), E458 (= E455)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ V144), T145 (= T145), A146 (≠ P146), W147 (= W147), N148 (= N148), K171 (= K171), T173 (≠ A173), S174 (= S174), G204 (≠ S202), G208 (= G206), T223 (= T224), G224 (= G225), S225 (= S226), A228 (≠ V229), S231 (≠ K232), I232 (≠ L233), E246 (= E247), L247 (= L248), C280 (= C281), E381 (= E378), F383 (= F380), H447 (≠ F444)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
39% identity, 99% coverage: 3:471/474 of query aligns to 2:473/476 of 5x5uA
- active site: N151 (= N148), K174 (= K171), E249 (= E247), C283 (= C281), E380 (= E378), E457 (= E455)
- binding glycerol: D15 (vs. gap), A16 (≠ H13), A17 (≠ K14), G19 (≠ S16)
- binding nicotinamide-adenine-dinucleotide: P149 (= P146), P207 (= P201), A208 (≠ S202), S211 (≠ T205), G227 (= G225), S228 (= S226), V231 (= V229), R329 (≠ D327), R330 (≠ T328), E380 (= E378), F382 (= F380)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
39% identity, 99% coverage: 3:471/474 of query aligns to 2:473/476 of 5x5tA
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)
36% identity, 98% coverage: 6:471/474 of query aligns to 10:483/497 of P17202
- I28 (= I22) binding
- D96 (≠ E88) binding
- SPW 156:158 (≠ TPW 145:147) binding
- Y160 (= Y149) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R156) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAS 171:174) binding
- L186 (≠ E175) binding
- SSAT 236:239 (≠ STGV 226:229) binding
- V251 (≠ L242) binding in other chain
- L258 (= L248) binding
- W285 (≠ R275) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E378) binding
- A441 (≠ M429) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S438) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F444) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K448) binding
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 99% coverage: 1:470/474 of query aligns to 3:476/486 of 4pxlA
- active site: N154 (= N148), K177 (= K171), E253 (= E247), C287 (= C281), E384 (= E378), D461 (≠ E455)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V144), V151 (≠ T145), P152 (= P146), W153 (= W147), K177 (= K171), E180 (≠ S174), G210 (vs. gap), G214 (≠ T205), A215 (≠ G206), F228 (= F223), G230 (= G225), S231 (= S226), V234 (= V229), E253 (= E247), G255 (= G249), C287 (= C281), Q334 (≠ T328), K337 (= K331), E384 (= E378), F386 (= F380)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
36% identity, 98% coverage: 6:471/474 of query aligns to 8:481/495 of 4v37A
- active site: N157 (= N148), K180 (= K171), E255 (= E247), A289 (≠ C281), E388 (= E378), E465 (= E455)
- binding 3-aminopropan-1-ol: C448 (≠ S438), W454 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V144), S154 (≠ T145), P155 (= P146), W156 (= W147), N157 (= N148), M162 (= M153), K180 (= K171), S182 (≠ A173), E183 (≠ S174), G213 (≠ K204), G217 (vs. gap), A218 (vs. gap), T232 (= T224), G233 (= G225), S234 (= S226), T237 (≠ V229), E255 (= E247), L256 (= L248), A289 (≠ C281), E388 (= E378), F390 (= F380)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
38% identity, 99% coverage: 1:470/474 of query aligns to 8:484/494 of 4pz2B
- active site: N159 (= N148), K182 (= K171), E258 (= E247), C292 (= C281), E392 (= E378), D469 (≠ E455)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V144), I156 (≠ T145), P157 (= P146), W158 (= W147), N159 (= N148), M164 (= M153), K182 (= K171), A184 (= A173), E185 (≠ S174), G215 (vs. gap), G219 (≠ T205), F233 (= F223), T234 (= T224), G235 (= G225), S236 (= S226), V239 (= V229), E258 (= E247), L259 (= L248), C292 (= C281), E392 (= E378), F394 (= F380)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 95% coverage: 18:468/474 of query aligns to 39:491/503 of O14293
- S248 (= S226) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
37% identity, 99% coverage: 1:471/474 of query aligns to 35:510/518 of O94788
- E50 (≠ K14) to G: in dbSNP:rs34266719
- A110 (≠ W71) to V: in dbSNP:rs35365164
- Q182 (≠ L143) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 145:147) binding
- KPAE 210:213 (≠ KPAS 171:174) binding
- STE 264:266 (≠ STG 226:228) binding
- C320 (= C281) active site, Nucleophile
- R347 (≠ L308) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K309) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ DTRDK 327:331) binding
- A383 (= A344) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E378) binding
- E436 (≠ A397) to K: in dbSNP:rs34744827
- S461 (≠ C422) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
37% identity, 99% coverage: 1:471/474 of query aligns to 9:484/492 of 6b5hA
- active site: N161 (= N148), E260 (= E247), C294 (= C281), E468 (= E455)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G98), G116 (≠ Y102), F162 (≠ Y149), W169 (≠ R156), Q284 (≠ L271), F288 (≠ R275), T295 (= T282), N449 (≠ L436), L451 (≠ S438), N452 (≠ D439), F457 (= F444)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V144), I158 (≠ T145), W160 (= W147), N161 (= N148), K184 (= K171), G217 (vs. gap), G221 (≠ T205), F235 (= F223), T236 (= T224), G237 (= G225), S238 (= S226), V241 (= V229), E260 (= E247), L261 (= L248), C294 (= C281), F393 (= F380)
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)
37% identity, 99% coverage: 1:471/474 of query aligns to 9:484/492 of 6b5gA
- active site: N161 (= N148), E260 (= E247), C294 (= C281), E468 (= E455)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y149), L165 (≠ A152), W169 (≠ R156), F288 (≠ R275), C293 (≠ A280), C294 (= C281), T295 (= T282), N449 (≠ L436), L451 (≠ S438)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V144), I158 (≠ T145), P159 (= P146), W160 (= W147), N161 (= N148), M166 (= M153), K184 (= K171), E187 (≠ S174), G217 (vs. gap), G221 (≠ T205), F235 (= F223), T236 (= T224), G237 (= G225), S238 (= S226), V241 (= V229), E260 (= E247), L261 (= L248), C294 (= C281), E391 (= E378), F393 (= F380)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
37% identity, 99% coverage: 1:471/474 of query aligns to 9:484/492 of 6aljA
- active site: N161 (= N148), E260 (= E247), C294 (= C281), E468 (= E455)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ Y102), F162 (≠ Y149), L165 (≠ A152), M166 (= M153), W169 (≠ R156), E260 (= E247), C293 (≠ A280), C294 (= C281), L451 (≠ S438), N452 (≠ D439), A453 (≠ P440)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V144), I158 (≠ T145), P159 (= P146), W160 (= W147), N161 (= N148), K184 (= K171), E187 (≠ S174), G217 (vs. gap), G221 (≠ T205), F235 (= F223), G237 (= G225), S238 (= S226), V241 (= V229), Q341 (≠ T328), K344 (= K331), E391 (= E378), F393 (= F380)
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)
37% identity, 99% coverage: 1:471/474 of query aligns to 35:510/518 of Q63639
Q28399 Aldehyde dehydrogenase, cytosolic 1; ALDH class 1; ETA-crystallin; EC 1.2.1.3 from Elephantulus edwardii (Cape long-eared elephant shrew) (see paper)
37% identity, 99% coverage: 1:471/474 of query aligns to 18:493/501 of Q28399
Query Sequence
>GFF2285 PGA1_c23170 succinate-semialdehyde dehdyrogenase GabD
MEYTDLYINGAWHKTSERFDVINPATEEVLASVASADIADADAALDAAEAAMKDWAARTP
RQRSEVLRKAWELMTKRLDYFANLITLENGKAGTDAKGEATYAAEFFRWFAEEAVRADGM
ITHAPASGARIVVQHKPAGLAVLVTPWNYPAAMGTRKIAPALAAGCGVIIKPASETPLTM
LALMPLLEEAGVPAGLVNVLPSRKTGSLVDHMLHDPRIRVVSFTGSTGVGRKLLKGAADQ
VLKPAMELGGNAPVVVFEDADMDVAIEGTMLAKMRNLGEACTAANRIYVHEDIADEFTKR
LSAAMSALKVGDGTDPSVDVGPLVNADTRDKVAAFVADAVAKGAKVECGGTTPNGKGFYY
PPTVLSNVSEDAECVRDEIFGPVAAIQTFTNQDEVIARANDTEYGLVAYVFSEDFKRALQ
VCEQLEYGMVGLNRGLVSDPAAPFGGVKQSGLGREGGHEGMLEFMETQYISASW
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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