SitesBLAST
Comparing SMa0805 SMa0805 GabD4 succinate-semialdehyde dehdyrogenase 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)
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)
62% identity, 98% coverage: 9:490/490 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
62% identity, 98% coverage: 10:490/490 of query aligns to 1:481/481 of 3jz4A
- active site: N156 (= N166), K179 (= K189), E254 (= E265), C288 (= C299), E385 (= E394), E462 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P164), W155 (= W165), K179 (= K189), A181 (= A191), S182 (≠ A192), A212 (≠ D222), G216 (= G227), G232 (= G243), S233 (= S244), I236 (≠ V247), C288 (= C299), K338 (= K349), E385 (= E394), F387 (= F396)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
60% identity, 98% coverage: 11:488/490 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I162), T153 (= T163), P154 (= P164), K179 (= K189), A212 (≠ S223), K213 (≠ A224), F230 (= F241), T231 (= T242), G232 (= G243), S233 (= S244), V236 (= V247), W239 (≠ I250), G256 (= G267)
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)
54% identity, 95% coverage: 22:487/490 of query aligns to 64:531/535 of P51649
- C93 (≠ M54) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G137) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P141) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H143) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R174) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C184) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAA 189:192) binding
- T233 (= T194) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A198) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N216) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G227) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTNVG 243:248) binding
- R334 (= R293) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N294) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C299) modified: Disulfide link with 342, In inhibited form
- C342 (= C301) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D330) natural variant: N -> S
- P382 (= P340) to L: in SSADHD; 2% of activity
- V406 (≠ L364) to I: in dbSNP:rs143741652
- G409 (= G367) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S454) 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)
54% identity, 95% coverage: 22:487/490 of query aligns to 14:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 95% coverage: 22:487/490 of query aligns to 14:481/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 95% coverage: 23:489/490 of query aligns to 6:476/477 of 6j76A
- active site: N148 (= N166), E246 (= E265), C280 (= C299), E458 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I162), T145 (= T163), A146 (≠ P164), W147 (= W165), N148 (= N166), K171 (= K189), T173 (≠ A191), S174 (≠ A192), G204 (≠ S223), G208 (= G227), T223 (= T242), G224 (= G243), S225 (= S244), A228 (≠ V247), S231 (≠ I250), I232 (≠ L251), E246 (= E265), L247 (= L266), C280 (= C299), E381 (= E394), F383 (= F396), H447 (≠ F460)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 92% coverage: 33:484/490 of query aligns to 19:474/486 of 4pxlA
- active site: N154 (= N166), K177 (= K189), E253 (= E265), C287 (= C299), E384 (= E394), D461 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I150 (= I162), V151 (≠ T163), P152 (= P164), W153 (= W165), K177 (= K189), E180 (≠ A192), G210 (≠ S223), G214 (= G227), A215 (≠ K228), F228 (= F241), G230 (= G243), S231 (= S244), V234 (= V247), E253 (= E265), G255 (= G267), C287 (= C299), Q334 (≠ A346), K337 (= K349), E384 (= E394), F386 (= F396)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 98% coverage: 11:490/490 of query aligns to 12:495/501 of Q56YU0
- G152 (≠ I149) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V411) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
39% identity, 97% coverage: 14:490/490 of query aligns to 31:513/518 of O94788
- E50 (≠ D32) to G: in dbSNP:rs34266719
- A110 (≠ Y89) to V: in dbSNP:rs35365164
- Q182 (≠ A161) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 163:165) binding
- KPAE 210:213 (≠ KPAA 189:192) binding
- STE 264:266 (≠ STN 244:246) binding
- C320 (= C299) active site, Nucleophile
- R347 (≠ M326) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ T327) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ KALAK 345:349) binding
- A383 (= A362) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E394) binding
- E436 (≠ S413) to K: in dbSNP:rs34744827
- S461 (≠ A438) to Y: in DIH4; decreased retinoic acid biosynthetic process
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
37% identity, 96% coverage: 20:488/490 of query aligns to 4:475/494 of 5izdA
- active site: N149 (= N166), K172 (= K189), E247 (= E265), C281 (= C299), E381 (= E394), E458 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I162), T146 (= T163), W148 (= W165), K172 (= K189), P173 (= P190), S174 (≠ A191), S175 (≠ A192), R204 (≠ T221), G205 (≠ D222), G209 (= G227), D210 (≠ K228), G225 (= G243), S226 (= S244), T229 (≠ V247)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
39% identity, 97% coverage: 14:490/490 of query aligns to 5:487/492 of 6b5hA
- active site: N161 (= N166), E260 (= E265), C294 (= C299), E468 (= E471)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (vs. gap), G116 (= G116), F162 (= F167), W169 (≠ R174), Q284 (≠ V289), F288 (≠ R293), T295 (≠ V300), N449 (≠ L452), L451 (≠ S454), N452 (≠ T455), F457 (= F460)
- binding nicotinamide-adenine-dinucleotide: I157 (= I162), I158 (≠ T163), W160 (= W165), N161 (= N166), K184 (= K189), G217 (≠ S223), G221 (= G227), F235 (= F241), T236 (= T242), G237 (= G243), S238 (= S244), V241 (= V247), E260 (= E265), L261 (= L266), C294 (= C299), F393 (= F396)
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)
39% identity, 97% coverage: 14:490/490 of query aligns to 5:487/492 of 6b5gA
- active site: N161 (= N166), E260 (= E265), C294 (= C299), E468 (= E471)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F167), L165 (≠ A170), W169 (≠ R174), F288 (≠ R293), C293 (≠ T298), C294 (= C299), T295 (≠ V300), N449 (≠ L452), L451 (≠ S454)
- binding nicotinamide-adenine-dinucleotide: I157 (= I162), I158 (≠ T163), P159 (= P164), W160 (= W165), N161 (= N166), M166 (= M171), K184 (= K189), E187 (≠ A192), G217 (≠ S223), G221 (= G227), F235 (= F241), T236 (= T242), G237 (= G243), S238 (= S244), V241 (= V247), E260 (= E265), L261 (= L266), C294 (= C299), E391 (= E394), F393 (= F396)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
39% identity, 97% coverage: 14:490/490 of query aligns to 5:487/492 of 6aljA
- active site: N161 (= N166), E260 (= E265), C294 (= C299), E468 (= E471)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G116), F162 (= F167), L165 (≠ A170), M166 (= M171), W169 (≠ R174), E260 (= E265), C293 (≠ T298), C294 (= C299), L451 (≠ S454), N452 (≠ T455), A453 (≠ E456)
- binding nicotinamide-adenine-dinucleotide: I157 (= I162), I158 (≠ T163), P159 (= P164), W160 (= W165), N161 (= N166), K184 (= K189), E187 (≠ A192), G217 (≠ S223), G221 (= G227), F235 (= F241), G237 (= G243), S238 (= S244), V241 (= V247), Q341 (≠ A346), K344 (= K349), E391 (= E394), F393 (= F396)
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)
38% identity, 97% coverage: 14:490/490 of query aligns to 31:513/518 of Q63639
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
37% identity, 95% coverage: 20:486/490 of query aligns to 19:491/505 of 4neaA
- active site: N166 (= N166), K189 (= K189), E264 (= E265), C298 (= C299), E399 (= E394), E476 (= E471)
- binding nicotinamide-adenine-dinucleotide: P164 (= P164), K189 (= K189), E192 (≠ A192), G222 (≠ D222), G226 (= G227), G242 (= G243), G243 (≠ S244), T246 (≠ V247), H249 (≠ I250), I250 (≠ L251), C298 (= C299), E399 (= E394), F401 (= F396)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 92% coverage: 37:489/490 of query aligns to 22:476/477 of 2opxA
- active site: N151 (= N166), K174 (= K189), E249 (= E265), C283 (= C299), E381 (= E394), A458 (≠ E471)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y120), F152 (= F167), N284 (≠ V300), F312 (≠ I328), G313 (= G329), R318 (vs. gap), D320 (= D335), I321 (≠ V336), A322 (≠ D337), Y362 (≠ F375), F440 (≠ I453), F440 (≠ I453), E441 (≠ S454)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
39% identity, 95% coverage: 22:488/490 of query aligns to 8:474/476 of 5x5uA
- active site: N151 (= N166), K174 (= K189), E249 (= E265), C283 (= C299), E380 (= E394), E457 (= E471)
- binding glycerol: D15 (= D29), A16 (≠ S31), A17 (≠ D32), G19 (= G34)
- binding nicotinamide-adenine-dinucleotide: P149 (= P164), P207 (≠ S223), A208 (= A224), S211 (≠ G227), G227 (= G243), S228 (= S244), V231 (= V247), R329 (≠ K345), R330 (≠ A346), E380 (= E394), F382 (= F396)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
39% identity, 95% coverage: 22:488/490 of query aligns to 8:474/476 of 5x5tA
7radA Crystal structure analysis of aldh1b1
39% identity, 98% coverage: 13:490/490 of query aligns to 7:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I162), I159 (≠ T163), P160 (= P164), W161 (= W165), N162 (= N166), M167 (= M171), K185 (= K189), E188 (≠ A192), G218 (vs. gap), G222 (≠ S223), A223 (= A224), T237 (= T242), G238 (= G243), S239 (= S244), V242 (= V247), E261 (= E265), L262 (= L266), C295 (= C299), E392 (= E394), F394 (= F396)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ E117), E117 (≠ G121), F163 (= F167), E285 (≠ V289), F289 (≠ R293), N450 (≠ L452), V452 (≠ S454)
Query Sequence
>SMa0805 SMa0805 GabD4 succinate-semialdehyde dehdyrogenase
MTISETLLVKLKDPSLAVDKGLIGAEWLDRSDSGKTFDVSNPATGEVIAILPDMSRSETA
RAIDAAHAAQRAWAEKTGKERAAVLRNLYDLVVANADDLATILTMEMGKPLTEAKGEILY
GASYVEWFGEEAKRVYGDTIPGHQPDKRIIVLKQPIGVVAAITPWNFPNAMLARKLAPAA
AAGCAVVSKPAAETPLSALALALLAERAGLPAGVFNVILSTDSAEVGKEMCANDKVRKLT
FTGSTNVGKILMRQGADQIMKLGLELGGNAPFIVFDDADLDAAVEGAMVAKYRNNGQTCV
CANRIFVQAGIYDAFAARLTAKVSEMTIGDGFEPDVDAGPLISEKALAKVEEHIRDAVTK
GADLVLGGNARGGLFFEPTVLTGATMDMKIAGEETFGPVAPLFKFETENEVVSMANKTEF
GLASYFYSKDVSKVFRVAEALEYGMVGINTGLISTEVAPFGGVKQSGQGREGSKYGIDDY
VETKYLCLSI
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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