SitesBLAST
Comparing Dsui_0437 Dsui_0437 succinate-semialdehyde dehydrogenase 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)
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)
70% identity, 100% coverage: 1:483/483 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
70% identity, 100% coverage: 2:483/483 of query aligns to 1:481/481 of 3jz4A
- active site: N156 (= N155), K179 (= K178), E254 (= E253), C288 (= C287), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P153), W155 (= W154), K179 (= K178), A181 (= A180), S182 (≠ E181), A212 (≠ P211), G216 (= G215), G232 (= G231), S233 (= S232), I236 (≠ V235), C288 (= C287), K338 (= K337), E385 (= E387), F387 (= F389)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
62% identity, 99% coverage: 3:482/483 of query aligns to 2:480/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I151), T153 (= T152), P154 (= P153), K179 (= K178), A212 (≠ P211), K213 (≠ V212), F230 (= F229), T231 (= T230), G232 (= G231), S233 (= S232), V236 (= V235), W239 (≠ L238), G256 (= G255)
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)
58% identity, 98% coverage: 8:482/483 of query aligns to 58:533/535 of P51649
- C93 (≠ F43) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G126) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P130) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ V132) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R163) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C173) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 178:181) binding
- T233 (= T183) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A187) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N205) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G215) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 231:236) binding
- R334 (= R281) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N282) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C287) modified: Disulfide link with 342, In inhibited form
- C342 (= C289) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ E318) natural variant: N -> S
- P382 (= P328) to L: in SSADHD; 2% of activity
- V406 (= V352) to I: in dbSNP:rs143741652
- G409 (= G355) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S447) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G482) to R: in SSADHD; <1% of activity; dbSNP:rs72552284
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
58% identity, 98% coverage: 8:482/483 of query aligns to 8:483/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
58% identity, 98% coverage: 8:482/483 of query aligns to 8:483/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
42% identity, 97% coverage: 12:481/483 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N155), K174 (= K178), E249 (= E253), C283 (= C287), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (≠ G21), A16 (≠ G22), A17 (≠ E23), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P153), P207 (= P211), A208 (≠ V212), S211 (≠ G215), G227 (= G231), S228 (= S232), V231 (= V235), R329 (≠ D333), R330 (≠ A334), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
42% identity, 97% coverage: 12:481/483 of query aligns to 6:474/476 of 5x5tA
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
39% identity, 98% coverage: 9:481/483 of query aligns to 3:475/477 of 2opxA
- active site: N151 (= N155), K174 (= K178), E249 (= E253), C283 (= C287), E381 (= E387), A458 (≠ E464)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y109), F152 (= F156), N284 (≠ V288), F312 (≠ V316), G313 (= G317), R318 (≠ A322), D320 (vs. gap), I321 (≠ V324), A322 (≠ T325), Y362 (≠ F368), F440 (≠ I446), F440 (≠ I446), E441 (≠ S447)
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)
39% identity, 98% coverage: 9:481/483 of query aligns to 3:475/477 of 2impA
- active site: N151 (= N155), K174 (= K178), E249 (= E253), C283 (= C287), E381 (= E387), A458 (≠ E464)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I151), L148 (≠ T152), P149 (= P153), W150 (= W154), K174 (= K178), E177 (= E181), F178 (≠ Q182), G207 (≠ P211), G211 (= G215), Q212 (≠ G216), S228 (= S232), A231 (≠ V235), K234 (≠ L238), R334 (≠ K337)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 98% coverage: 9:481/483 of query aligns to 3:475/477 of 2iluA
- active site: N151 (= N155), K174 (= K178), E249 (= E253), C283 (= C287), E381 (= E387), A458 (≠ E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I151), L148 (≠ T152), P149 (= P153), W150 (= W154), K174 (= K178), S176 (≠ A180), E177 (= E181), R206 (≠ D210), G207 (≠ P211), G211 (= G215), Q212 (≠ G216), S228 (= S232), A231 (≠ V235), K234 (≠ L238), I235 (≠ L239), N328 (≠ D331), R334 (≠ K337), F383 (= F389)
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)
39% identity, 98% coverage: 9:481/483 of query aligns to 5:477/479 of P25553
- L150 (≠ T152) binding
- R161 (= R163) binding
- KPSE 176:179 (≠ KPAE 178:181) binding
- F180 (≠ Q182) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ G216) binding
- S230 (= S232) binding
- E251 (= E253) binding
- N286 (≠ V288) 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 (≠ K337) binding
- E443 (≠ S447) binding
- H449 (≠ F453) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 12:477/483 of query aligns to 3:471/477 of 6j76A
- active site: N148 (= N155), E246 (= E253), C280 (= C287), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I151), T145 (= T152), A146 (≠ P153), W147 (= W154), N148 (= N155), K171 (= K178), T173 (≠ A180), S174 (≠ E181), G204 (≠ P211), G208 (= G215), T223 (= T230), G224 (= G231), S225 (= S232), A228 (≠ V235), S231 (≠ L238), I232 (≠ L239), E246 (= E253), L247 (= L254), C280 (= C287), E381 (= E387), F383 (= F389), H447 (≠ F453)
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)
38% identity, 98% coverage: 9:480/483 of query aligns to 16:492/505 of 4neaA
- active site: N166 (= N155), K189 (= K178), E264 (= E253), C298 (= C287), E399 (= E387), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P153), K189 (= K178), E192 (= E181), G222 (≠ P211), G226 (= G215), G242 (= G231), G243 (≠ S232), T246 (≠ V235), H249 (≠ L238), I250 (≠ L239), C298 (= C287), E399 (= E387), F401 (= F389)
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)
39% identity, 98% coverage: 12:483/483 of query aligns to 39:513/518 of Q63639
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, 98% coverage: 12:483/483 of query aligns to 39:513/518 of O94788
- E50 (= E23) to G: in dbSNP:rs34266719
- A110 (≠ F78) to V: in dbSNP:rs35365164
- Q182 (≠ A150) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 152:154) binding
- KPAE 210:213 (= KPAE 178:181) binding
- STE 264:266 (= STE 232:234) binding
- C320 (= C287) active site, Nucleophile
- R347 (≠ L314) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K315) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ DALAK 333:337) binding
- A383 (= A350) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E387) binding
- E436 (≠ A406) to K: in dbSNP:rs34744827
- S461 (≠ G431) 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)
39% identity, 98% coverage: 12:483/483 of query aligns to 13:487/492 of 6b5hA
- active site: N161 (= N155), E260 (= E253), C294 (= C287), E468 (= E464)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G105), G116 (≠ Y109), F162 (= F156), W169 (≠ R163), Q284 (≠ I277), F288 (≠ R281), T295 (≠ V288), N449 (≠ L445), L451 (≠ S447), N452 (= N448), F457 (= F453)
- binding nicotinamide-adenine-dinucleotide: I157 (= I151), I158 (≠ T152), W160 (= W154), N161 (= N155), K184 (= K178), G217 (≠ P211), G221 (= G215), F235 (= F229), T236 (= T230), G237 (= G231), S238 (= S232), V241 (= V235), E260 (= E253), L261 (= L254), C294 (= C287), F393 (= F389)
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, 98% coverage: 12:483/483 of query aligns to 13:487/492 of 6b5gA
- active site: N161 (= N155), E260 (= E253), C294 (= C287), E468 (= E464)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F156), L165 (≠ A159), W169 (≠ R163), F288 (≠ R281), C293 (≠ T286), C294 (= C287), T295 (≠ V288), N449 (≠ L445), L451 (≠ S447)
- binding nicotinamide-adenine-dinucleotide: I157 (= I151), I158 (≠ T152), P159 (= P153), W160 (= W154), N161 (= N155), M166 (= M160), K184 (= K178), E187 (= E181), G217 (≠ P211), G221 (= G215), F235 (= F229), T236 (= T230), G237 (= G231), S238 (= S232), V241 (= V235), E260 (= E253), L261 (= L254), C294 (= C287), E391 (= E387), F393 (= F389)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
39% identity, 98% coverage: 12:483/483 of query aligns to 13:487/492 of 6aljA
- active site: N161 (= N155), E260 (= E253), C294 (= C287), E468 (= E464)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ Y109), F162 (= F156), L165 (≠ A159), M166 (= M160), W169 (≠ R163), E260 (= E253), C293 (≠ T286), C294 (= C287), L451 (≠ S447), N452 (= N448), A453 (≠ E449)
- binding nicotinamide-adenine-dinucleotide: I157 (= I151), I158 (≠ T152), P159 (= P153), W160 (= W154), N161 (= N155), K184 (= K178), E187 (= E181), G217 (≠ P211), G221 (= G215), F235 (= F229), G237 (= G231), S238 (= S232), V241 (= V235), Q341 (≠ A334), K344 (= K337), E391 (= E387), F393 (= F389)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
39% identity, 96% coverage: 12:477/483 of query aligns to 104:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K178), S310 (≠ D210), G311 (≠ P211), G315 (= G215), G331 (= G231), S332 (= S232), V335 (= V235)
- binding 4'-phosphopantetheine: K201 (≠ R104), F382 (≠ R281), N387 (≠ T286), C388 (= C287), N545 (≠ L445)
Query Sequence
>Dsui_0437 Dsui_0437 succinate-semialdehyde dehydrogenase
MKLEDSNLLRQQCYLNGQWVGGESDFPVHNPASGAELARVPRFGAAETRAAIAAADAAWP
AWRSRTAKERTGVLRRWFELMNQHADDLALLMTSEQGKPLAEARGEVAYAASFVEWFAEE
AKRAYGETIPAVAADKRMLVIKQPIGVCAAITPWNFPAAMITRKVAPALAAGCTVVVKPA
EQTPLTALALAELAHRAGFPAGVFNVITGDPVAIGGELTSNPTVRKLSFTGSTEVGRLLM
GQCAPSIKKLSLELGGNAPFIVFDDADLDAAVEGAMISKYRNTGQTCVCANRLLVQDGIY
EAFAARLAAKVATLKVGEGTEAGVTQGPLIDADALAKVEAHIADAVAHGARVLAGGRRHE
RYREGGAFFQPTVLADVTPQMRVAREETFGPVAPLFRFQTEEEAIALANATEFGLASYFY
SRDIGRIFRVGEALEYGMVGVNTGLISNEVAPFGGIKQSGLGREGSKYGLEEYLEVKYLC
LGL
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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