SitesBLAST
Comparing SM_b21185 SM_b21185 succinate-semialdehyde dehydrogenase (NAD(P)+) protein 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)
59% identity, 93% coverage: 32:489/491 of query aligns to 25:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
59% identity, 93% coverage: 32:489/491 of query aligns to 24:480/481 of 3jz4A
- active site: N156 (= N164), K179 (= K187), E254 (= E263), C288 (= C297), E385 (= E394), E462 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P162), W155 (= W163), K179 (= K187), A181 (= A189), S182 (≠ E190), A212 (≠ E220), G216 (= G225), G232 (= G241), S233 (= S242), I236 (≠ V245), C288 (= C297), K338 (= K347), E385 (= E394), F387 (= F396)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
57% identity, 95% coverage: 28:491/491 of query aligns to 20:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I160), T153 (= T161), P154 (= P162), K179 (= K187), A212 (≠ G221), K213 (≠ A222), F230 (= F239), T231 (= T240), G232 (= G241), S233 (= S242), V236 (= V245), W239 (≠ L248), G256 (= G265)
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)
50% identity, 94% coverage: 30:491/491 of query aligns to 71:535/535 of P51649
- C93 (≠ M52) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G135) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P139) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P141) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R172) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C182) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 187:190) binding
- T233 (= T192) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A196) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N214) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G225) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 241:246) binding
- R334 (= R291) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N292) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C297) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S299) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D328) natural variant: N -> S
- P382 (= P338) to L: in SSADHD; 2% of activity
- V406 (= V362) to I: in dbSNP:rs143741652
- G409 (= G365) 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.
- G533 (= G489) 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)
50% identity, 94% coverage: 30:491/491 of query aligns to 21:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
50% identity, 94% coverage: 30:491/491 of query aligns to 21:485/485 of 2w8qA
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)
39% identity, 92% coverage: 36:487/491 of query aligns to 36:492/505 of 4neaA
- active site: N166 (= N164), K189 (= K187), E264 (= E263), C298 (= C297), E399 (= E394), E476 (= E471)
- binding nicotinamide-adenine-dinucleotide: P164 (= P162), K189 (= K187), E192 (= E190), G222 (= G221), G226 (= G225), G242 (= G241), G243 (≠ S242), T246 (≠ V245), H249 (≠ L248), I250 (≠ L249), C298 (= C297), E399 (= E394), F401 (= F396)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
39% identity, 92% coverage: 35:488/491 of query aligns to 22:475/477 of 2opxA
- active site: N151 (= N164), K174 (= K187), E249 (= E263), C283 (= C297), E381 (= E394), A458 (≠ E471)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ H118), F152 (= F165), N284 (≠ V298), F312 (≠ V326), G313 (= G327), R318 (≠ A331), D320 (= D333), I321 (≠ V334), A322 (= A335), Y362 (≠ F375), F440 (≠ M453), F440 (≠ M453), E441 (≠ S454)
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, 92% coverage: 35:488/491 of query aligns to 24:477/479 of P25553
- L150 (≠ T161) binding
- R161 (= R172) binding
- KPSE 176:179 (≠ KPAE 187:190) binding
- F180 (≠ Q191) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ R226) binding
- S230 (= S242) binding
- E251 (= E263) binding
- N286 (≠ V298) 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 (≠ K347) binding
- E443 (≠ S454) binding
- H449 (≠ F460) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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, 92% coverage: 35:488/491 of query aligns to 22:475/477 of 2impA
- active site: N151 (= N164), K174 (= K187), E249 (= E263), C283 (= C297), E381 (= E394), A458 (≠ E471)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I160), L148 (≠ T161), P149 (= P162), W150 (= W163), K174 (= K187), E177 (= E190), F178 (≠ Q191), G207 (= G221), G211 (= G225), Q212 (≠ R226), S228 (= S242), A231 (≠ V245), K234 (≠ L248), R334 (≠ K347)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 92% coverage: 35:488/491 of query aligns to 22:475/477 of 2iluA
- active site: N151 (= N164), K174 (= K187), E249 (= E263), C283 (= C297), E381 (= E394), A458 (≠ E471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I160), L148 (≠ T161), P149 (= P162), W150 (= W163), K174 (= K187), S176 (≠ A189), E177 (= E190), R206 (≠ E220), G207 (= G221), G211 (= G225), Q212 (≠ R226), S228 (= S242), A231 (≠ V245), K234 (≠ L248), I235 (≠ L249), N328 (≠ D341), R334 (≠ K347), F383 (= F396)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 97% coverage: 10:484/491 of query aligns to 2:474/486 of 4pxlA
- active site: N154 (= N164), K177 (= K187), E253 (= E263), C287 (= C297), E384 (= E394), D461 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I150 (= I160), V151 (≠ T161), P152 (= P162), W153 (= W163), K177 (= K187), E180 (= E190), G210 (= G221), G214 (= G225), A215 (≠ R226), F228 (= F239), G230 (= G241), S231 (= S242), V234 (= V245), E253 (= E263), G255 (= G265), C287 (= C297), Q334 (≠ A344), K337 (= K347), E384 (= E394), F386 (= F396)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 91% coverage: 37:484/491 of query aligns to 21:471/477 of 6j76A
- active site: N148 (= N164), E246 (= E263), C280 (= C297), E458 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I160), T145 (= T161), A146 (≠ P162), W147 (= W163), N148 (= N164), K171 (= K187), T173 (≠ A189), S174 (≠ E190), G204 (= G221), G208 (= G225), T223 (= T240), G224 (= G241), S225 (= S242), A228 (≠ V245), S231 (≠ L248), I232 (≠ L249), E246 (= E263), L247 (= L264), C280 (= C297), E381 (= E394), F383 (= F396), H447 (≠ F460)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 97% coverage: 10:484/491 of query aligns to 7:482/494 of 4pz2B
- active site: N159 (= N164), K182 (= K187), E258 (= E263), C292 (= C297), E392 (= E394), D469 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I155 (= I160), I156 (≠ T161), P157 (= P162), W158 (= W163), N159 (= N164), M164 (= M169), K182 (= K187), A184 (= A189), E185 (= E190), G215 (= G221), G219 (= G225), F233 (= F239), T234 (= T240), G235 (= G241), S236 (= S242), V239 (= V245), E258 (= E263), L259 (= L264), C292 (= C297), E392 (= E394), F394 (= F396)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
39% identity, 93% coverage: 31:488/491 of query aligns to 18:474/476 of 5x5uA
- active site: N151 (= N164), K174 (= K187), E249 (= E263), C283 (= C297), E380 (= E394), E457 (= E471)
- binding glycerol: G19 (= G32)
- binding nicotinamide-adenine-dinucleotide: P149 (= P162), P207 (≠ G221), A208 (= A222), S211 (≠ G225), G227 (= G241), S228 (= S242), V231 (= V245), R329 (≠ H343), R330 (≠ A344), E380 (= E394), F382 (= F396)
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
39% identity, 93% coverage: 31:488/491 of query aligns to 18:474/476 of 5x5tA
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)
38% identity, 98% coverage: 4:484/491 of query aligns to 28:507/518 of O94788
- E50 (≠ S26) to G: in dbSNP:rs34266719
- A110 (≠ H87) to V: in dbSNP:rs35365164
- Q182 (≠ T159) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 161:163) binding
- KPAE 210:213 (= KPAE 187:190) binding
- STE 264:266 (= STE 242:244) binding
- C320 (= C297) active site, Nucleophile
- R347 (≠ L324) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ T325) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ HAIDK 343:347) binding
- A383 (= A360) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E394) binding
- E436 (≠ A413) to K: in dbSNP:rs34744827
- S461 (≠ A438) to Y: in DIH4; decreased retinoic acid biosynthetic process
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, 98% coverage: 4:484/491 of query aligns to 28:507/518 of Q63639
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
38% identity, 98% coverage: 4:484/491 of query aligns to 2:481/492 of 6b5hA
- active site: N161 (= N164), E260 (= E263), C294 (= C297), E468 (= E471)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ E115), G116 (≠ A119), F162 (= F165), W169 (≠ R172), Q284 (= Q287), F288 (≠ R291), T295 (≠ V298), N449 (≠ R452), L451 (≠ S454), N452 (≠ S455), F457 (= F460)
- binding nicotinamide-adenine-dinucleotide: I157 (= I160), I158 (≠ T161), W160 (= W163), N161 (= N164), K184 (= K187), G217 (= G221), G221 (= G225), F235 (= F239), T236 (= T240), G237 (= G241), S238 (= S242), V241 (= V245), E260 (= E263), L261 (= L264), C294 (= C297), 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)
38% identity, 98% coverage: 4:484/491 of query aligns to 2:481/492 of 6b5gA
- active site: N161 (= N164), E260 (= E263), C294 (= C297), E468 (= E471)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F165), L165 (≠ S168), W169 (≠ R172), F288 (≠ R291), C293 (≠ T296), C294 (= C297), T295 (≠ V298), N449 (≠ R452), L451 (≠ S454)
- binding nicotinamide-adenine-dinucleotide: I157 (= I160), I158 (≠ T161), P159 (= P162), W160 (= W163), N161 (= N164), M166 (= M169), K184 (= K187), E187 (= E190), G217 (= G221), G221 (= G225), F235 (= F239), T236 (= T240), G237 (= G241), S238 (= S242), V241 (= V245), E260 (= E263), L261 (= L264), C294 (= C297), E391 (= E394), F393 (= F396)
Query Sequence
>SM_b21185 SM_b21185 succinate-semialdehyde dehydrogenase (NAD(P)+) protein
MALTPALTRHIRRPKIFASLDEVTRSSGQPAGPVFDVSNPSTGELLATLPDMGIDDARTA
IDAAALAQPLWAGKPAKDRSIILRRWHDLIVEHADDLAAILTAEMGKPVGEAKGEVLHAA
SYVEWYAEEAKRVYGETFPAPANDRRMLVIKQPVGVVGTITPWNFPASMVARKISPALAA
GCTIVLKPAEQTPLVAGAMFVLAEKAGFPEGVLNLLYASEGAPIGRELCGNPKVRKISFT
GSTEVGRLLMRQCSDQIKKVSLELGGNAPFIVFDDADIDEAVDGAVQAKFRNAGQTCVSA
NRIYVQSAVHDAFAEKFVTRVRELTVGDGFAPDVAIGPMIDAHAIDKIEAHVADAVAKGA
QVRSGGSRIGTTGTFFEPTVLTGISHDMRIAQEETFGPIAPIIRFETAEQVVAEANDTIY
GLAAYFYAENLKRVWHVAEALEYGMVGINTGRMSSEAAPFGGIKQSGIGREGSRHGLEDY
LEMKYLCMGNI
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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