SitesBLAST
Comparing SMa0260 FitnessBrowser__Smeli:SMa0260 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)
48% identity, 97% coverage: 12:485/487 of query aligns to 4:479/481 of 3jz4A
- active site: N156 (= N161), K179 (= K184), E254 (= E260), C288 (= C294), E385 (= E391), E462 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P159), W155 (= W160), K179 (= K184), A181 (= A186), S182 (= S187), A212 (≠ P218), G216 (≠ T222), G232 (= G238), S233 (= S239), I236 (≠ V242), C288 (= C294), K338 (= K344), E385 (= E391), F387 (= F393)
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)
48% identity, 97% coverage: 12:485/487 of query aligns to 5:480/482 of P25526
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)
48% identity, 95% coverage: 21:482/487 of query aligns to 64:529/535 of P51649
- C93 (≠ A49) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G132) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (= H136) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P138) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R169) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C179) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 184:187) binding
- T233 (= T189) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A193) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N211) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ T222) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTGVG 238:243) binding
- R334 (= R288) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N289) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C294) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A296) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P325) natural variant: N -> S
- P382 (= P335) to L: in SSADHD; 2% of activity
- V406 (≠ A359) to I: in dbSNP:rs143741652
- G409 (= G362) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S451) 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)
48% identity, 95% coverage: 21:482/487 of query aligns to 14:479/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
48% identity, 95% coverage: 21:482/487 of query aligns to 14:479/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
47% identity, 97% coverage: 12:485/487 of query aligns to 4:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I157), T153 (= T158), P154 (= P159), K179 (= K184), A212 (≠ S216), K213 (≠ N217), F230 (= F236), T231 (= T237), G232 (= G238), S233 (= S239), V236 (= V242), W239 (≠ V245), G256 (= G262)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 96% coverage: 20:487/487 of query aligns to 4:477/477 of 6j76A
- active site: N148 (= N161), E246 (= E260), C280 (= C294), E458 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I157), T145 (= T158), A146 (≠ P159), W147 (= W160), N148 (= N161), K171 (= K184), T173 (≠ A186), S174 (= S187), G204 (= G220), G208 (vs. gap), T223 (= T237), G224 (= G238), S225 (= S239), A228 (≠ V242), S231 (≠ V245), I232 (≠ L246), E246 (= E260), L247 (= L261), C280 (= C294), E381 (= E391), F383 (= F393), H447 (≠ F457)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 96% coverage: 15:481/487 of query aligns to 20:491/503 of O14293
- S248 (= S239) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 95% coverage: 20:481/487 of query aligns to 8:474/486 of 4pxlA
- active site: N154 (= N161), K177 (= K184), E253 (= E260), C287 (= C294), E384 (= E391), D461 (≠ E468)
- binding nicotinamide-adenine-dinucleotide: I150 (= I157), V151 (≠ T158), P152 (= P159), W153 (= W160), K177 (= K184), E180 (≠ S187), G210 (≠ N217), G214 (≠ T222), A215 (≠ N223), F228 (= F236), G230 (= G238), S231 (= S239), V234 (= V242), E253 (= E260), G255 (= G262), C287 (= C294), Q334 (≠ A341), K337 (= K344), E384 (= E391), F386 (= F393)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 95% coverage: 20:481/487 of query aligns to 7:471/477 of 2opxA
- active site: N151 (= N161), K174 (= K184), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y115), F152 (= F162), N284 (≠ T295), F312 (≠ L323), G313 (= G324), R318 (≠ D328), D320 (≠ E330), I321 (≠ T331), A322 (≠ Q332), Y362 (≠ F372), F440 (≠ M450), F440 (≠ M450), E441 (≠ S451)
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)
37% identity, 95% coverage: 20:481/487 of query aligns to 7:471/477 of 2impA
- active site: N151 (= N161), K174 (= K184), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I157), L148 (≠ T158), P149 (= P159), W150 (= W160), K174 (= K184), E177 (≠ S187), F178 (≠ E188), G207 (≠ P218), G211 (≠ T222), Q212 (≠ N223), S228 (= S239), A231 (≠ V242), K234 (≠ V245), R334 (≠ K344)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 95% coverage: 20:481/487 of query aligns to 7:471/477 of 2iluA
- active site: N151 (= N161), K174 (= K184), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I157), L148 (≠ T158), P149 (= P159), W150 (= W160), K174 (= K184), S176 (≠ A186), E177 (≠ S187), R206 (≠ N217), G207 (≠ P218), G211 (≠ T222), Q212 (≠ N223), S228 (= S239), A231 (≠ V242), K234 (≠ V245), I235 (≠ L246), N328 (≠ T338), R334 (≠ K344), F383 (= F393)
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)
37% identity, 95% coverage: 20:481/487 of query aligns to 9:473/479 of P25553
- L150 (≠ T158) binding
- R161 (= R169) binding
- KPSE 176:179 (≠ KPAS 184:187) binding
- F180 (≠ E188) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ N223) binding
- S230 (= S239) binding
- E251 (= E260) binding
- N286 (≠ T295) 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 (≠ K344) binding
- E443 (≠ S451) binding
- H449 (≠ F457) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 96% coverage: 20:486/487 of query aligns to 19:489/491 of 5gtlA
- active site: N165 (= N161), K188 (= K184), E263 (= E260), C297 (= C294), E394 (= E391), E471 (= E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I157), P163 (= P159), K188 (= K184), A190 (= A186), E191 (≠ S187), Q192 (≠ E188), G221 (≠ N217), G225 (≠ T222), G241 (= G238), S242 (= S239), T245 (≠ V242), L264 (= L261), C297 (= C294), E394 (= E391), F396 (= F393)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 96% coverage: 20:486/487 of query aligns to 19:489/491 of 5gtkA
- active site: N165 (= N161), K188 (= K184), E263 (= E260), C297 (= C294), E394 (= E391), E471 (= E468)
- binding nicotinamide-adenine-dinucleotide: I161 (= I157), I162 (≠ T158), P163 (= P159), W164 (= W160), K188 (= K184), E191 (≠ S187), G221 (≠ N217), G225 (≠ T222), A226 (≠ N223), F239 (= F236), G241 (= G238), S242 (= S239), T245 (≠ V242), Y248 (≠ V245), L264 (= L261), C297 (= C294), Q344 (≠ A341), R347 (≠ K344), E394 (= E391), F396 (= F393)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 96% coverage: 13:481/487 of query aligns to 6:482/494 of 4pz2B
- active site: N159 (= N161), K182 (= K184), E258 (= E260), C292 (= C294), E392 (= E391), D469 (≠ E468)
- binding nicotinamide-adenine-dinucleotide: I155 (= I157), I156 (≠ T158), P157 (= P159), W158 (= W160), N159 (= N161), M164 (= M166), K182 (= K184), A184 (= A186), E185 (≠ S187), G215 (≠ N217), G219 (≠ T222), F233 (= F236), T234 (= T237), G235 (= G238), S236 (= S239), V239 (= V242), E258 (= E260), L259 (= L261), C292 (= C294), E392 (= E391), F394 (= F393)
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, 96% coverage: 20:485/487 of query aligns to 40:511/518 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)
36% identity, 95% coverage: 21:483/487 of query aligns to 21:491/505 of 4neaA
- active site: N166 (= N161), K189 (= K184), E264 (= E260), C298 (= C294), E399 (= E391), E476 (= E468)
- binding nicotinamide-adenine-dinucleotide: P164 (= P159), K189 (= K184), E192 (≠ S187), G222 (≠ N217), G226 (≠ T222), G242 (= G238), G243 (≠ S239), T246 (≠ V242), H249 (≠ V245), I250 (≠ L246), C298 (= C294), E399 (= E391), F401 (= F393)
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, 96% coverage: 20:485/487 of query aligns to 14:485/492 of 6b5hA
- active site: N161 (= N161), E260 (= E260), C294 (= C294), E468 (= E468)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G111), G116 (≠ Y115), F162 (= F162), W169 (≠ R169), Q284 (≠ I284), F288 (≠ R288), T295 (= T295), N449 (≠ L449), L451 (≠ S451), N452 (≠ D452), F457 (= F457)
- binding nicotinamide-adenine-dinucleotide: I157 (= I157), I158 (≠ T158), W160 (= W160), N161 (= N161), K184 (= K184), G217 (≠ N217), G221 (≠ T222), F235 (= F236), T236 (= T237), G237 (= G238), S238 (= S239), V241 (= V242), E260 (= E260), L261 (= L261), C294 (= C294), F393 (= F393)
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, 96% coverage: 20:485/487 of query aligns to 14:485/492 of 6b5gA
- active site: N161 (= N161), E260 (= E260), C294 (= C294), E468 (= E468)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F162), L165 (≠ A165), W169 (≠ R169), F288 (≠ R288), C293 (≠ A293), C294 (= C294), T295 (= T295), N449 (≠ L449), L451 (≠ S451)
- binding nicotinamide-adenine-dinucleotide: I157 (= I157), I158 (≠ T158), P159 (= P159), W160 (= W160), N161 (= N161), M166 (= M166), K184 (= K184), E187 (≠ S187), G217 (≠ N217), G221 (≠ T222), F235 (= F236), T236 (= T237), G237 (= G238), S238 (= S239), V241 (= V242), E260 (= E260), L261 (= L261), C294 (= C294), E391 (= E391), F393 (= F393)
Query Sequence
>SMa0260 FitnessBrowser__Smeli:SMa0260
MTFHAKFSGYADPALHAAGLYIGGKWQSGSGITVLDPSTGNLLAEVADASIEDAQRAVDA
ADAAAAGWRATPARQRSEILRRWYQLMTQHAEELATLIALENGKALADARGEVAYAAEFF
RWYAEEATRIPGEFRHTPSGSHNILVDHEPIGIAVLITPWNFPAAMATRKIGPALAAGCT
VILKPASETPLTAYAMARLGEEAGVPPGVVNVLTTSNPGGITNAMLADPRVRKLSFTGST
GVGRVLLAEAAKSVVSCSMELGGNAPFIVFDDADLEVALDGAMIAKMRNAGEACTAANRF
YVQAGIHDAFVAGLTARMKSLKLGPGYDPETQCGPMITQNAVRKIDRLVSEALAAGARAT
TGGKPLTENGYFYPPTVLENVPVNASIAREEIFGPVAPVYKFESDDEAIRLANNTEYGLA
AYIYSRDLKRAMKVGKRIETGMLGINRGLMSDPAAPFGGVKQSGLGREGGVTGILEFMEP
KYFAVDY
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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