SitesBLAST
Comparing RR42_RS26155 FitnessBrowser__Cup4G11:RR42_RS26155 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)
65% identity, 99% coverage: 5:484/487 of query aligns to 1:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
65% identity, 98% coverage: 7:484/487 of query aligns to 2:479/481 of 3jz4A
- active site: N156 (= N161), K179 (= K184), E254 (= E259), C288 (= C293), E385 (= E390), E462 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P159), W155 (= W160), K179 (= K184), A181 (= A186), S182 (≠ E187), A212 (≠ P217), G216 (= G221), G232 (= G237), S233 (= S238), I236 (= I241), C288 (= C293), K338 (= K343), E385 (= E390), F387 (= F392)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
62% identity, 98% coverage: 7:484/487 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I157), T153 (= T158), P154 (= P159), K179 (= K184), A212 (≠ P217), K213 (≠ V218), F230 (= F235), T231 (= T236), G232 (= G237), S233 (= S238), V236 (≠ I241), W239 (≠ L244), G256 (= G261)
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, 97% coverage: 12:483/487 of query aligns to 58:531/535 of P51649
- C93 (= C49) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G132) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ S136) 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 (= KPAE 184:187) binding
- T233 (= T189) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A193) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ Q211) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G221) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTAIG 237:242) binding
- R334 (= R287) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N288) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C293) modified: Disulfide link with 342, In inhibited form
- C342 (= C295) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ H324) natural variant: N -> S
- P382 (= P334) to L: in SSADHD; 2% of activity
- V406 (= V358) to I: in dbSNP:rs143741652
- G409 (= G361) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S450) 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, 97% coverage: 12:483/487 of query aligns to 8:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 97% coverage: 12:483/487 of query aligns to 8:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
42% identity, 97% coverage: 15:486/487 of query aligns to 5:476/476 of 5x5uA
- active site: N151 (= N161), K174 (= K184), E249 (= E259), C283 (= C293), E380 (= E390), E457 (= E467)
- binding glycerol: D15 (≠ G25), A16 (= A26), A17 (= A27), G19 (= G29)
- binding nicotinamide-adenine-dinucleotide: P149 (= P159), P207 (= P217), A208 (≠ V218), S211 (≠ G221), G227 (= G237), S228 (= S238), V231 (≠ I241), R329 (≠ D339), R330 (≠ A340), E380 (= E390), F382 (= F392)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
42% identity, 97% coverage: 15:486/487 of query aligns to 5:476/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 19:484/487 of query aligns to 6:475/477 of 6j76A
- active site: N148 (= N161), E246 (= E259), C280 (= C293), E458 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I157), T145 (= T158), A146 (≠ P159), W147 (= W160), N148 (= N161), K171 (= K184), T173 (≠ A186), S174 (≠ E187), G204 (≠ P217), G208 (= G221), T223 (= T236), G224 (= G237), S225 (= S238), A228 (≠ I241), S231 (≠ L244), I232 (≠ L245), E246 (= E259), L247 (= L260), C280 (= C293), E381 (= E390), F383 (= F392), H447 (≠ F456)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
36% identity, 97% coverage: 13:486/487 of query aligns to 3:477/477 of 2opxA
- active site: N151 (= N161), K174 (= K184), E249 (= E259), C283 (= C293), E381 (= E390), A458 (≠ E467)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y115), F152 (= F162), N284 (≠ V294), F312 (≠ P322), G313 (= G323), R318 (vs. gap), D320 (= D329), I321 (≠ V330), A322 (≠ T331), Y362 (≠ F371), F440 (≠ I449), F440 (≠ I449), E441 (≠ S450)
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)
36% identity, 97% coverage: 13:486/487 of query aligns to 3:477/477 of 2impA
- active site: N151 (= N161), K174 (= K184), E249 (= E259), C283 (= C293), E381 (= E390), A458 (≠ E467)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I157), L148 (≠ T158), P149 (= P159), W150 (= W160), K174 (= K184), E177 (= E187), F178 (≠ Q188), G207 (≠ P217), G211 (= G221), Q212 (≠ G222), S228 (= S238), A231 (≠ I241), K234 (≠ L244), R334 (≠ K343)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
36% identity, 97% coverage: 13:486/487 of query aligns to 3:477/477 of 2iluA
- active site: N151 (= N161), K174 (= K184), E249 (= E259), C283 (= C293), E381 (= E390), A458 (≠ E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I157), L148 (≠ T158), P149 (= P159), W150 (= W160), K174 (= K184), S176 (≠ A186), E177 (= E187), R206 (≠ D216), G207 (≠ P217), G211 (= G221), Q212 (≠ G222), S228 (= S238), A231 (≠ I241), K234 (≠ L244), I235 (≠ L245), N328 (≠ D337), R334 (≠ K343), F383 (= F392)
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, 97% coverage: 13:482/487 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N161), K189 (= K184), E264 (= E259), C298 (= C293), E399 (= E390), E476 (= E467)
- binding nicotinamide-adenine-dinucleotide: P164 (= P159), K189 (= K184), E192 (= E187), G222 (≠ P217), G226 (= G221), G242 (= G237), G243 (≠ S238), T246 (≠ I241), H249 (≠ L244), I250 (≠ L245), C298 (= C293), E399 (= E390), F401 (= F392)
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)
36% identity, 97% coverage: 13:486/487 of query aligns to 5:479/479 of P25553
- L150 (≠ T158) binding
- R161 (= R169) binding
- KPSE 176:179 (≠ KPAE 184:187) binding
- F180 (≠ Q188) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ G222) binding
- S230 (= S238) binding
- E251 (= E259) binding
- N286 (≠ V294) 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 (≠ K343) binding
- E443 (≠ S450) binding
- H449 (≠ F456) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
38% identity, 95% coverage: 18:480/487 of query aligns to 11:480/497 of P17202
- I28 (≠ H35) binding
- D96 (≠ E101) binding
- SPW 156:158 (≠ TPW 158:160) binding
- Y160 (≠ F162) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R169) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 184:187) binding
- L186 (≠ Q188) binding
- SSAT 236:239 (≠ STAI 238:241) binding
- V251 (= V253) binding in other chain
- L258 (= L260) binding
- W285 (≠ R287) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E390) binding
- A441 (≠ M441) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S450) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F456) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K460) binding
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: 6:484/487 of query aligns to 11:493/501 of Q56YU0
- G152 (≠ M144) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V407) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 96% coverage: 15:480/487 of query aligns to 6:474/486 of 4pxlA
- active site: N154 (= N161), K177 (= K184), E253 (= E259), C287 (= C293), E384 (= E390), D461 (≠ E467)
- binding nicotinamide-adenine-dinucleotide: I150 (= I157), V151 (≠ T158), P152 (= P159), W153 (= W160), K177 (= K184), E180 (= E187), G210 (≠ P217), G214 (= G221), A215 (≠ G222), F228 (= F235), G230 (= G237), S231 (= S238), V234 (≠ I241), E253 (= E259), G255 (= G261), C287 (= C293), Q334 (≠ A340), K337 (= K343), E384 (= E390), F386 (= F392)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 95% coverage: 18:480/487 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N161), K180 (= K184), E255 (= E259), A289 (≠ C293), E388 (= E390), E465 (= E467)
- binding 3-aminopropan-1-ol: C448 (≠ S450), W454 (≠ F456)
- binding nicotinamide-adenine-dinucleotide: I153 (= I157), S154 (≠ T158), P155 (= P159), W156 (= W160), N157 (= N161), M162 (= M166), K180 (= K184), S182 (≠ A186), E183 (= E187), G213 (≠ P217), G217 (= G221), A218 (≠ G222), T232 (= T236), G233 (= G237), S234 (= S238), T237 (≠ I241), E255 (= E259), L256 (= L260), A289 (≠ C293), E388 (= E390), F390 (= F392)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 95% coverage: 18:480/487 of query aligns to 20:484/491 of 5gtlA
- active site: N165 (= N161), K188 (= K184), E263 (= E259), C297 (= C293), E394 (= E390), E471 (= E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I157), P163 (= P159), K188 (= K184), A190 (= A186), E191 (= E187), Q192 (= Q188), G221 (≠ P217), G225 (= G221), G241 (= G237), S242 (= S238), T245 (≠ I241), L264 (= L260), C297 (= C293), E394 (= E390), F396 (= F392)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 95% coverage: 18:480/487 of query aligns to 20:484/491 of 5gtkA
- active site: N165 (= N161), K188 (= K184), E263 (= E259), C297 (= C293), E394 (= E390), E471 (= E467)
- binding nicotinamide-adenine-dinucleotide: I161 (= I157), I162 (≠ T158), P163 (= P159), W164 (= W160), K188 (= K184), E191 (= E187), G221 (≠ P217), G225 (= G221), A226 (≠ G222), F239 (= F235), G241 (= G237), S242 (= S238), T245 (≠ I241), Y248 (≠ L244), L264 (= L260), C297 (= C293), Q344 (≠ A340), R347 (≠ K343), E394 (= E390), F396 (= F392)
Query Sequence
>RR42_RS26155 FitnessBrowser__Cup4G11:RR42_RS26155
MGHTLTLQRPGLLRSACLIDGEWTGAAGGAVLMVHNPATHDVVGTVPRCGAAETRQAVEA
AARALPAWRDLTGKARAAVLRRWADLMLVHQEDLAQLMTAEQGKPLAEARGEIAYAASFL
EWFGEEAKRVDGDVLSSPRAGQKMLVLRQPVGVCAAITPWNFPAAMITRKAGPALAAGCT
MIVKPAEQTPLTALALAALAEEAGVPRGVLQVVTGDPVQIGGVLCESPVVRKLSFTGSTA
IGKLLMAQCAGTVKKLSLELGGNAPLIVFEDADLDRAVDGILASKFRNSGQTCVCANRIY
VHDAVYDEVASRLVRAVSALRPGHGIDSDVTQGPLIDADAVAKVESHIADALAHGARVLT
GGKRHALGGTFFEPTVVAGATAAMRVAREETFGPLAPLFRFKGDQEVIAMANDTESGLAA
YFFSKDMARVWRVAEALEYGMVGINTGLISNEVAPFGGVKQSGLGREGSSYGIDEYLEMK
YLCLEAG
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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