SitesBLAST
Comparing RR42_RS26645 FitnessBrowser__Cup4G11:RR42_RS26645 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)
53% identity, 99% coverage: 6:492/494 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
53% identity, 98% coverage: 8:492/494 of query aligns to 2:481/481 of 3jz4A
- active site: N156 (= N162), K179 (= K185), E254 (= E263), C288 (= C297), E385 (= E396), E462 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P160), W155 (= W161), K179 (= K185), A181 (= A187), S182 (≠ E188), A212 (≠ R218), G216 (≠ V225), G232 (= G241), S233 (= S242), I236 (≠ V245), C288 (= C297), K338 (= K347), E385 (= E396), F387 (= F398)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
54% identity, 98% coverage: 8:491/494 of query aligns to 2:480/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I158), T153 (= T159), P154 (= P160), K179 (= K185), A212 (= A219), K213 (= K220), F230 (= F239), T231 (= T240), G232 (= G241), S233 (= S242), V236 (= V245), W239 (≠ H248), 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)
52% identity, 98% coverage: 12:493/494 of query aligns to 57:535/535 of P51649
- C93 (≠ S50) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G133) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ A137) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ S139) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R170) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C180) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 185:188) binding
- T233 (= T190) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A194) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N212) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ V225) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 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 (= C299) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P328) 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 (≠ A456) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G491) 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)
51% identity, 98% coverage: 12:493/494 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
51% identity, 98% coverage: 12:493/494 of query aligns to 7:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 95% coverage: 20:486/494 of query aligns to 6:471/477 of 6j76A
- active site: N148 (= N162), E246 (= E263), C280 (= C297), E458 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I158), T145 (= T159), A146 (≠ P160), W147 (= W161), N148 (= N162), K171 (= K185), T173 (≠ A187), S174 (≠ E188), G204 (≠ A219), G208 (≠ V225), T223 (= T240), G224 (= G241), S225 (= S242), A228 (≠ V245), S231 (≠ H248), I232 (≠ L249), E246 (= E263), L247 (= L264), C280 (= C297), E381 (= E396), F383 (= F398), H447 (≠ F462)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 96% coverage: 16:489/494 of query aligns to 5:473/476 of 5x5uA
- active site: N151 (= N162), K174 (= K185), E249 (= E263), C283 (= C297), E380 (= E396), E457 (= E473)
- binding glycerol: D15 (≠ A26), A16 (= A27), A17 (≠ H28), G19 (= G30)
- binding nicotinamide-adenine-dinucleotide: P149 (= P160), P207 (= P222), A208 (= A223), S211 (≠ D226), G227 (= G241), S228 (= S242), V231 (= V245), R329 (= R343), R330 (≠ A344), E380 (= E396), F382 (= F398)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 96% coverage: 16:489/494 of query aligns to 5:473/476 of 5x5tA
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)
38% identity, 98% coverage: 5:488/494 of query aligns to 2:475/479 of P25553
- L150 (≠ T159) binding
- R161 (= R170) binding
- KPSE 176:179 (≠ KPAE 185:188) binding
- F180 (≠ D189) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D226) 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 (≠ A456) binding
- H449 (≠ F462) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 98% coverage: 6:488/494 of query aligns to 1:473/477 of 2opxA
- active site: N151 (= N162), K174 (= K185), E249 (= E263), C283 (= C297), E381 (= E396), A458 (≠ E473)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y116), F152 (= F163), N284 (≠ V298), F312 (≠ V326), G313 (= G327), R318 (≠ E331), D320 (≠ A333), I321 (≠ S334), A322 (≠ Q335), Y362 (= Y377), F440 (≠ I455), F440 (≠ I455), E441 (≠ A456)
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, 98% coverage: 6:488/494 of query aligns to 1:473/477 of 2impA
- active site: N151 (= N162), K174 (= K185), E249 (= E263), C283 (= C297), E381 (= E396), A458 (≠ E473)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I158), L148 (≠ T159), P149 (= P160), W150 (= W161), K174 (= K185), E177 (= E188), F178 (≠ D189), G207 (≠ A219), G211 (≠ V225), Q212 (≠ D226), S228 (= S242), A231 (≠ V245), K234 (≠ H248), R334 (≠ K347)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 98% coverage: 6:488/494 of query aligns to 1:473/477 of 2iluA
- active site: N151 (= N162), K174 (= K185), E249 (= E263), C283 (= C297), E381 (= E396), A458 (≠ E473)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I158), L148 (≠ T159), P149 (= P160), W150 (= W161), K174 (= K185), S176 (≠ A187), E177 (= E188), R206 (= R218), G207 (≠ A219), G211 (≠ V225), Q212 (≠ D226), S228 (= S242), A231 (≠ V245), K234 (≠ H248), I235 (≠ L249), N328 (= N341), R334 (≠ K347), F383 (= F398)
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)
36% identity, 98% coverage: 11:492/494 of query aligns to 15:495/501 of Q56YU0
- G152 (≠ M145) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V413) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 97% coverage: 12:490/494 of query aligns to 6:489/505 of O24174
- N164 (= N162) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ R170) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
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, 96% coverage: 14:489/494 of query aligns to 16:492/505 of 4neaA
- active site: N166 (= N162), K189 (= K185), E264 (= E263), C298 (= C297), E399 (= E396), E476 (= E473)
- binding nicotinamide-adenine-dinucleotide: P164 (= P160), K189 (= K185), E192 (= E188), G222 (≠ R218), G226 (≠ V225), G242 (= G241), G243 (≠ S242), T246 (≠ V245), H249 (= H248), I250 (≠ L249), C298 (= C297), E399 (= E396), F401 (= F398)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
38% identity, 98% coverage: 11:492/494 of query aligns to 6:488/494 of 4pz2B
- active site: N159 (= N162), K182 (= K185), E258 (= E263), C292 (= C297), E392 (= E396), D469 (≠ E473)
- binding nicotinamide-adenine-dinucleotide: I155 (= I158), I156 (≠ T159), P157 (= P160), W158 (= W161), N159 (= N162), M164 (= M167), K182 (= K185), A184 (= A187), E185 (= E188), G215 (≠ T221), G219 (≠ V225), F233 (= F239), T234 (= T240), G235 (= G241), S236 (= S242), V239 (= V245), E258 (= E263), L259 (= L264), C292 (= C297), E392 (= E396), F394 (= F398)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
37% identity, 97% coverage: 16:492/494 of query aligns to 6:480/486 of 4pxlA
- active site: N154 (= N162), K177 (= K185), E253 (= E263), C287 (= C297), E384 (= E396), D461 (≠ E473)
- binding nicotinamide-adenine-dinucleotide: I150 (= I158), V151 (≠ T159), P152 (= P160), W153 (= W161), K177 (= K185), E180 (= E188), G210 (≠ R218), G214 (≠ P222), A215 (= A223), F228 (= F239), G230 (= G241), S231 (= S242), V234 (= V245), E253 (= E263), G255 (= G265), C287 (= C297), Q334 (≠ A344), K337 (= K347), E384 (= E396), F386 (= F398)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
39% identity, 93% coverage: 30:488/494 of query aligns to 16:470/474 of P77674
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
35% identity, 96% coverage: 14:488/494 of query aligns to 1:473/494 of 5izdA
- active site: N149 (= N162), K172 (= K185), E247 (= E263), C281 (= C297), E381 (= E396), E458 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I158), T146 (= T159), W148 (= W161), K172 (= K185), P173 (= P186), S174 (≠ A187), S175 (≠ E188), R204 (≠ K220), G205 (≠ T221), G209 (≠ V225), D210 (= D226), G225 (= G241), S226 (= S242), T229 (≠ V245)
Query Sequence
>RR42_RS26645 FitnessBrowser__Cup4G11:RR42_RS26645
MTSTSLPLTHPALLRTSNLIGQAWSAAHTGHRLDVTNPATNTVFACVPDSDARDASQATD
AAAAAFPAWSRRTARDRAQIIKRWHALILEHQEDLARIISTEQGKPIKEARGEVLYGASY
VEWFAEEATRISGEIVAESVPGRKMLVLKEPVGVVAAITPWNFPLAMIARKIAPALAAGC
TVVAKPAEDTPLTALALVYLAQQAGLPAGVLNIVTASRAKTPAVVDAWLADSRVRKITFT
GSTPVGKHLARESAGTLKKLSLELGGNAPFIVFDDADIDAAVDGLMASKFRNGGQTCVCP
NRVYVQAGVHDYFVARLSQRVAALQVGPATEDASQIGPMINARAVEKIARHVADAVAKGA
VVMTGGERVRLADGPHYYAPTVLTNATPQMALSCEETFGPVAAVFRFTDEAEVIRDANDT
PFGLAAYFYSNDVRRIWRVAQALETGIVGVNEGAIASEAAPFGGVKESGYGREGSRHGLD
DYMHTKYICQGLLG
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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