SitesBLAST
Comparing HSERO_RS05395 FitnessBrowser__HerbieS:HSERO_RS05395 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, 99% coverage: 2:482/484 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
70% identity, 99% coverage: 3:482/484 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E256), C288 (= C290), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P156), W155 (= W157), K179 (= K181), A181 (= A183), S182 (≠ E184), A212 (≠ P214), G216 (= G218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C290), K338 (= K340), E385 (= E387), F387 (= F389)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
64% identity, 99% coverage: 4:484/484 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I154), T153 (= T155), P154 (= P156), K179 (= K181), A212 (≠ P214), K213 (= K215), F230 (= F232), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), W239 (≠ L241), G256 (= G258)
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)
59% identity, 99% coverage: 8:484/484 of query aligns to 57:535/535 of P51649
- C93 (≠ M46) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G129) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P133) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P135) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R166) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C176) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 181:184) binding
- T233 (= T186) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A190) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S208) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G218) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTGVG 234:239) binding
- R334 (= R284) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N285) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C290) modified: Disulfide link with 342, In inhibited form
- C342 (= C292) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ Q321) natural variant: N -> S
- P382 (= P331) to L: in SSADHD; 2% of activity
- V406 (= V355) to I: in dbSNP:rs143741652
- G409 (= G358) 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)
59% identity, 99% coverage: 8:484/484 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
59% identity, 99% coverage: 8:484/484 of query aligns to 7:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 97% coverage: 13:481/484 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (= D22), A16 (= A23), A17 (≠ D24), G19 (= G26)
- binding nicotinamide-adenine-dinucleotide: P149 (= P156), P207 (= P214), A208 (≠ K215), S211 (≠ G218), G227 (= G234), S228 (= S235), V231 (= V238), R329 (≠ Q336), R330 (≠ A337), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 97% coverage: 13:481/484 of query aligns to 6:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 95% coverage: 13:474/484 of query aligns to 3:468/477 of 6j76A
- active site: N148 (= N158), E246 (= E256), C280 (= C290), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I154), T145 (= T155), A146 (≠ P156), W147 (= W157), N148 (= N158), K171 (= K181), T173 (≠ A183), S174 (≠ E184), G204 (≠ P214), G208 (= G218), T223 (= T233), G224 (= G234), S225 (= S235), A228 (≠ V238), S231 (≠ L241), I232 (≠ L242), E246 (= E256), L247 (= L257), C280 (= C290), E381 (= E387), F383 (= F389), H447 (≠ F453)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 96% coverage: 15:481/484 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E381 (= E387), A458 (≠ E464)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y112), F152 (= F159), N284 (≠ V291), F312 (≠ V319), G313 (= G320), R318 (≠ E325), D320 (vs. gap), I321 (≠ V327), A322 (≠ T328), Y362 (≠ F368), F440 (≠ I446), F440 (≠ I446), E441 (≠ S447)
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, 96% coverage: 15:481/484 of query aligns to 10:477/479 of P25553
- L150 (≠ T155) binding
- R161 (= R166) binding
- KPSE 176:179 (≠ KPAE 181:184) binding
- F180 (≠ A185) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ G219) binding
- S230 (= S235) binding
- E251 (= E256) binding
- N286 (≠ V291) 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 (≠ K340) binding
- E443 (≠ S447) binding
- H449 (≠ F453) 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)
37% identity, 98% coverage: 10:481/484 of query aligns to 3:475/477 of 2impA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E381 (= E387), A458 (≠ E464)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (= W157), K174 (= K181), E177 (= E184), F178 (≠ A185), G207 (≠ P214), G211 (= G218), Q212 (≠ G219), S228 (= S235), A231 (≠ V238), K234 (≠ L241), R334 (≠ K340)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 98% coverage: 10:481/484 of query aligns to 3:475/477 of 2iluA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E381 (= E387), A458 (≠ E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (= W157), K174 (= K181), S176 (≠ A183), E177 (= E184), R206 (≠ T213), G207 (≠ P214), G211 (= G218), Q212 (≠ G219), S228 (= S235), A231 (≠ V238), K234 (≠ L241), I235 (≠ L242), N328 (= N334), R334 (≠ K340), F383 (= F389)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
37% identity, 96% coverage: 15:477/484 of query aligns to 26:491/503 of O14293
- S248 (= S235) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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, 99% coverage: 4:481/484 of query aligns to 12:493/501 of Q56YU0
- G152 (≠ I141) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V404) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
37% identity, 96% coverage: 13:477/484 of query aligns to 19:492/498 of 4go2A
- active site: N170 (= N158), K193 (= K181), E269 (= E256), C303 (= C290), E400 (= E387), D479 (≠ E464)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I154), I167 (≠ T155), P168 (= P156), W169 (= W157), K193 (= K181), A195 (= A183), Q196 (≠ E184), S225 (≠ T213), G226 (≠ P214), G230 (= G218), Q231 (≠ G219), F244 (= F232), G246 (= G234), S247 (= S235), V250 (= V238), I254 (≠ L242), E269 (= E256), G271 (= G258), C303 (= C290), E400 (= E387), F402 (= F389)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
37% identity, 96% coverage: 13:477/484 of query aligns to 19:492/498 of 2o2rA
- active site: N170 (= N158), K193 (= K181), E269 (= E256), C303 (= C290), E400 (= E387), D479 (≠ E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I154), I167 (≠ T155), W169 (= W157), K193 (= K181), A195 (= A183), Q196 (≠ E184), S225 (≠ T213), G226 (≠ P214), G230 (= G218), Q231 (≠ G219), F244 (= F232), S247 (= S235), V250 (= V238), I254 (≠ L242)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
37% identity, 96% coverage: 13:477/484 of query aligns to 104:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K181), S310 (≠ T213), G311 (≠ P214), G315 (= G218), G331 (= G234), S332 (= S235), V335 (= V238)
- binding 4'-phosphopantetheine: K201 (≠ R107), F382 (≠ R284), N387 (≠ T289), C388 (= C290), N545 (≠ L445)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 97% coverage: 8:477/484 of query aligns to 6:485/505 of O24174
- N164 (= N158) 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 (≠ R166) 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.
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
37% identity, 96% coverage: 13:477/484 of query aligns to 423:896/902 of P28037
- IPW 571:573 (≠ TPW 155:157) binding
- KPAQ 597:600 (≠ KPAE 181:184) binding
- GSLVGQ 630:635 (≠ PKGIGG 214:219) binding
- GS 650:651 (= GS 234:235) binding
- E673 (= E256) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 256:257) binding
- C707 (= C290) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K340) binding
- ESF 804:806 (≠ ETF 387:389) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
Query Sequence
>HSERO_RS05395 FitnessBrowser__HerbieS:HSERO_RS05395
MLQLKDPALLRQQAFVNGQWCDADQGERLAVHNPANGELLGHVPLMGAAETRRAIEAANA
AWPAWKKKTAKERSAILRRWYELMLANTDDLALIMTAEQGKPLAEARGEIGYAASFIEWF
AEEGKRTYGDTIPSPSPSNRIVVIKEAIGVCAAITPWNFPAAMITRKAGPALAAGCPMVL
KPAEATPFSALALAVLAERAGIPAGVFSVVTGTPKGIGGEMTSNPIVRKISFTGSTGVGK
LLMQQSASSIKKLSLELGGNAPFIVFDDADLDAAVEGAIASKYRNAGQTCVCANRIYVQD
GVYDAFAAKLVEAVKKFKVGQGTEEGVTQGPLINEQAVQKVEQHVADAVAKGARVLLGGK
RHALGHSFFEPTVLADVTPAMQVAREETFGPMAPLFRFKTDEEVLALANDTEFGLASYFY
SRDIGRIWRVAEGLESGMVGINTGLISNEVAPFGGVKQSGLGREGSHYGIDDYLVVKYLC
MGGI
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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