SitesBLAST
Comparing H281DRAFT_06351 FitnessBrowser__Burk376:H281DRAFT_06351 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)
55% identity, 99% coverage: 3:487/491 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
55% identity, 98% coverage: 5:487/491 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (= E260), C288 (= C294), E385 (= E392), E462 (= E469)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P157), W155 (= W158), K179 (= K182), A181 (= A184), S182 (≠ E185), A212 (≠ R215), G216 (≠ A223), G232 (= G238), S233 (= S239), I236 (≠ V242), C288 (= C294), K338 (= K344), E385 (= E392), F387 (= F394)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
51% identity, 99% coverage: 4:489/491 of query aligns to 1:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I155), T153 (= T156), P154 (= P157), K179 (= K182), A212 (≠ S214), K213 (≠ R215), F230 (= F236), T231 (= T237), G232 (= G238), S233 (= S239), V236 (= V242), W239 (≠ H245), G256 (= G262)
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, 98% coverage: 10:489/491 of query aligns to 58:535/535 of P51649
- C93 (≠ S47) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G130) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P134) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ Q136) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R167) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C177) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 182:185) binding
- T233 (= T187) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A191) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N209) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ V222) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 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 (= C296) 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 (= V359) to I: in dbSNP:rs143741652
- G409 (= G362) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S452) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G487) 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, 98% coverage: 10:489/491 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
50% identity, 98% coverage: 10:489/491 of query aligns to 8:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 95% coverage: 16:482/491 of query aligns to 5:471/477 of 6j76A
- active site: N148 (= N159), E246 (= E260), C280 (= C294), E458 (= E469)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I155), T145 (= T156), A146 (≠ P157), W147 (= W158), N148 (= N159), K171 (= K182), T173 (≠ A184), S174 (≠ E185), G204 (≠ S214), G208 (= G218), T223 (= T237), G224 (= G238), S225 (= S239), A228 (≠ V242), S231 (≠ H245), I232 (≠ L246), E246 (= E260), L247 (= L261), C280 (= C294), E381 (= E392), F383 (= F394), H447 (≠ F458)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 96% coverage: 16:485/491 of query aligns to 8:473/476 of 5x5uA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E380 (= E392), E457 (= E469)
- binding glycerol: D15 (≠ A23), A16 (= A24), A17 (= A25), G19 (= G27)
- binding nicotinamide-adenine-dinucleotide: P149 (= P157), P207 (≠ R215), A208 (≠ I219), S211 (≠ V222), G227 (= G238), S228 (= S239), V231 (= V242), R329 (= R340), R330 (≠ A341), E380 (= E392), F382 (= F394)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 96% coverage: 16:485/491 of query aligns to 8:473/476 of 5x5tA
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
41% identity, 95% coverage: 16:482/491 of query aligns to 14:482/494 of 4pz2B
- active site: N159 (= N159), K182 (= K182), E258 (= E260), C292 (= C294), E392 (= E392), D469 (≠ E469)
- binding nicotinamide-adenine-dinucleotide: I155 (= I155), I156 (≠ T156), P157 (= P157), W158 (= W158), N159 (= N159), M164 (= M164), K182 (= K182), A184 (= A184), E185 (= E185), G215 (= G218), G219 (≠ V222), F233 (= F236), T234 (= T237), G235 (= G238), S236 (= S239), V239 (= V242), E258 (= E260), L259 (= L261), C292 (= C294), E392 (= E392), F394 (= F394)
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)
38% identity, 95% coverage: 16:482/491 of query aligns to 23:489/501 of Q56YU0
- G152 (≠ M142) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A409) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
39% identity, 95% coverage: 16:482/491 of query aligns to 10:477/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 156:159) binding
- K162 (= K168) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 182:185) binding
- G209 (≠ R215) binding
- GTST 230:233 (≠ STPV 239:242) binding
- E252 (= E260) active site, Proton acceptor
- C286 (= C294) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E392) binding
- E464 (= E469) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 95% coverage: 16:482/491 of query aligns to 9:476/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E392), E463 (= E469)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I155), G149 (≠ T156), W151 (= W158), N152 (= N159), K175 (= K182), E178 (= E185), G208 (≠ R215), G212 (≠ A223), F226 (= F236), T227 (= T237), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (vs. gap), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E392), F388 (= F394)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 95% coverage: 16:482/491 of query aligns to 9:476/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E392), E463 (= E469)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ T156), W151 (= W158), N152 (= N159), K175 (= K182), S177 (≠ A184), E178 (= E185), G208 (≠ R215), G212 (≠ A223), F226 (= F236), T227 (= T237), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (vs. gap), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E392), F388 (= F394)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 95% coverage: 16:482/491 of query aligns to 9:476/489 of 2wmeA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E392), E463 (= E469)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T156), W151 (= W158), K175 (= K182), S177 (≠ A184), E178 (= E185), G208 (≠ R215), G212 (≠ A223), F226 (= F236), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (vs. gap)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 97% coverage: 8:482/491 of query aligns to 14:484/491 of 5gtlA
- active site: N165 (= N159), K188 (= K182), E263 (= E260), C297 (= C294), E394 (= E392), E471 (= E469)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I155), P163 (= P157), K188 (= K182), A190 (= A184), E191 (= E185), Q192 (≠ D186), G221 (= G218), G225 (≠ V222), G241 (= G238), S242 (= S239), T245 (≠ V242), L264 (= L261), C297 (= C294), E394 (= E392), F396 (= F394)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 97% coverage: 8:482/491 of query aligns to 14:484/491 of 5gtkA
- active site: N165 (= N159), K188 (= K182), E263 (= E260), C297 (= C294), E394 (= E392), E471 (= E469)
- binding nicotinamide-adenine-dinucleotide: I161 (= I155), I162 (≠ T156), P163 (= P157), W164 (= W158), K188 (= K182), E191 (= E185), G221 (= G218), G225 (≠ V222), A226 (= A223), F239 (= F236), G241 (= G238), S242 (= S239), T245 (≠ V242), Y248 (≠ H245), L264 (= L261), C297 (= C294), Q344 (≠ A341), R347 (≠ K344), E394 (= E392), F396 (= F394)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 95% coverage: 16:482/491 of query aligns to 9:474/486 of 4pxlA
- active site: N154 (= N159), K177 (= K182), E253 (= E260), C287 (= C294), E384 (= E392), D461 (≠ E469)
- binding nicotinamide-adenine-dinucleotide: I150 (= I155), V151 (≠ T156), P152 (= P157), W153 (= W158), K177 (= K182), E180 (= E185), G210 (≠ R215), G214 (≠ I219), A215 (≠ E220), F228 (= F236), G230 (= G238), S231 (= S239), V234 (= V242), E253 (= E260), G255 (= G262), C287 (= C294), Q334 (≠ A341), K337 (= K344), E384 (= E392), F386 (= F394)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 97% coverage: 16:491/491 of query aligns to 13:494/505 of O24174
- N164 (= N159) 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 (≠ R167) 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.
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)
36% identity, 97% coverage: 16:491/491 of query aligns to 11:489/497 of P17202
- I28 (≠ T33) binding
- D96 (≠ E99) binding
- SPW 156:158 (≠ TPW 156:158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R167) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 182:185) binding
- L186 (≠ D186) binding
- SSAT 236:239 (≠ STPV 239:242) binding
- V251 (≠ L254) binding in other chain
- L258 (= L261) binding
- W285 (≠ R288) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E392) binding
- A441 (≠ V443) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S452) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F458) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K462) binding
Query Sequence
>H281DRAFT_06351 FitnessBrowser__Burk376:H281DRAFT_06351
MSLALTRNELIRPLNFIGGKWIAAANGARFPVTNPATGDTIVEVANSSAADARAATDAAA
SALPAWRGKLPRERAEILRRWHALIVENTEDLAKLMSTEQGKPLAESRGEVAYGASYVAW
FADEATRIYGDIIPQQQRGKRMSAVKEAIGIVAAITPWNFPLAMIARKIAPALAAGCTVV
AKPAEDTPLTALALAALAQEAGVPDGVLNMLSASRDQGIEAVADWLADARVRKITFTGST
PVGKHLARESAATLKKLSLELGGNAPFIVFDDADLDAAVTGLMAAKFRNGGQTCVCPNRV
YVQAGVYERFADLLAKRVAALKVAPATDPSAQIGPMINERAIDKIARHVEDAVKQGAKVL
TGGKRLTELGPNYYAPTVLTDANDGMLVCCEETFGPVAPLFRFSDEAEAVRLANDTPFGL
AAYFFTQDVRRIDRVATRLEAGVIGINEGAVSSEVAPFGGVKESGYGREGSKYGLDDYLS
IKYLCQGGFDQ
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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