SitesBLAST
Comparing Ac3H11_2357 FitnessBrowser__acidovorax_3H11:Ac3H11_2357 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)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
49% identity, 93% coverage: 17:490/507 of query aligns to 10:485/491 of 4iymC
- active site: N153 (= N160), K176 (= K183), F250 (≠ M257), C284 (= C291), E386 (= E391), Q466 (≠ P471)
- binding nicotinamide-adenine-dinucleotide: I149 (= I156), T150 (= T157), P151 (= P158), F152 (= F159), N153 (= N160), F154 (= F161), K176 (= K183), K209 (≠ E216), V212 (= V219), F226 (= F233), V227 (= V234), G228 (= G235), S229 (= S236), I232 (≠ V239), G251 (≠ M258), C284 (= C291), E386 (= E391), F388 (= F393)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
49% identity, 94% coverage: 14:490/507 of query aligns to 5:479/484 of 1t90A
- active site: N151 (= N160), K174 (= K183), L248 (≠ M257), C282 (= C291), E380 (= E391), A460 (≠ P471)
- binding nicotinamide-adenine-dinucleotide: I147 (= I156), A148 (≠ T157), P149 (= P158), F150 (= F159), N151 (= N160), W159 (= W168), K174 (= K183), E177 (= E186), R178 (≠ Q187), H207 (≠ E216), V225 (= V234), G226 (= G235), S227 (= S236), V230 (= V239), L248 (≠ M257), T249 (≠ M258), C282 (= C291), E380 (= E391), F382 (= F393)
P42412 Malonate-semialdehyde dehydrogenase; MSA dehydrogenase; Methylmalonate-semialdehyde dehydrogenase; MMSA dehydrogenase; MMSDH; MSDH; EC 1.2.1.27 from Bacillus subtilis (strain 168) (see 3 papers)
49% identity, 94% coverage: 14:490/507 of query aligns to 7:481/487 of P42412
- C36 (≠ A43) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-160; A-287; A-351 and A-413.
- R107 (= R114) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T157) binding
- F152 (= F159) binding
- C160 (≠ L167) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-287; A-351 and A-413.
- K176 (= K183) binding
- E179 (= E186) binding
- R180 (≠ Q187) binding
- S229 (= S236) binding
- T251 (≠ M258) binding
- R283 (= R290) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ L294) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-351 and A-413.
- C351 (≠ L357) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-413.
- E382 (= E391) binding
- C413 (≠ A422) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
46% identity, 94% coverage: 13:490/507 of query aligns to 3:481/489 of 4zz7A
- active site: N149 (= N160), K172 (= K183), L246 (≠ M257), C280 (= C291), E382 (= E391), A462 (≠ P471)
- binding nicotinamide-adenine-dinucleotide: T146 (= T157), P147 (= P158), F148 (= F159), N149 (= N160), K172 (= K183), E175 (= E186), K205 (≠ E216), V208 (= V219), F222 (= F233), V223 (= V234), G224 (= G235), S225 (= S236), I228 (≠ V239), L246 (≠ M257), G247 (≠ M258), C280 (= C291), E382 (= E391), F384 (= F393)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
46% identity, 94% coverage: 14:490/507 of query aligns to 3:455/468 of 5tjrD
- active site: N144 (= N160), K167 (= K183), L241 (≠ M257), C270 (= C291), E356 (= E391), A436 (≠ P471)
- binding adenosine-5'-diphosphate: I140 (= I156), T141 (= T157), F143 (= F159), K167 (= K183), E170 (= E186), K200 (≠ E216), F217 (= F233), S220 (= S236), I223 (≠ V239)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 98% coverage: 1:496/507 of query aligns to 11:503/503 of O14293
- S248 (= S236) modified: Phosphoserine
- S501 (= S494) modified: Phosphoserine
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
34% identity, 95% coverage: 4:486/507 of query aligns to 7:486/491 of 5gtlA
- active site: N165 (= N160), K188 (= K183), E263 (≠ M257), C297 (= C291), E394 (= E391), E471 (≠ D468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I156), P163 (= P158), K188 (= K183), A190 (≠ S185), E191 (= E186), Q192 (= Q187), G221 (= G215), G225 (≠ V219), G241 (= G235), S242 (= S236), T245 (≠ V239), L264 (≠ M258), C297 (= C291), E394 (= E391), F396 (= F393)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
34% identity, 95% coverage: 4:486/507 of query aligns to 7:486/491 of 5gtkA
- active site: N165 (= N160), K188 (= K183), E263 (≠ M257), C297 (= C291), E394 (= E391), E471 (≠ D468)
- binding nicotinamide-adenine-dinucleotide: I161 (= I156), I162 (≠ T157), P163 (= P158), W164 (≠ F159), K188 (= K183), E191 (= E186), G221 (= G215), G225 (≠ V219), A226 (≠ N220), F239 (= F233), G241 (= G235), S242 (= S236), T245 (≠ V239), Y248 (≠ H242), L264 (≠ M258), C297 (= C291), Q344 (≠ A337), R347 (= R340), E394 (= E391), F396 (= F393)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
33% identity, 91% coverage: 15:474/507 of query aligns to 7:474/489 of 4cazA
- active site: N152 (= N160), K175 (= K183), E251 (≠ M257), C285 (= C291), E386 (= E391), E463 (≠ A463)
- 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 (= I156), G149 (≠ T157), W151 (≠ F159), N152 (= N160), K175 (= K183), E178 (= E186), G208 (= G215), G212 (≠ V219), F226 (= F233), T227 (≠ V234), G228 (= G235), G229 (≠ S236), T232 (≠ V239), V236 (= V243), E251 (≠ M257), L252 (≠ M258), C285 (= C291), E386 (= E391), F388 (= F393)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
33% identity, 91% coverage: 15:474/507 of query aligns to 7:474/489 of 2woxA
- active site: N152 (= N160), K175 (= K183), E251 (≠ M257), C285 (= C291), E386 (= E391), E463 (≠ A463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I156), G149 (≠ T157), W151 (≠ F159), N152 (= N160), K175 (= K183), S177 (= S185), E178 (= E186), G208 (= G215), G212 (≠ V219), F226 (= F233), T227 (≠ V234), G228 (= G235), G229 (≠ S236), T232 (≠ V239), V236 (= V243), E251 (≠ M257), L252 (≠ M258), C285 (= C291), E386 (= E391), F388 (= F393)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
33% identity, 91% coverage: 15:474/507 of query aligns to 7:474/489 of 2wmeA
- active site: N152 (= N160), K175 (= K183), E251 (≠ M257), C285 (= C291), E386 (= E391), E463 (≠ A463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T157), W151 (≠ F159), K175 (= K183), S177 (= S185), E178 (= E186), G208 (= G215), G212 (≠ V219), F226 (= F233), G228 (= G235), G229 (≠ S236), T232 (≠ V239), V236 (= V243)
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)
33% identity, 91% coverage: 15:474/507 of query aligns to 8:475/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 157:160) binding
- K162 (≠ M169) active site, Charge relay system
- KPSE 176:179 (= KPSE 183:186) binding
- G209 (= G215) binding
- GTST 230:233 (≠ STKV 236:239) binding
- E252 (≠ M257) active site, Proton acceptor
- C286 (= C291) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E391) binding
- E464 (≠ A463) active site, Charge relay system
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
34% identity, 93% coverage: 15:486/507 of query aligns to 4:473/487 of 4go4A
- active site: N149 (= N160), K172 (= K183), E247 (≠ M257), C281 (= C291), E381 (= E391), E458 (≠ P471)
- binding nicotinamide-adenine-dinucleotide: I145 (= I156), V146 (≠ T157), W148 (≠ F159), N149 (= N160), F154 (≠ I165), K172 (= K183), G205 (= G215), G209 (≠ V219), Q210 (≠ N220), F223 (= F233), T224 (≠ V234), G225 (= G235), S226 (= S236), T229 (≠ V239), E247 (≠ M257), G249 (= G259), C281 (= C291), E381 (= E391), F383 (= F393)
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)
29% identity, 94% coverage: 15:491/507 of query aligns to 19:503/505 of 4neaA
- active site: N166 (= N160), K189 (= K183), E264 (≠ M257), C298 (= C291), E399 (= E391), E476 (≠ D468)
- binding nicotinamide-adenine-dinucleotide: P164 (= P158), K189 (= K183), E192 (= E186), G222 (≠ E216), G226 (vs. gap), G242 (= G235), G243 (≠ S236), T246 (≠ V239), H249 (= H242), I250 (≠ V243), C298 (= C291), E399 (= E391), F401 (= F393)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
32% identity, 93% coverage: 17:486/507 of query aligns to 30:501/515 of 2d4eC
- active site: N173 (= N160), K196 (= K183), E271 (≠ M257), C305 (= C291), E409 (= E391), E486 (≠ P471)
- binding nicotinamide-adenine-dinucleotide: I169 (= I156), T170 (= T157), P171 (= P158), W172 (≠ F159), K196 (= K183), A198 (≠ S185), G229 (= G215), G233 (≠ V219), A234 (≠ N220), T248 (≠ V234), G249 (= G235), E250 (≠ S236), T253 (≠ V239), E271 (≠ M257), L272 (≠ M258), C305 (= C291), E409 (= E391), F411 (= F393), F475 (= F458)
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)
31% identity, 94% coverage: 12:487/507 of query aligns to 6:483/497 of P17202
- I28 (≠ V34) binding
- D96 (≠ E100) binding
- SPW 156:158 (≠ TPF 157:159) binding
- Y160 (≠ F161) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W168) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 183:186) binding
- L186 (≠ Q187) binding
- SSAT 236:239 (≠ STKV 236:239) binding
- V251 (≠ G251) binding in other chain
- L258 (≠ M258) binding
- W285 (≠ G285) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E391) binding
- A441 (≠ Q442) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V451) 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 (≠ R462) binding
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 97% coverage: 1:493/507 of query aligns to 1:494/505 of O24174
- N164 (= N160) 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 (= W168) 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.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
32% identity, 93% coverage: 15:486/507 of query aligns to 5:475/489 of 4o6rA
- active site: N150 (= N160), K173 (= K183), E248 (≠ M257), C282 (= C291), E383 (= E391), E460 (≠ P471)
- binding adenosine monophosphate: I146 (= I156), V147 (≠ T157), K173 (= K183), G206 (= G215), G210 (≠ V219), Q211 (≠ N220), F224 (= F233), G226 (= G235), S227 (= S236), T230 (≠ V239), R233 (≠ H242)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
33% identity, 90% coverage: 29:486/507 of query aligns to 18:480/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (≠ F159), K180 (= K183), A182 (≠ S185), T212 (vs. gap), G213 (= G215), G217 (≠ V219), F231 (= F233), G233 (= G235), S234 (= S236), V237 (= V239), Q337 (≠ A337), E388 (= E391), F390 (= F393)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
31% identity, 94% coverage: 12:487/507 of query aligns to 4:481/495 of 4v37A
- active site: N157 (= N160), K180 (= K183), E255 (≠ M257), A289 (≠ C291), E388 (= E391), E465 (≠ D468)
- binding 3-aminopropan-1-ol: C448 (≠ V451), W454 (≠ F458)
- binding nicotinamide-adenine-dinucleotide: I153 (= I156), S154 (≠ T157), P155 (= P158), W156 (≠ F159), N157 (= N160), M162 (≠ I165), K180 (= K183), S182 (= S185), E183 (= E186), G213 (= G215), G217 (≠ V219), A218 (≠ N220), T232 (≠ V234), G233 (= G235), S234 (= S236), T237 (≠ V239), E255 (≠ M257), L256 (≠ M258), A289 (≠ C291), E388 (= E391), F390 (= F393)
Query Sequence
>Ac3H11_2357 FitnessBrowser__acidovorax_3H11:Ac3H11_2357
MNAPTSQAVLAPTVKLLIGGKFVESKTTQWRDVVNPATQEVLARVPFATPEEIDAAVASA
QEAFKTWKKTAIGARARIFLKYQQLIRENMAELAAILTAEQGKTLPDAEGDVFRGLEVVE
HAASIGNLQLGELANNVAGGVDTYTLMQPLGVCAGITPFNFPAMIPLWMFPMAIATGNTF
VLKPSEQDPMVTMRLVELALEAGIPPGVLNVIHGGEAAVNAICDHKDIKAISFVGSTKVG
THVYNRASLNGKRVQCMMGAKNHAIVMPDANKEQTLNALAGAAFGAAGQRCMALSVVVLV
GEAQKWIPELVAKAKTLKVSAGVEKGTDVGPVVSCAAKDRVQSLIERGIADGATLELDGR
NPEVAGYEKGNFVGPTVFSGVKPGMSIYDQEIFGPVLCLSAAADIDEAIAFINDNPNGNG
TAIFTQSGAAARKFQEEIDVGQVGINVPIPVPVPLFSFSGSRASKLGDLGPYGKQVVLFY
TQTKTVTARWFDDSTISHGVNTTISLK
Or try a new SitesBLAST search
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