SitesBLAST
Comparing RR42_RS25635 FitnessBrowser__Cup4G11:RR42_RS25635 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)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
48% identity, 96% coverage: 12:500/507 of query aligns to 1:486/489 of 4zz7A
- active site: N149 (= N161), K172 (= K184), L246 (≠ M258), C280 (= C292), E382 (= E392), A462 (≠ P472)
- binding nicotinamide-adenine-dinucleotide: T146 (= T158), P147 (= P159), F148 (= F160), N149 (= N161), K172 (= K184), E175 (= E187), K205 (= K217), V208 (= V220), F222 (= F234), V223 (= V235), G224 (= G236), S225 (= S237), I228 (≠ V240), L246 (≠ M258), G247 (≠ M259), C280 (= C292), E382 (= E392), F384 (= F394)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
49% identity, 93% coverage: 18:491/507 of query aligns to 10:485/491 of 4iymC
- active site: N153 (= N161), K176 (= K184), F250 (≠ M258), C284 (= C292), E386 (= E392), Q466 (≠ P472)
- binding nicotinamide-adenine-dinucleotide: I149 (= I157), T150 (= T158), P151 (= P159), F152 (= F160), N153 (= N161), F154 (= F162), K176 (= K184), K209 (= K217), V212 (= V220), F226 (= F234), V227 (= V235), G228 (= G236), S229 (= S237), I232 (≠ V240), G251 (≠ M259), C284 (= C292), E386 (= E392), F388 (= F394)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
49% identity, 94% coverage: 16:491/507 of query aligns to 4:455/468 of 5tjrD
- active site: N144 (= N161), K167 (= K184), L241 (≠ M258), C270 (= C292), E356 (= E392), A436 (≠ P472)
- binding adenosine-5'-diphosphate: I140 (= I157), T141 (= T158), F143 (= F160), K167 (= K184), E170 (= E187), K200 (= K217), F217 (= F234), S220 (= S237), I223 (≠ V240)
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)
46% identity, 95% coverage: 11:491/507 of query aligns to 3:481/487 of P42412
- C36 (≠ G44) 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 (= R115) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T158) binding
- F152 (= F160) binding
- C160 (≠ L168) 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 (= K184) binding
- E179 (= E187) binding
- R180 (≠ Q188) binding
- S229 (= S237) binding
- T251 (≠ M259) binding
- R283 (= R291) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ T295) 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 (≠ L358) 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 (= E392) binding
- C413 (≠ G423) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
46% identity, 95% coverage: 11:491/507 of query aligns to 1:479/484 of 1t90A
- active site: N151 (= N161), K174 (= K184), L248 (≠ M258), C282 (= C292), E380 (= E392), A460 (≠ P472)
- binding nicotinamide-adenine-dinucleotide: I147 (= I157), A148 (≠ T158), P149 (= P159), F150 (= F160), N151 (= N161), W159 (= W169), K174 (= K184), E177 (= E187), R178 (≠ Q188), H207 (≠ K217), V225 (= V235), G226 (= G236), S227 (= S237), V230 (= V240), L248 (≠ M258), T249 (≠ M259), C282 (= C292), E380 (= E392), F382 (= F394)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
32% identity, 93% coverage: 24:493/507 of query aligns to 17:498/503 of 1bpwA
- active site: N166 (= N161), K189 (= K184), E263 (≠ M258), C297 (= C292), E400 (= E392), E477 (≠ L470)
- binding nicotinamide-adenine-dinucleotide: I162 (= I157), L163 (≠ T158), W165 (≠ F160), N166 (= N161), K189 (= K184), G221 (= G216), G225 (≠ V220), T240 (≠ V235), G241 (= G236), S242 (= S237), T245 (≠ V240), E263 (≠ M258), L264 (≠ M259), C297 (= C292), E400 (= E392), F402 (= F394), F466 (= F459)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
32% identity, 93% coverage: 24:493/507 of query aligns to 17:498/503 of P56533
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
34% identity, 93% coverage: 16:487/507 of query aligns to 5:475/489 of 4o6rA
- active site: N150 (= N161), K173 (= K184), E248 (≠ M258), C282 (= C292), E383 (= E392), E460 (≠ Q476)
- binding adenosine monophosphate: I146 (= I157), V147 (≠ T158), K173 (= K184), G206 (= G216), G210 (≠ V220), Q211 (≠ D221), F224 (= F234), G226 (= G236), S227 (= S237), T230 (≠ V240), R233 (≠ H243)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 97% coverage: 5:496/507 of query aligns to 6:502/503 of O14293
- S248 (= S237) modified: Phosphoserine
- S501 (≠ T495) modified: Phosphoserine
4wb9A Human aldh1a1 complexed with nadh (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 8:487/493 of 4wb9A
- active site: N162 (= N161), K185 (= K184), E261 (≠ M258), C295 (= C292), E392 (= E392), E469 (≠ D469)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I157), I159 (≠ T158), P160 (= P159), W161 (≠ F160), N162 (= N161), K185 (= K184), E188 (= E187), G218 (= G216), G222 (≠ V220), F236 (= F234), T237 (≠ V235), G238 (= G236), S239 (= S237), V242 (= V240), G263 (= G260), C295 (= C292), Q342 (≠ A338), K345 (≠ R341), E392 (= E392), F394 (= F394)
7um9A Human aldh1a1 with bound compound cm38 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I157), I160 (≠ T158), P161 (= P159), W162 (≠ F160), N163 (= N161), K186 (= K184), E189 (= E187), G219 (= G216), G223 (≠ V220), F237 (= F234), T238 (≠ V235), G239 (= G236), S240 (= S237), V243 (= V240), E262 (≠ M258), G264 (= G260), Q343 (≠ A338), K346 (≠ R341), E393 (= E392), F395 (= F394)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (= W169), H286 (≠ G282), Y290 (≠ G286), I297 (≠ M293), G451 (vs. gap)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 5l2nA
- active site: N163 (= N161), K186 (= K184), E262 (≠ M258), C296 (= C292), E393 (= E392), E470 (≠ D469)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (= F162), M168 (≠ I166), W171 (= W169), H286 (≠ G282), G287 (≠ A283), Y290 (≠ G286), C295 (≠ R291), C296 (= C292), I297 (≠ M293), Y450 (≠ P449), G451 (vs. gap), V453 (≠ I450), F459 (≠ Y456)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 5l2mA
- active site: N163 (= N161), K186 (= K184), E262 (≠ M258), C296 (= C292), E393 (= E392), E470 (≠ D469)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F162), F283 (≠ A279), H286 (≠ G282), Y290 (≠ G286)
4wpnA Structure of human aldh1a1 with inhibitor cm053 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 4wpnA
- active site: N163 (= N161), K186 (= K184), E262 (≠ M258), C296 (= C292), E393 (= E392), E470 (≠ D469)
- binding 1-{[1,3-dimethyl-7-(3-methylbutyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]methyl}piperidine-4-carboxamide: F164 (= F162), H286 (≠ G282), G287 (≠ A283), Y290 (≠ G286), C295 (≠ R291), I297 (≠ M293), G451 (vs. gap), V453 (≠ I450)
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
32% identity, 95% coverage: 10:490/507 of query aligns to 16:495/501 of P00352
- N121 (≠ D112) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ TPFN 158:161) binding
- I177 (≠ L168) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPSE 184:187) binding
- GP 226:227 (≠ GK 216:217) binding
- GS 246:247 (= GS 236:237) binding
- E269 (≠ M258) active site, Proton acceptor
- ELG 269:271 (≠ MMG 258:260) binding
- C302 (≠ R291) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C292) active site, Nucleophile
- EQYDK 349:353 (≠ AAHAR 337:341) binding
- EIF 400:402 (= EIF 392:394) binding
- G458 (vs. gap) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
33% identity, 93% coverage: 16:488/507 of query aligns to 6:473/476 of 5x5uA
- active site: N151 (= N161), K174 (= K184), E249 (≠ M258), C283 (= C292), E380 (= E392), E457 (≠ L470)
- binding glycerol: D15 (≠ E25), A16 (≠ S26), A17 (≠ D27), G19 (≠ N29)
- binding nicotinamide-adenine-dinucleotide: P149 (= P159), P207 (≠ K217), A208 (≠ T218), S211 (≠ V220), G227 (= G236), S228 (= S237), V231 (= V240), R329 (≠ A337), R330 (≠ A338), E380 (= E392), F382 (= F394)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
33% identity, 93% coverage: 16:488/507 of query aligns to 6:473/476 of 5x5tA
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 7jwwA
- active site: N163 (= N161), K186 (= K184), E262 (≠ M258), C296 (= C292), E393 (= E392), E470 (≠ D469)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G116), T122 (≠ V120), F164 (= F162), M168 (≠ I166), Y290 (≠ G286), C295 (≠ R291), C296 (= C292), I297 (≠ M293), V453 (≠ I450), F459 (≠ Y456)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
32% identity, 95% coverage: 10:490/507 of query aligns to 9:488/494 of 7jwvA
- active site: N163 (= N161), K186 (= K184), E262 (≠ M258), C296 (= C292), E393 (= E392), E470 (≠ D469)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G116), T122 (≠ V120), F164 (= F162), M168 (≠ I166), Y290 (≠ G286), C295 (≠ R291), I297 (≠ M293), V453 (≠ I450), F459 (≠ Y456)
Query Sequence
>RR42_RS25635 FitnessBrowser__Cup4G11:RR42_RS25635
MNSAVPHATLQLPTAKLLIDGKFVESDSNQWGNVVNPATQQVIGRVPFATVEEVDAAIAS
AQRAFLAWRNTPLGARLRVMLKFQDLVRRNMERIARTLTAEQGKTLPDAQGDIFRGLEVV
EHACSVGTLQMGEFAENVAGGVDTYTLRQPIGVCAGITPFNFPGMIPLWMFPMAIVCGNT
FVLKPSEQDPLSTMELVELAMEAGVPPGVLNVVHGGKTVVDMLCTHPDVKAISFVGSTHV
GTHVYNLGSKHGKRVQSMMGAKNHAVVLPDANRQQTLNALVGAGFGAAGQRCMATSVVVL
VGQSRDWLPELVAKAKLLKVNAGHEPGTDVGPVMSKAAHARITGLIEEGVQAGAALLLDG
RNVKVPGYENGNFVGPTIFSGVSPDMSIYTQEIFGPVVVVLEVDTLDEAIALVNRNPMGN
GVGLFTQSGAAARKFQSEIDVGQVGINIPIPVPVPYFSFTGSRGSKLGDLGPYGKQVVQF
YTQTKTVTARWFDDTPAEGVNTTIALR
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