SitesBLAST
Comparing RR42_RS24025 FitnessBrowser__Cup4G11:RR42_RS24025 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)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
48% identity, 95% coverage: 18:500/507 of query aligns to 7:486/489 of 4zz7A
- active site: N149 (= N161), K172 (= K184), L246 (≠ M258), C280 (= C292), E382 (= E392), A462 (≠ P472)
- binding nicotinamide-adenine-dinucleotide: I145 (= I157), T146 (= T158), P147 (= P159), F148 (= F160), N149 (= N161), W157 (= W169), K172 (= K184), P173 (= P185), S174 (= S186), E175 (= E187), R176 (≠ Q188), K205 (= K217), V208 (= V220), F222 (= F234), V223 (= V235), G224 (= G236), S225 (= S237), I228 (≠ V240), L246 (≠ M258), G247 (≠ M259), G248 (= G260), C280 (= C292), E382 (= E392), F384 (= F394), N410 (= N420), F449 (= F459)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
48% 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), P177 (= P185), S178 (= S186), E179 (= E187), K209 (= K217), V212 (= V220), F226 (= F234), V227 (= V235), G228 (= G236), S229 (= S237), I232 (≠ V240), G251 (≠ M259), G252 (= G260), R283 (= R291), 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), P142 (= P159), F143 (= F160), K167 (= K184), P168 (= P185), S169 (= S186), E170 (= E187), R171 (≠ Q188), K200 (= K217), V203 (= V220), F217 (= F234), G219 (= G236), S220 (= S237), I223 (≠ V240)
P42412 Malonate-semialdehyde dehydrogenase; MSA dehydrogenase; Methylmalonate-semialdehyde dehydrogenase; MMSA dehydrogenase; MMSDH; MSDH; EC 1.2.1.-; 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.
- 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.
- KPSER 176:180 (≠ KPSEQ 184:188) 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), P175 (= P185), S176 (= S186), E177 (= E187), R178 (≠ Q188), H207 (≠ K217), V210 (= V220), F224 (= F234), V225 (= V235), G226 (= G236), S227 (= S237), V230 (= V240), L248 (≠ M258), T249 (≠ M259), G250 (= G260), C282 (= C292), E380 (= E392), F382 (= F394), N408 (= N420), F447 (= F459)
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), A164 (≠ P159), W165 (≠ F160), N166 (= N161), K189 (= K184), S191 (= S186), G221 (= G216), A222 (≠ K217), G225 (≠ V220), S226 (≠ D221), F239 (= F234), T240 (≠ V235), G241 (= G236), S242 (= S237), T245 (≠ V240), M252 (≠ L247), E263 (≠ M258), L264 (≠ M259), G265 (= G260), C297 (= C292), E400 (= E392), F402 (= F394), L428 (≠ N420), 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), P174 (= P185), S175 (= S186), E176 (= E187), G206 (= G216), G210 (≠ V220), Q211 (≠ D221), F224 (= F234), T225 (≠ V235), G226 (= G236), S227 (= S237), T230 (≠ V240), R233 (≠ H243), I234 (≠ V244)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 97% coverage: 5:496/507 of query aligns to 6:502/503 of O14293
- S248 (= S237) modified: Phosphoserine
- S501 (≠ T495) modified: Phosphoserine
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