SitesBLAST
Comparing AZOBR_RS22500 AZOBR_RS22500 methylmalonate-semialdehyde dehydrogenase 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)
70% identity, 98% coverage: 1:490/499 of query aligns to 1:489/489 of 4zz7A
- active site: N149 (= N150), K172 (= K173), L246 (= L247), C280 (= C281), E382 (= E383), A462 (= A463)
- binding nicotinamide-adenine-dinucleotide: T146 (= T147), P147 (= P148), F148 (= F149), N149 (= N150), K172 (= K173), E175 (= E176), K205 (= K206), V208 (= V209), F222 (= F223), V223 (= V224), G224 (= G225), S225 (= S226), I228 (≠ V229), L246 (= L247), G247 (= G248), C280 (= C281), E382 (= E383), F384 (= F385)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
68% identity, 99% coverage: 3:495/499 of query aligns to 2:468/468 of 5tjrD
- active site: N144 (= N150), K167 (= K173), L241 (= L247), C270 (= C281), E356 (= E383), A436 (= A463)
- binding adenosine-5'-diphosphate: I140 (= I146), T141 (= T147), F143 (= F149), K167 (= K173), E170 (= E176), K200 (= K206), F217 (= F223), S220 (= S226), I223 (≠ V229)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
56% identity, 96% coverage: 6:485/499 of query aligns to 9:488/491 of 4iymC
- active site: N153 (= N150), K176 (= K173), F250 (≠ L247), C284 (= C281), E386 (= E383), Q466 (≠ A463)
- binding nicotinamide-adenine-dinucleotide: I149 (= I146), T150 (= T147), P151 (= P148), F152 (= F149), N153 (= N150), F154 (= F151), K176 (= K173), K209 (= K206), V212 (= V209), F226 (= F223), V227 (= V224), G228 (= G225), S229 (= S226), I232 (≠ V229), G251 (= G248), C284 (= C281), E386 (= E383), F388 (= F385)
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)
44% identity, 96% coverage: 4:483/499 of query aligns to 7:482/487 of P42412
- C36 (≠ G33) 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 (= R104) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T147) binding
- F152 (= F149) binding
- C160 (≠ L157) 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 (= K173) binding
- E179 (= E176) binding
- R180 (= R177) binding
- S229 (= S226) binding
- T251 (≠ G248) binding
- R283 (= R280) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I284) 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 (≠ V349) 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 (= E383) binding
- C413 (= C414) 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
44% identity, 96% coverage: 4:483/499 of query aligns to 5:480/484 of 1t90A
- active site: N151 (= N150), K174 (= K173), L248 (= L247), C282 (= C281), E380 (= E383), A460 (= A463)
- binding nicotinamide-adenine-dinucleotide: I147 (= I146), A148 (≠ T147), P149 (= P148), F150 (= F149), N151 (= N150), W159 (= W158), K174 (= K173), E177 (= E176), R178 (= R177), H207 (≠ K206), V225 (= V224), G226 (= G225), S227 (= S226), V230 (= V229), L248 (= L247), T249 (≠ G248), C282 (= C281), E380 (= E383), F382 (= F385)
7radA Crystal structure analysis of aldh1b1
32% identity, 97% coverage: 1:483/499 of query aligns to 10:489/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (≠ F149), N162 (= N150), M167 (≠ V155), K185 (= K173), E188 (= E176), G218 (≠ D205), G222 (≠ V209), A223 (≠ D210), T237 (≠ V224), G238 (= G225), S239 (= S226), V242 (= V229), E261 (≠ L247), L262 (≠ G248), C295 (= C281), E392 (= E383), F394 (= F385)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ R104), F163 (= F151), E285 (≠ G271), F289 (≠ G275), N450 (≠ P442), V452 (≠ P444)
7mjdA Crystal structure analysis of aldh1b1
32% identity, 97% coverage: 1:483/499 of query aligns to 10:489/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (≠ F149), N162 (= N150), M167 (≠ V155), K185 (= K173), E188 (= E176), G218 (≠ D205), G222 (≠ V209), F236 (= F223), T237 (≠ V224), G238 (= G225), S239 (= S226), V242 (= V229), E261 (≠ L247), L262 (≠ G248), C295 (= C281), E392 (= E383), F394 (= F385)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R104), E285 (≠ G271), F289 (≠ G275), N450 (≠ P442), V452 (≠ P444)
7mjcA Crystal structure analysis of aldh1b1
32% identity, 97% coverage: 1:483/499 of query aligns to 10:489/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (≠ F149), N162 (= N150), K185 (= K173), E188 (= E176), G218 (≠ D205), G222 (≠ V209), T237 (≠ V224), G238 (= G225), S239 (= S226), V242 (= V229), E261 (≠ L247), L262 (≠ G248), C295 (= C281), E392 (= E383), F394 (= F385)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
31% identity, 92% coverage: 22:481/499 of query aligns to 26:486/487 of Q9H2A2
- R109 (= R104) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N150) mutation to A: Complete loss of activity.
- R451 (≠ V443) mutation to A: Complete loss of activity.
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 95% coverage: 7:480/499 of query aligns to 13:489/505 of O24174
- N164 (= N150) 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 (= W158) 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.
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
30% identity, 94% coverage: 9:478/499 of query aligns to 16:483/494 of P49189
- C116 (≠ N108) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
30% identity, 94% coverage: 9:478/499 of query aligns to 15:482/493 of 6vr6D
- active site: N156 (= N150), E253 (≠ L247), C287 (= C281), E467 (≠ A463)
- binding nicotinamide-adenine-dinucleotide: I152 (= I146), G153 (≠ T147), W155 (≠ F149), K179 (= K173), A212 (≠ K206), G215 (≠ V209), Q216 (≠ D210), F229 (= F223), G231 (= G225), S232 (= S226), T235 (≠ V229), I239 (≠ V233)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
36% identity, 94% coverage: 8:478/499 of query aligns to 16:477/485 of 6x9lA
- active site: N154 (= N150), E252 (≠ L247), A286 (≠ C281), E462 (≠ A463)
- binding nicotinamide-adenine-dinucleotide: I150 (= I146), T151 (= T147), W153 (≠ F149), N154 (= N150), Q159 (≠ V155), K177 (= K173), E180 (= E176), G210 (vs. gap), P211 (≠ K206), G214 (≠ V209), T229 (≠ V224), G230 (= G225), S231 (= S226), E252 (≠ L247), L253 (≠ G248), A286 (≠ C281), E386 (= E383), F388 (= F385), F451 (= F450)
- binding octanal: W155 (≠ F151), S285 (≠ R280)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
31% identity, 91% coverage: 23:478/499 of query aligns to 40:492/503 of 1bpwA
- active site: N166 (= N150), K189 (= K173), E263 (≠ L247), C297 (= C281), E400 (= E383), E477 (≠ A463)
- binding nicotinamide-adenine-dinucleotide: I162 (= I146), L163 (≠ T147), W165 (≠ F149), N166 (= N150), K189 (= K173), G221 (≠ D205), G225 (≠ V209), T240 (≠ V224), G241 (= G225), S242 (= S226), T245 (≠ V229), E263 (≠ L247), L264 (≠ G248), C297 (= C281), E400 (= E383), F402 (= F385), F466 (= F450)
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)
31% identity, 91% coverage: 23:478/499 of query aligns to 40:492/503 of P56533
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)
30% identity, 96% coverage: 1:480/499 of query aligns to 5:484/497 of P17202
- I28 (≠ V24) binding
- D96 (≠ E90) binding
- SPW 156:158 (≠ TPF 147:149) binding
- Y160 (≠ F151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 173:176) binding
- L186 (≠ R177) binding
- SSAT 236:239 (≠ STPV 226:229) binding
- V251 (≠ G241) binding in other chain
- L258 (≠ G248) binding
- W285 (≠ G275) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E383) binding
- A441 (≠ M434) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V443) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F450) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K454) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
31% identity, 96% coverage: 1:480/499 of query aligns to 2:484/500 of 3iwjA
- active site: N159 (= N150), K182 (= K173), E257 (≠ L247), C291 (= C281), E390 (= E383), E467 (≠ D460)
- binding glycerol: D110 (≠ R104), Y160 (≠ F151), W167 (= W158), I290 (≠ R280), C291 (= C281), C450 (≠ V443), W456 (≠ F450)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), T156 (= T147), W158 (≠ F149), K182 (= K173), S184 (= S175), E185 (= E176), G215 (≠ D205), A220 (≠ D210), F233 (= F223), G235 (= G225), S236 (= S226), T239 (≠ V229), I243 (≠ V233)
Q93YB2 Aminoaldehyde dehydrogenase 2, peroxisomal; PsAMADH2; Aminobutyraldehyde dehydrogenase AMADH2; Gamma-guanidinobutyraldehyde dehydrogenase AMADH2; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
31% identity, 96% coverage: 1:480/499 of query aligns to 5:487/503 of Q93YB2
- I28 (≠ V24) binding
- D99 (≠ E90) binding
- W161 (≠ F149) binding
- K185 (= K173) binding
- L189 (≠ R177) binding
- S239 (= S226) binding
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
32% identity, 95% coverage: 6:478/499 of query aligns to 29:501/515 of 2d4eC
- active site: N173 (= N150), K196 (= K173), E271 (≠ L247), C305 (= C281), E409 (= E383), E486 (≠ A463)
- binding nicotinamide-adenine-dinucleotide: I169 (= I146), T170 (= T147), P171 (= P148), W172 (≠ F149), K196 (= K173), A198 (≠ S175), G229 (≠ D205), G233 (≠ V209), A234 (≠ D210), T248 (≠ V224), G249 (= G225), E250 (≠ S226), T253 (≠ V229), E271 (≠ L247), L272 (≠ G248), C305 (= C281), E409 (= E383), F411 (= F385), F475 (= F450)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
30% identity, 95% coverage: 7:480/499 of query aligns to 11:487/503 of Q8VWZ1
- N27 (≠ I23) binding
- I28 (≠ V24) binding
- D99 (≠ E90) binding
- L189 (≠ R177) binding
- 238:245 (vs. 225:232, 25% identical) binding
- C294 (= C281) binding
- E393 (= E383) binding
Query Sequence
>AZOBR_RS22500 AZOBR_RS22500 methylmalonate-semialdehyde dehydrogenase
MPLVPHLIGGAADAPAETRSADIVNPATGETVGRVPLAGRATVESAIAAAEAAFPAWRAT
PPAKRARVMFRFRQLLEDNADRVCAAITREHGKTLEDARGELTRGIENVEYACGIADLLK
GEHSKNVGPGIDSWSEFQPLGVVAGITPFNFPAMVPLWMFPVAVACGNCFILKPSERDPS
ASLLVAQLAQEAGLPPGVLNVVHGDKEAVDTLLTDPRVQAVSFVGSTPVAEYVYATGTAH
GKRVQALGGAKNHAIVMPDADLDNAVSAIMGAAYGSCGERCMAISVVVAVGDATADRVVA
MLAEQVRSLKVGAGTGAGCDMGPLVTRAHFEKVKGFVDQGVAEGAELVVDGRGLVVPGHE
GGFFLGGCLFDRVTPDMRIYREEIFGPVLCVVRVATMQEGMDLIDAHEYGNGTCLFTRDG
EAARYFTDAIKVGMVGINVPLPVPVSYHSFGGWKRSLFGDLAAYGPDGVRFYTRRKTITQ
RWPTGGVREGAQFSFPSMK
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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