SitesBLAST
Comparing Ac3H11_4340 FitnessBrowser__acidovorax_3H11:Ac3H11_4340 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)
72% identity, 97% coverage: 9:496/505 of query aligns to 2:489/489 of 4zz7A
- active site: N149 (= N156), K172 (= K179), L246 (= L253), C280 (= C287), E382 (= E389), A462 (= A469)
- binding nicotinamide-adenine-dinucleotide: T146 (= T153), P147 (= P154), F148 (= F155), N149 (= N156), K172 (= K179), E175 (= E182), K205 (= K212), V208 (= V215), F222 (= F229), V223 (= V230), G224 (= G231), S225 (= S232), I228 (= I235), L246 (= L253), G247 (= G254), C280 (= C287), E382 (= E389), F384 (= F391)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
69% identity, 98% coverage: 9:501/505 of query aligns to 1:468/468 of 5tjrD
- active site: N144 (= N156), K167 (= K179), L241 (= L253), C270 (= C287), E356 (= E389), A436 (= A469)
- binding adenosine-5'-diphosphate: I140 (= I152), T141 (= T153), F143 (= F155), K167 (= K179), E170 (= E182), K200 (= K212), F217 (= F229), S220 (= S232), I223 (= I235)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
53% identity, 97% coverage: 5:495/505 of query aligns to 1:491/491 of 4iymC
- active site: N153 (= N156), K176 (= K179), F250 (≠ L253), C284 (= C287), E386 (= E389), Q466 (≠ A469)
- binding nicotinamide-adenine-dinucleotide: I149 (= I152), T150 (= T153), P151 (= P154), F152 (= F155), N153 (= N156), F154 (= F157), K176 (= K179), K209 (= K212), V212 (= V215), F226 (= F229), V227 (= V230), G228 (= G231), S229 (= S232), I232 (= I235), G251 (= G254), C284 (= C287), E386 (= E389), F388 (= F391)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
43% identity, 95% coverage: 13:490/505 of query aligns to 7:481/484 of 1t90A
- active site: N151 (= N156), K174 (= K179), L248 (= L253), C282 (= C287), E380 (= E389), A460 (= A469)
- binding nicotinamide-adenine-dinucleotide: I147 (= I152), A148 (≠ T153), P149 (= P154), F150 (= F155), N151 (= N156), W159 (= W164), K174 (= K179), E177 (= E182), R178 (= R183), H207 (≠ K212), V225 (= V230), G226 (= G231), S227 (= S232), V230 (≠ I235), L248 (= L253), T249 (≠ G254), C282 (= C287), E380 (= E389), F382 (= F391)
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)
43% identity, 95% coverage: 13:490/505 of query aligns to 9:483/487 of P42412
- C36 (≠ T39) 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 (= R110) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T153) binding
- F152 (= F155) binding
- C160 (≠ L163) 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 (= K179) binding
- E179 (= E182) binding
- R180 (= R183) binding
- S229 (= S232) binding
- T251 (≠ G254) binding
- R283 (= R286) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I290) 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 (≠ V355) 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 (= E389) binding
- C413 (= C420) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
30% identity, 92% coverage: 21:485/505 of query aligns to 22:483/493 of 6vr6D
- active site: N156 (= N156), E253 (≠ L253), C287 (= C287), E467 (≠ A469)
- binding nicotinamide-adenine-dinucleotide: I152 (= I152), G153 (≠ T153), W155 (≠ F155), K179 (= K179), A212 (≠ K212), G215 (≠ V215), Q216 (≠ D216), F229 (= F229), G231 (= G231), S232 (= S232), T235 (≠ I235), I239 (= I239)
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, 92% coverage: 21:485/505 of query aligns to 23:484/494 of P49189
- C116 (≠ N114) 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
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
30% identity, 92% coverage: 22:484/505 of query aligns to 33:492/503 of 1bpwA
- active site: N166 (= N156), K189 (= K179), E263 (≠ L253), C297 (= C287), E400 (= E389), E477 (≠ A469)
- binding nicotinamide-adenine-dinucleotide: I162 (= I152), L163 (≠ T153), W165 (≠ F155), N166 (= N156), K189 (= K179), G221 (≠ D211), G225 (≠ V215), T240 (≠ V230), G241 (= G231), S242 (= S232), T245 (≠ I235), E263 (≠ L253), L264 (≠ G254), C297 (= C287), E400 (= E389), F402 (= F391), F466 (= F456)
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)
30% identity, 92% coverage: 22:484/505 of query aligns to 33:492/503 of P56533
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
33% identity, 93% coverage: 13:484/505 of query aligns to 29:501/515 of 2d4eC
- active site: N173 (= N156), K196 (= K179), E271 (≠ L253), C305 (= C287), E409 (= E389), E486 (≠ A469)
- binding nicotinamide-adenine-dinucleotide: I169 (= I152), T170 (= T153), P171 (= P154), W172 (≠ F155), K196 (= K179), A198 (≠ S181), G229 (≠ D211), G233 (≠ V215), A234 (≠ D216), T248 (≠ V230), G249 (= G231), E250 (≠ S232), T253 (≠ I235), E271 (≠ L253), L272 (≠ G254), C305 (= C287), E409 (= E389), F411 (= F391), F475 (= F456)
Q3SY69 Mitochondrial 10-formyltetrahydrofolate dehydrogenase; Mitochondrial 10-FTHFDH; mtFDH; Aldehyde dehydrogenase family 1 member L2; EC 1.5.1.6 from Homo sapiens (Human) (see paper)
33% identity, 93% coverage: 21:488/505 of query aligns to 454:923/923 of Q3SY69
Sites not aligning to the query:
- 374 S→A: No effect on phosphopantetheinylation.
- 375 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation.
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
33% identity, 86% coverage: 13:444/505 of query aligns to 8:435/454 of 3ty7B
7radA Crystal structure analysis of aldh1b1
32% identity, 93% coverage: 21:490/505 of query aligns to 24:490/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I152), I159 (≠ T153), P160 (= P154), W161 (≠ F155), N162 (= N156), M167 (≠ V161), K185 (= K179), E188 (= E182), G218 (≠ D211), G222 (≠ V215), A223 (≠ D216), T237 (≠ V230), G238 (= G231), S239 (= S232), V242 (≠ I235), E261 (≠ L253), L262 (≠ G254), C295 (= C287), E392 (= E389), F394 (= F391)
- 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 (≠ R110), F163 (= F157), E285 (≠ G277), F289 (≠ G281), N450 (≠ P448), V452 (≠ P450)
7mjdA Crystal structure analysis of aldh1b1
32% identity, 93% coverage: 21:490/505 of query aligns to 24:490/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I152), I159 (≠ T153), P160 (= P154), W161 (≠ F155), N162 (= N156), M167 (≠ V161), K185 (= K179), E188 (= E182), G218 (≠ D211), G222 (≠ V215), F236 (= F229), T237 (≠ V230), G238 (= G231), S239 (= S232), V242 (≠ I235), E261 (≠ L253), L262 (≠ G254), C295 (= C287), E392 (= E389), F394 (= F391)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R110), E285 (≠ G277), F289 (≠ G281), N450 (≠ P448), V452 (≠ P450)
7mjcA Crystal structure analysis of aldh1b1
32% identity, 93% coverage: 21:490/505 of query aligns to 24:490/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I152), I159 (≠ T153), P160 (= P154), W161 (≠ F155), N162 (= N156), K185 (= K179), E188 (= E182), G218 (≠ D211), G222 (≠ V215), T237 (≠ V230), G238 (= G231), S239 (= S232), V242 (≠ I235), E261 (≠ L253), L262 (≠ G254), C295 (= C287), E392 (= E389), F394 (= F391)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
33% identity, 93% coverage: 21:490/505 of query aligns to 51:517/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
33% identity, 93% coverage: 21:490/505 of query aligns to 27:493/496 of 4fr8C
- active site: N165 (= N156), K188 (= K179), Q264 (≠ L253), C298 (= C287), E395 (= E389), E472 (≠ D466)
- binding nicotinamide-adenine-dinucleotide: I161 (= I152), I162 (≠ T153), W164 (≠ F155), K188 (= K179), G221 (≠ D211), G225 (≠ V215), A226 (≠ D216), F239 (= F229), G241 (= G231), S242 (= S232), I245 (= I235), Q345 (≠ H335), E395 (= E389), F397 (= F391)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
33% identity, 93% coverage: 21:490/505 of query aligns to 24:490/493 of 4fr8A
- active site: N162 (= N156), K185 (= K179), Q261 (≠ L253), C295 (= C287), E392 (= E389), E469 (≠ D466)
- binding nicotinamide-adenine-dinucleotide: I158 (= I152), I159 (≠ T153), W161 (≠ F155), K185 (= K179), G218 (≠ D211), G222 (≠ V215), A223 (≠ D216), F236 (= F229), G238 (= G231), S239 (= S232), I242 (= I235), Q342 (≠ H335), K345 (= K338), E392 (= E389), F394 (= F391)
- binding propane-1,2,3-triyl trinitrate: F163 (= F157), L166 (≠ M160), W170 (= W164), F289 (≠ G281), S294 (≠ R286), C295 (= C287), D450 (≠ P448), F452 (≠ P450)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
33% identity, 93% coverage: 21:490/505 of query aligns to 25:491/494 of 5l13A
- active site: N163 (= N156), K186 (= K179), E262 (≠ L253), C296 (= C287), E393 (= E389), E470 (≠ D466)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F157), M168 (≠ V161), W171 (= W164), F290 (≠ G281), C295 (≠ R286), C296 (= C287), C297 (≠ M288), D451 (≠ P448), F453 (≠ P450)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
33% identity, 93% coverage: 21:490/505 of query aligns to 25:491/494 of 4kwgA
- active site: N163 (= N156), K186 (= K179), E262 (≠ L253), C296 (= C287), E393 (= E389), E470 (≠ D466)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F157), M168 (≠ V161), C295 (≠ R286), C296 (= C287), C297 (≠ M288), D451 (≠ P448), F453 (≠ P450)
Query Sequence
>Ac3H11_4340 FitnessBrowser__acidovorax_3H11:Ac3H11_4340
MNHDKNVTTTVGHLIDGKSVADAERTQPVFNPATGQSTTSVALASKATVEAAIASAEAAF
PAWRNTPPLKRARVMSKLKVLLEENADKIAALITAEHGKVLADAHGELQRGIENVEYASY
APELLKGEHSRNVGPSIDSWSEFQALGVTAGITPFNFPAMVPLWMWPMAVACGNTFVLKP
SERDPSSTLFIAQLALEAGLPPGVLNVVNGDKLAVDTLLQDPRVKAVSFVGSTPIAEYIY
SEGCKHGKRVQALGGAKNHAVLMPDADVGNAVSALMGAAYGSCGERCMAIPLLVAVGDAV
GDAVIAGLKTEIAKMKVGPGTDNSNDMGPLVTKPHFEKVKAYVDSGVTEGATLVVDGRGV
KVAGHEEGYFLGACLFDNVKPGMKIYQEEIFGPVLGVVRVKTLQEAMQLINDHEYGNGTC
IFTRDGEAARYFTDHIQVGMVGVNVPLPVPVAYHSFGGWKRSLFGDLHAYGPDAVRFYTK
RKTITQRWPSAGVREGAVFSFPSSR
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