SitesBLAST
Comparing H281DRAFT_02373 FitnessBrowser__Burk376:H281DRAFT_02373 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)
59% identity, 94% coverage: 21:499/512 of query aligns to 6:484/489 of 4zz7A
- active site: N149 (= N165), K172 (= K188), L246 (= L262), C280 (= C296), E382 (= E397), A462 (= A477)
- binding nicotinamide-adenine-dinucleotide: T146 (= T162), P147 (= P163), F148 (= F164), N149 (= N165), K172 (= K188), E175 (= E191), K205 (= K221), V208 (= V224), F222 (= F238), V223 (= V239), G224 (= G240), S225 (= S241), I228 (= I244), L246 (= L262), G247 (= G263), C280 (= C296), E382 (= E397), F384 (= F399)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
59% identity, 94% coverage: 19:498/512 of query aligns to 3:457/468 of 5tjrD
- active site: N144 (= N165), K167 (= K188), L241 (= L262), C270 (= C296), E356 (= E397), A436 (= A477)
- binding adenosine-5'-diphosphate: I140 (= I161), T141 (= T162), F143 (= F164), K167 (= K188), E170 (= E191), K200 (= K221), F217 (= F238), S220 (= S241), I223 (= I244)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
58% identity, 94% coverage: 19:500/512 of query aligns to 7:489/491 of 4iymC
- active site: N153 (= N165), K176 (= K188), F250 (≠ L262), C284 (= C296), E386 (= E397), Q466 (≠ A477)
- binding nicotinamide-adenine-dinucleotide: I149 (= I161), T150 (= T162), P151 (= P163), F152 (= F164), N153 (= N165), F154 (= F166), K176 (= K188), K209 (= K221), V212 (= V224), F226 (= F238), V227 (= V239), G228 (= G240), S229 (= S241), I232 (= I244), G251 (= G263), C284 (= C296), E386 (= E397), F388 (= F399)
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)
48% identity, 95% coverage: 14:497/512 of query aligns to 2:482/487 of P42412
- C36 (≠ A48) 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 (= R119) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T162) binding
- F152 (= F164) binding
- C160 (= C172) 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 (= K188) binding
- E179 (= E191) binding
- R180 (= R192) binding
- S229 (= S241) binding
- T251 (≠ G263) binding
- R283 (= R295) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I299) 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 (≠ V363) 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 (= E397) binding
- C413 (≠ S428) 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
48% identity, 94% coverage: 17:497/512 of query aligns to 3:480/484 of 1t90A
- active site: N151 (= N165), K174 (= K188), L248 (= L262), C282 (= C296), E380 (= E397), A460 (= A477)
- binding nicotinamide-adenine-dinucleotide: I147 (= I161), A148 (≠ T162), P149 (= P163), F150 (= F164), N151 (= N165), W159 (= W173), K174 (= K188), E177 (= E191), R178 (= R192), H207 (≠ K221), V225 (= V239), G226 (= G240), S227 (= S241), V230 (≠ I244), L248 (= L262), T249 (≠ G263), C282 (= C296), E380 (= E397), F382 (= F399)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
34% identity, 95% coverage: 8:492/512 of query aligns to 16:501/515 of 2d4eC
- active site: N173 (= N165), K196 (= K188), E271 (≠ L262), C305 (= C296), E409 (= E397), E486 (≠ A477)
- binding nicotinamide-adenine-dinucleotide: I169 (= I161), T170 (= T162), P171 (= P163), W172 (≠ F164), K196 (= K188), A198 (≠ S190), G229 (≠ D220), G233 (≠ V224), A234 (≠ D225), T248 (≠ V239), G249 (= G240), E250 (≠ S241), T253 (≠ I244), E271 (≠ L262), L272 (≠ G263), C305 (= C296), E409 (= E397), F411 (= F399), F475 (= F464)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
34% identity, 92% coverage: 22:493/512 of query aligns to 9:478/489 of 6wsbA
- active site: N152 (= N165), E250 (≠ L262), C284 (= C296), E462 (≠ H475)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), G149 (≠ T162), A150 (≠ P163), W151 (≠ F164), N152 (= N165), K175 (= K188), E178 (= E191), G208 (≠ K221), G211 (≠ V224), A212 (≠ D225), F225 (= F238), T226 (≠ V239), G227 (= G240), G228 (≠ S241), T231 (≠ I244), V235 (≠ I248), E250 (≠ L262), L251 (≠ G263), G252 (= G264), C284 (= C296), E385 (= E397), F387 (= F399)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
33% identity, 92% coverage: 22:492/512 of query aligns to 17:486/497 of 8skfA
- binding calcium ion: T33 (≠ V38), I34 (≠ F39), D100 (≠ E105), V187 (≠ R192)
- binding nicotinamide-adenine-dinucleotide: I156 (= I161), G157 (≠ T162), A158 (≠ P163), W159 (≠ F164), K183 (= K188), E186 (= E191), G216 (≠ K221), G220 (≠ D225), T235 (≠ V239), G236 (= G240), G237 (≠ S241), S240 (≠ I244), K243 (≠ Y247), E259 (≠ L262), C293 (= C296), F396 (= F399)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8vqwC
- binding coenzyme a: I147 (= I161), W150 (≠ F164), K174 (= K188), S176 (= S190), E177 (= E191), G207 (≠ K221), G211 (≠ D225), F225 (= F238), G227 (= G240), G228 (≠ S241), S231 (≠ I244), H331 (= H343), F387 (= F399)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8vj3A
8uzoA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (adp bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8uzoA
8uznA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (amp bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8uznA
- binding adenosine monophosphate: I147 (= I161), G148 (≠ T162), K174 (= K188), S176 (= S190), E177 (= E191), G207 (≠ K221), G211 (≠ D225), F225 (= F238), G228 (≠ S241), S231 (≠ I244), K234 (≠ Y247)
8uzmA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADPH bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8uzmA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G148 (≠ T162), W150 (≠ F164), K174 (= K188), S176 (= S190), E177 (= E191), G207 (≠ K221), G211 (≠ D225), F225 (= F238), T226 (≠ V239), G227 (= G240), G228 (≠ S241), S231 (≠ I244), E250 (≠ L262), G252 (= G264), C284 (= C296), E385 (= E397), F387 (= F399)
8uzkA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADP+ bound)
33% identity, 92% coverage: 22:492/512 of query aligns to 8:477/488 of 8uzkA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I147 (= I161), G148 (≠ T162), W150 (≠ F164), N151 (= N165), K174 (= K188), S176 (= S190), E177 (= E191), G207 (≠ K221), G211 (≠ D225), F225 (= F238), G227 (= G240), G228 (≠ S241), S231 (≠ I244), E250 (≠ L262), F387 (= F399)
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, 94% coverage: 14:492/512 of query aligns to 2:483/487 of Q9H2A2
- R109 (= R119) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N165) mutation to A: Complete loss of activity.
- R451 (≠ V457) mutation to A: Complete loss of activity.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 92% coverage: 22:492/512 of query aligns to 20:486/491 of 5gtlA
- active site: N165 (= N165), K188 (= K188), E263 (≠ L262), C297 (= C296), E394 (= E397), E471 (≠ A477)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I161), P163 (= P163), K188 (= K188), A190 (≠ S190), E191 (= E191), Q192 (≠ R192), G221 (≠ K221), G225 (≠ D225), G241 (= G240), S242 (= S241), T245 (≠ I244), L264 (≠ G263), C297 (= C296), E394 (= E397), F396 (= F399)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 92% coverage: 22:492/512 of query aligns to 20:486/491 of 5gtkA
- active site: N165 (= N165), K188 (= K188), E263 (≠ L262), C297 (= C296), E394 (= E397), E471 (≠ A477)
- binding nicotinamide-adenine-dinucleotide: I161 (= I161), I162 (≠ T162), P163 (= P163), W164 (≠ F164), K188 (= K188), E191 (= E191), G221 (≠ K221), G225 (≠ D225), A226 (= A226), F239 (= F238), G241 (= G240), S242 (= S241), T245 (≠ I244), Y248 (= Y247), L264 (≠ G263), C297 (= C296), Q344 (≠ H343), R347 (≠ K346), E394 (= E397), F396 (= F399)
Query Sequence
>H281DRAFT_02373 FitnessBrowser__Burk376:H281DRAFT_02373
MSETYQEEGVRADAGTRALTHFINGKAIDGTSGRFGDVFNPALGDVAARVPLASVAEVDA
AVAAAYAAFPAWSETAPIKRARVLFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRG
IEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVVGITPFNFPMMVPCWMFPVAIA
CGNTFVLKPSERDPSASNRLAELLKEAGLPDGVFNVVHGDKVAVDALLVHPDVSAVSFVG
STPIAEYIHTEGTKHGKRVQALGGAKNHLVVMPDADLDQAVDALIGAAYGSAGERCMAIS
VAVAVGHIADELIERLTPRVESLKIMNGMESAAEMGPLVTAVHREKVVGYIEAGIAEGAK
LVVDGRGHRVDGHEKGFFLGGTLFDDVSTDMKIYREEIFGPVLCVVRVPDFASAVELINA
NDFANGVSLFTSDGGIARAFSRQIQIGMVGINVPIPVPMAWHSFGGWKKSLFGDHHAYGE
EGVRFYTRYKSIMQRWPDSIAKGAEFTMPVAK
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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