SitesBLAST
Comparing BPHYT_RS28825 FitnessBrowser__BFirm:BPHYT_RS28825 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)
61% identity, 95% coverage: 15:494/507 of query aligns to 4:484/489 of 4zz7A
- active site: N149 (= N161), K172 (= K184), L246 (= L258), C280 (= C292), E382 (= E392), A462 (= A472)
- 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 (= I240), L246 (= L258), G247 (= G259), C280 (= C292), E382 (= E392), F384 (= F394)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
61% identity, 94% coverage: 15:492/507 of query aligns to 3:456/468 of 5tjrD
- active site: N144 (= N161), K167 (= K184), L241 (= L258), C270 (= C292), E356 (= E392), A436 (= A472)
- binding adenosine-5'-diphosphate: I140 (= I157), T141 (= T158), F143 (= F160), K167 (= K184), E170 (= E187), K200 (= K217), F217 (= F234), S220 (= S237), I223 (= I240)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
58% identity, 95% coverage: 14:495/507 of query aligns to 6:489/491 of 4iymC
- active site: N153 (= N161), K176 (= K184), F250 (≠ L258), C284 (= C292), E386 (= E392), Q466 (≠ A472)
- 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 (= I240), G251 (= G259), C284 (= C292), E386 (= E392), F388 (= F394)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
48% identity, 95% coverage: 12:492/507 of query aligns to 2:480/484 of 1t90A
- active site: N151 (= N161), K174 (= K184), L248 (= L258), C282 (= C292), E380 (= E392), A460 (= A472)
- binding nicotinamide-adenine-dinucleotide: I147 (= I157), A148 (≠ T158), P149 (= P159), F150 (= F160), N151 (= N161), W159 (= W169), K174 (= K184), E177 (= E187), R178 (= R188), H207 (≠ K217), V225 (= V235), G226 (= G236), S227 (= S237), V230 (≠ I240), L248 (= L258), T249 (≠ G259), C282 (= C292), E380 (= E392), F382 (= F394)
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: 12:492/507 of query aligns to 4:482/487 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 (≠ M168) 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 (= R188) binding
- S229 (= S237) binding
- T251 (≠ G259) binding
- R283 (= R291) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I295) 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 (≠ V359) 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 (≠ S423) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
35% identity, 93% coverage: 17:487/507 of query aligns to 29:501/515 of 2d4eC
- active site: N173 (= N161), K196 (= K184), E271 (≠ L258), C305 (= C292), E409 (= E392), E486 (≠ A472)
- binding nicotinamide-adenine-dinucleotide: I169 (= I157), T170 (= T158), P171 (= P159), W172 (≠ F160), K196 (= K184), A198 (≠ S186), G229 (≠ D216), G233 (≠ V220), A234 (≠ D221), T248 (≠ V235), G249 (= G236), E250 (≠ S237), T253 (≠ I240), E271 (≠ L258), L272 (≠ G259), C305 (= C292), E409 (= E392), F411 (= F394), F475 (= F459)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
34% identity, 95% coverage: 8:487/507 of query aligns to 9:486/497 of 8skfA
- binding calcium ion: T33 (≠ V34), I34 (≠ F35), D100 (≠ E101), V187 (≠ R188)
- binding nicotinamide-adenine-dinucleotide: I156 (= I157), G157 (≠ T158), A158 (≠ P159), W159 (≠ F160), K183 (= K184), E186 (= E187), G216 (≠ K217), G220 (vs. gap), T235 (≠ V235), G236 (= G236), G237 (≠ S237), S240 (≠ I240), K243 (≠ Y243), E259 (≠ A257), C293 (= C292), F396 (= F394)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
31% identity, 93% coverage: 17:488/507 of query aligns to 22:493/503 of 1bpwA
- active site: N166 (= N161), K189 (= K184), E263 (≠ L258), C297 (= C292), E400 (= E392), E477 (≠ H470)
- binding nicotinamide-adenine-dinucleotide: I162 (= I157), L163 (≠ T158), W165 (≠ F160), N166 (= N161), K189 (= K184), G221 (≠ D216), G225 (≠ V220), T240 (≠ V235), G241 (= G236), S242 (= S237), T245 (≠ I240), E263 (≠ L258), L264 (≠ G259), 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)
31% identity, 93% coverage: 17:488/507 of query aligns to 22:493/503 of P56533
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8vqwC
- binding coenzyme a: I147 (= I157), W150 (≠ F160), K174 (= K184), S176 (= S186), E177 (= E187), G207 (≠ K217), G211 (vs. gap), F225 (= F234), G227 (= G236), G228 (≠ S237), S231 (≠ I240), H331 (= H339), F387 (= F394)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8vj3A
8uzoA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (adp bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8uzoA
8uznA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (amp bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8uznA
- binding adenosine monophosphate: I147 (= I157), G148 (≠ T158), K174 (= K184), S176 (= S186), E177 (= E187), G207 (≠ K217), G211 (vs. gap), F225 (= F234), G228 (≠ S237), S231 (≠ I240), K234 (≠ Y243)
8uzmA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADPH bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8uzmA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G148 (≠ T158), W150 (≠ F160), K174 (= K184), S176 (= S186), E177 (= E187), G207 (≠ K217), G211 (vs. gap), F225 (= F234), T226 (≠ V235), G227 (= G236), G228 (≠ S237), S231 (≠ I240), E250 (≠ A257), G252 (= G259), C284 (= C292), E385 (= E392), F387 (= F394)
8uzkA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADP+ bound)
35% identity, 94% coverage: 9:487/507 of query aligns to 1:477/488 of 8uzkA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I147 (= I157), G148 (≠ T158), W150 (≠ F160), N151 (= N161), K174 (= K184), S176 (= S186), E177 (= E187), G207 (≠ K217), G211 (vs. gap), F225 (= F234), G227 (= G236), G228 (≠ S237), S231 (≠ I240), E250 (≠ A257), F387 (= F394)
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)
31% identity, 94% coverage: 12:487/507 of query aligns to 8:483/494 of P49189
- C116 (≠ V119) 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)
31% identity, 94% coverage: 12:487/507 of query aligns to 7:482/493 of 6vr6D
- active site: N156 (= N161), E253 (≠ L258), C287 (= C292), E467 (≠ H470)
- binding nicotinamide-adenine-dinucleotide: I152 (= I157), G153 (≠ T158), W155 (≠ F160), K179 (= K184), A212 (≠ K217), G215 (≠ V220), Q216 (≠ D221), F229 (= F234), G231 (= G236), S232 (= S237), T235 (≠ I240), I239 (= I244)
Query Sequence
>BPHYT_RS28825 FitnessBrowser__BFirm:BPHYT_RS28825
MNAANEQAKLSVQQLGHYIGGAPAAPTSGRFKDVFNPATGKVTGSVALASVEEVDAAVQA
ARAAFPAWSETAPLKRARILFRFKELLNQHHDELAMLITREHGKVFTDAQGEVVRGIEVV
EFACGIPNLLKTDFTDQIGGGIDNWNLRQALGVVAGITPFNFPVMVPMWMFPVALACGNT
FVLKPSERDPSASLRLAELLKEAGLPDGVFNVVNGDKVAVDALIDHPDVAALSFVGSTPI
AEYIHTEASKRGKRVQALGGAKNHLVVMPDADLDQAVDALIGAAYGSAGERCMAISVAVA
VGNVADKLIEKLVPRVKSLVIKNGEHLDAEMGPLVTAEHKAKVTGYIASGEAEGAKLIVD
GRAHPVTNEEGFFVGGTLFDHVGTEMKIYKEEIFGPVLAVVRVPDFASAVDLINAHEFGN
GVSLFTSDGGVARAFGRQIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGVRF
YTRYKSIMQRWPDSIAKGAEFTMPVAK
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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