SitesBLAST
Comparing BPHYT_RS28770 FitnessBrowser__BFirm:BPHYT_RS28770 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)
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
35% identity, 97% coverage: 5:471/480 of query aligns to 19:489/505 of 4neaA
- active site: N166 (= N149), K189 (= K172), E264 (= E247), C298 (= C281), E399 (= E379), E476 (= E458)
- binding nicotinamide-adenine-dinucleotide: P164 (= P147), K189 (= K172), E192 (= E175), G222 (= G205), G226 (= G209), G242 (= G225), G243 (≠ S226), T246 (= T229), H249 (≠ A232), I250 (= I233), C298 (= C281), E399 (= E379), F401 (= F381)
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)
35% identity, 97% coverage: 7:471/480 of query aligns to 11:480/497 of P17202
- I28 (≠ V22) binding
- D96 (≠ E89) binding
- SPW 156:158 (≠ TPW 146:148) binding
- Y160 (≠ F150) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 172:175) binding
- L186 (= L176) binding
- SSAT 236:239 (≠ SVGT 226:229) binding
- V251 (≠ G241) binding in other chain
- L258 (≠ M248) binding
- W285 (≠ Y275) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding
- A441 (≠ M430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G439) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F446) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K450) binding
7radA Crystal structure analysis of aldh1b1
38% identity, 98% coverage: 7:475/480 of query aligns to 16:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I145), I159 (≠ T146), P160 (= P147), W161 (= W148), N162 (= N149), M167 (≠ I154), K185 (= K172), E188 (= E175), G218 (= G205), G222 (= G209), A223 (≠ E210), T237 (= T224), G238 (= G225), S239 (= S226), V242 (≠ T229), E261 (= E247), L262 (≠ M248), C295 (= C281), E392 (= E379), F394 (= F381)
- 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 (≠ R103), F163 (= F150), E285 (≠ N271), F289 (≠ Y275), N450 (≠ T437), V452 (= V440)
7mjdA Crystal structure analysis of aldh1b1
38% identity, 98% coverage: 7:475/480 of query aligns to 16:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I145), I159 (≠ T146), P160 (= P147), W161 (= W148), N162 (= N149), M167 (≠ I154), K185 (= K172), E188 (= E175), G218 (= G205), G222 (= G209), F236 (= F223), T237 (= T224), G238 (= G225), S239 (= S226), V242 (≠ T229), E261 (= E247), L262 (≠ M248), C295 (= C281), E392 (= E379), F394 (= F381)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R103), E285 (≠ N271), F289 (≠ Y275), N450 (≠ T437), V452 (= V440)
7mjcA Crystal structure analysis of aldh1b1
38% identity, 98% coverage: 7:475/480 of query aligns to 16:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I145), I159 (≠ T146), P160 (= P147), W161 (= W148), N162 (= N149), K185 (= K172), E188 (= E175), G218 (= G205), G222 (= G209), T237 (= T224), G238 (= G225), S239 (= S226), V242 (≠ T229), E261 (= E247), L262 (≠ M248), C295 (= C281), E392 (= E379), F394 (= F381)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 97% coverage: 7:471/480 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N149), K180 (= K172), E255 (= E247), A289 (≠ C281), E388 (= E379), E465 (= E458)
- binding 3-aminopropan-1-ol: C448 (≠ G439), W454 (≠ F446)
- binding nicotinamide-adenine-dinucleotide: I153 (= I145), S154 (≠ T146), P155 (= P147), W156 (= W148), N157 (= N149), M162 (≠ I154), K180 (= K172), S182 (≠ A174), E183 (= E175), G213 (= G205), G217 (= G209), A218 (≠ E210), T232 (= T224), G233 (= G225), S234 (= S226), T237 (= T229), E255 (= E247), L256 (≠ M248), A289 (≠ C281), E388 (= E379), F390 (= F381)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 99% coverage: 3:475/480 of query aligns to 16:488/491 of 5gtlA
- active site: N165 (= N149), K188 (= K172), E263 (= E247), C297 (= C281), E394 (= E379), E471 (= E458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I145), P163 (= P147), K188 (= K172), A190 (= A174), E191 (= E175), Q192 (≠ L176), G221 (= G205), G225 (= G209), G241 (= G225), S242 (= S226), T245 (= T229), L264 (≠ M248), C297 (= C281), E394 (= E379), F396 (= F381)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 99% coverage: 3:475/480 of query aligns to 16:488/491 of 5gtkA
- active site: N165 (= N149), K188 (= K172), E263 (= E247), C297 (= C281), E394 (= E379), E471 (= E458)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ T146), P163 (= P147), W164 (= W148), K188 (= K172), E191 (= E175), G221 (= G205), G225 (= G209), A226 (≠ E210), F239 (= F223), G241 (= G225), S242 (= S226), T245 (= T229), Y248 (≠ A232), L264 (≠ M248), C297 (= C281), Q344 (= Q328), R347 (≠ Q331), E394 (= E379), F396 (= F381)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 97% coverage: 7:471/480 of query aligns to 13:485/505 of O24174
- N164 (= N149) 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 (= W157) 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.
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)
33% identity, 99% coverage: 1:475/480 of query aligns to 7:485/487 of Q9H2A2
- R109 (= R103) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N149) mutation to A: Complete loss of activity.
- R451 (≠ G439) mutation to A: Complete loss of activity.
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
35% identity, 99% coverage: 3:479/480 of query aligns to 10:486/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W148), K180 (= K172), A182 (= A174), T212 (≠ M204), G213 (= G205), G217 (= G209), F231 (= F223), G233 (= G225), S234 (= S226), V237 (≠ T229), Q337 (= Q328), E388 (= E379), F390 (= F381)
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)
37% identity, 97% coverage: 7:471/480 of query aligns to 11:483/503 of Q8VWZ1
- N27 (= N21) binding
- I28 (≠ V22) binding
- D99 (≠ E89) binding
- L189 (= L176) binding
- 238:245 (vs. 225:232, 50% identical) binding
- C294 (= C281) binding
- E393 (= E379) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
37% identity, 97% coverage: 7:471/480 of query aligns to 6:478/497 of 3iwkH
- active site: N157 (= N149), K180 (= K172), E255 (= E247), C289 (= C281), E388 (= E379), E465 (= E458)
- binding nicotinamide-adenine-dinucleotide: W156 (= W148), G213 (= G205), G217 (= G209), A218 (≠ E210), G233 (= G225), S234 (= S226), T237 (= T229), K240 (≠ A232), C289 (= C281), Q336 (= Q328), E388 (= E379), F390 (= F381)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 98% coverage: 5:472/480 of query aligns to 12:483/494 of 4pz2B
- active site: N159 (= N149), K182 (= K172), E258 (= E247), C292 (= C281), E392 (= E379), D469 (≠ E458)
- binding nicotinamide-adenine-dinucleotide: I155 (= I145), I156 (≠ T146), P157 (= P147), W158 (= W148), N159 (= N149), M164 (≠ I154), K182 (= K172), A184 (= A174), E185 (= E175), G215 (= G205), G219 (= G209), F233 (= F223), T234 (= T224), G235 (= G225), S236 (= S226), V239 (≠ T229), E258 (= E247), L259 (≠ M248), C292 (= C281), E392 (= E379), F394 (= F381)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
35% identity, 99% coverage: 3:479/480 of query aligns to 9:485/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I145), T153 (= T146), P154 (= P147), W155 (= W148), N156 (= N149), I161 (= I154), K179 (= K172), A181 (= A174), E182 (= E175), T211 (≠ M204), G212 (= G205), G216 (= G209), Q217 (≠ E210), F230 (= F223), T231 (= T224), G232 (= G225), S233 (= S226), V236 (≠ T229), E255 (= E247), L256 (≠ M248), G257 (= G249), A289 (≠ C281), E387 (= E379), F389 (= F381)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 97% coverage: 7:471/480 of query aligns to 13:475/481 of 3jz4A
- active site: N156 (= N149), K179 (= K172), E254 (= E247), C288 (= C281), E385 (= E379), E462 (= E458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P147), W155 (= W148), K179 (= K172), A181 (= A174), S182 (≠ E175), A212 (≠ G205), G216 (= G209), G232 (= G225), S233 (= S226), I236 (≠ T229), C288 (= C281), K338 (≠ Q331), E385 (= E379), F387 (= F381)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
37% identity, 98% coverage: 7:475/480 of query aligns to 16:486/493 of 4fr8A
- active site: N162 (= N149), K185 (= K172), Q261 (≠ E247), C295 (= C281), E392 (= E379), E469 (= E458)
- binding nicotinamide-adenine-dinucleotide: I158 (= I145), I159 (≠ T146), W161 (= W148), K185 (= K172), G218 (= G205), G222 (= G209), A223 (≠ E210), F236 (= F223), G238 (= G225), S239 (= S226), I242 (≠ T229), Q342 (= Q328), K345 (≠ Q331), E392 (= E379), F394 (= F381)
- binding propane-1,2,3-triyl trinitrate: F163 (= F150), L166 (≠ A153), W170 (= W157), F289 (≠ Y275), S294 (≠ R280), C295 (= C281), D450 (≠ T437), F452 (≠ V440)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
38% identity, 97% coverage: 3:468/480 of query aligns to 13:493/511 of 6fkuA
- active site: N159 (= N149), E261 (= E247), C295 (= C281), E483 (= E458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I145), T156 (= T146), N159 (= N149), K182 (= K172), S184 (≠ A174), E185 (= E175), G214 (≠ M204), G215 (= G205), K216 (≠ S206), G220 (= G209), Q221 (≠ E210), F237 (= F223), T238 (= T224), G239 (= G225), S240 (= S226), V243 (≠ T229), E261 (= E247), L262 (≠ M248), C295 (= C281), R342 (≠ K327), F343 (≠ Q328), E404 (= E379), F406 (= F381)
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
36% identity, 98% coverage: 7:476/480 of query aligns to 8:487/500 of 4i8pA
- active site: N159 (= N149), K182 (= K172), E257 (= E247), C291 (= C281), E390 (= E379), E467 (= E458)
- binding nicotinamide-adenine-dinucleotide: I155 (= I145), T156 (= T146), P157 (= P147), W158 (= W148), N159 (= N149), M164 (≠ I154), K182 (= K172), S184 (≠ A174), E185 (= E175), G215 (= G205), G219 (= G209), A220 (≠ E210), T234 (= T224), G235 (= G225), S236 (= S226), T239 (= T229), E257 (= E247), L258 (≠ M248), C291 (= C281), E390 (= E379), F392 (= F381), W456 (≠ F446)
C0P9J6 Aminoaldehyde dehydrogenase 1a; ZmAMADH1a; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a; Aminobutyraldehyde dehydrogenase AMADH1a; Betaine aldehyde dehydrogenase AMADH1a; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Zea mays (Maize) (see paper)
36% identity, 98% coverage: 7:476/480 of query aligns to 13:492/505 of C0P9J6
Query Sequence
>BPHYT_RS28770 FitnessBrowser__BFirm:BPHYT_RS28770
MTQFKNFVGGEWVDGNDFAPNVNPSDTSDVIGHFARASADQTQKAIASARSAFRTWSLST
PQQRFDLLDQAGSTILARKNELGKLLAREEGKTLAEAVGEVGRAGQIFKFFAGEALRVGG
EILPSVRPGLTVEVTREPVGVIGLITPWNFPIAIPAWKIAPALAYGNCVVIKPAELVPGS
VWELVKIIAEAGAPAGVINLVMGMGSIVGEILVMSADVDAVSFTGSVGTGQAIAAKCVAT
GKKFQLEMGGKNPMVVLDDADLDVAVEACINGAFYSTGQRCTASSRLIVTSGIHDRFVEA
MLARMRSLKIGNALDASTQIGPVVDAKQLEQDERYIELARNEGGSVFGGERVTSATEGFF
LAPALVTNTTPAMTINREEVFGPVASVIKVANYEEALAVANDSPFGLSAGICTMSLAHAS
HFKRHVQAGMVMINTATAGVDYHVPFGGRKGSSLGPREQGTYAREFYTIVKTAYVAPGNV
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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