SitesBLAST
Comparing RR42_RS11330 FitnessBrowser__Cup4G11:RR42_RS11330 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
52% identity, 99% coverage: 5:476/477 of query aligns to 12:483/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (= T144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (= E173), G210 (= G203), P211 (= P204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E379), F388 (= F381), F451 (= F444)
- binding octanal: W155 (≠ Y148), S285 (≠ T278)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
48% identity, 99% coverage: 3:472/477 of query aligns to 4:477/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E379), E460 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ P204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (≠ R230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E379), F386 (= F381)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
43% identity, 99% coverage: 1:470/477 of query aligns to 2:449/454 of 3ty7B
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)
41% identity, 97% coverage: 6:470/477 of query aligns to 9:482/497 of P17202
- I28 (= I25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ TPW 144:146) binding
- Y160 (= Y148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ L155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 170:173) binding
- L186 (≠ V174) binding
- SSAT 236:239 (≠ STRA 224:227) binding
- V251 (= V239) binding in other chain
- L258 (= L246) binding
- W285 (≠ L273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding
- A441 (≠ Q430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ F438) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F444) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K448) binding
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
42% identity, 98% coverage: 4:470/477 of query aligns to 9:487/505 of O24174
- N164 (= N147) 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 (≠ L155) 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.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
40% identity, 97% coverage: 6:470/477 of query aligns to 7:480/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E379), E465 (= E455)
- binding 3-aminopropan-1-ol: C448 (≠ F438), W454 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), S154 (≠ T144), P155 (= P145), W156 (= W146), N157 (= N147), M162 (≠ Q152), K180 (= K170), S182 (= S172), E183 (= E173), G213 (= G203), G217 (= G207), A218 (≠ E208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E379), F390 (= F381)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 99% coverage: 1:470/477 of query aligns to 13:486/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E379), E471 (= E455)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (= E173), Q192 (≠ V174), G221 (= G203), G225 (= G207), G241 (= G223), S242 (= S224), T245 (≠ A227), L264 (= L246), C297 (= C279), E394 (= E379), F396 (= F381)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 99% coverage: 1:470/477 of query aligns to 13:486/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E379), E471 (= E455)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ T144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (= E173), G221 (= G203), G225 (= G207), A226 (≠ E208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ R230), L264 (= L246), C297 (= C279), Q344 (= Q326), R347 (= R329), E394 (= E379), F396 (= F381)
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)
39% identity, 97% coverage: 6:470/477 of query aligns to 19:491/505 of 4neaA
- active site: N166 (= N147), K189 (= K170), E264 (= E245), C298 (= C279), E399 (= E379), E476 (= E455)
- binding nicotinamide-adenine-dinucleotide: P164 (= P145), K189 (= K170), E192 (= E173), G222 (= G203), G226 (= G207), G242 (= G223), G243 (≠ S224), T246 (≠ A227), H249 (≠ R230), I250 (≠ V231), C298 (= C279), E399 (= E379), F401 (= F381)
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)
41% identity, 97% coverage: 6:470/477 of query aligns to 9:485/503 of Q93YB2
- I28 (= I25) binding
- D99 (≠ E91) binding
- W161 (= W146) binding
- K185 (= K170) binding
- L189 (≠ V174) binding
- S239 (= S224) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
41% identity, 97% coverage: 6:470/477 of query aligns to 6:482/500 of 3iwjA
- active site: N159 (= N147), K182 (= K170), E257 (= E245), C291 (= C279), E390 (= E379), E467 (= E455)
- binding glycerol: D110 (≠ Q103), Y160 (= Y148), W167 (≠ L155), I290 (≠ T278), C291 (= C279), C450 (≠ F438), W456 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I155 (= I143), T156 (= T144), W158 (= W146), K182 (= K170), S184 (= S172), E185 (= E173), G215 (= G203), A220 (≠ E208), F233 (= F221), G235 (= G223), S236 (= S224), T239 (≠ A227), I243 (≠ V231)
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)
42% identity, 97% coverage: 6:470/477 of query aligns to 9:485/503 of Q8VWZ1
- N27 (≠ V24) binding
- I28 (= I25) binding
- D99 (≠ E91) binding
- L189 (≠ V174) binding
- 238:245 (vs. 223:230, 38% identical) binding
- C294 (= C279) binding
- E393 (= E379) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
42% identity, 97% coverage: 6:470/477 of query aligns to 4:480/497 of 3iwkH
- active site: N157 (= N147), K180 (= K170), E255 (= E245), C289 (= C279), E388 (= E379), E465 (= E455)
- binding nicotinamide-adenine-dinucleotide: W156 (= W146), G213 (= G203), G217 (= G207), A218 (≠ E208), G233 (= G223), S234 (= S224), T237 (≠ A227), K240 (≠ R230), C289 (= C279), Q336 (= Q326), E388 (= E379), F390 (= F381)
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
41% identity, 97% coverage: 6:470/477 of query aligns to 6:482/500 of 4i8pA
- active site: N159 (= N147), K182 (= K170), E257 (= E245), C291 (= C279), E390 (= E379), E467 (= E455)
- binding nicotinamide-adenine-dinucleotide: I155 (= I143), T156 (= T144), P157 (= P145), W158 (= W146), N159 (= N147), M164 (≠ Q152), K182 (= K170), S184 (= S172), E185 (= E173), G215 (= G203), G219 (= G207), A220 (≠ E208), T234 (= T222), G235 (= G223), S236 (= S224), T239 (≠ A227), E257 (= E245), L258 (= L246), C291 (= C279), E390 (= E379), F392 (= F381), W456 (≠ F444)
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)
41% identity, 97% coverage: 6:470/477 of query aligns to 11:487/505 of C0P9J6
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
41% identity, 97% coverage: 6:470/477 of query aligns to 9:485/503 of Q84LK3
- N162 (= N147) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ L155) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 98% coverage: 6:472/477 of query aligns to 21:493/501 of Q56YU0
- G152 (≠ S130) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A396) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Q56R04 Aminoaldehyde dehydrogenase 1; SlAMADH1; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Betaine aldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; 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 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) (see paper)
41% identity, 98% coverage: 4:470/477 of query aligns to 10:486/504 of Q56R04
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
42% identity, 97% coverage: 6:470/477 of query aligns to 12:484/494 of 4pz2B
- active site: N159 (= N147), K182 (= K170), E258 (= E245), C292 (= C279), E392 (= E379), D469 (≠ E455)
- binding nicotinamide-adenine-dinucleotide: I155 (= I143), I156 (≠ T144), P157 (= P145), W158 (= W146), N159 (= N147), M164 (≠ Q152), K182 (= K170), A184 (≠ S172), E185 (= E173), G215 (= G203), G219 (= G207), F233 (= F221), T234 (= T222), G235 (= G223), S236 (= S224), V239 (≠ A227), E258 (= E245), L259 (= L246), C292 (= C279), E392 (= E379), F394 (= F381)
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
41% identity, 98% coverage: 4:470/477 of query aligns to 5:481/496 of 4i9bA
- active site: N157 (= N147), K180 (= K170), E255 (= E245), C290 (= C279), E389 (= E379), D466 (≠ E455)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C279), W455 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), T154 (= T144), W156 (= W146), K180 (= K170), S182 (= S172), E183 (= E173), G213 (= G203), G217 (= G207), G218 (≠ E208), F231 (= F221), S234 (= S224), T237 (≠ A227), I241 (≠ V231)
Query Sequence
>RR42_RS11330 FitnessBrowser__Cup4G11:RR42_RS11330
MQQRDKLFINGKWVAPHGTGLINVIHSTTEAVMGRIPEGHARDAEDAIQAARAAFDSWSA
TPPSVRAGYIRKIAEGLKARSEELAQLIAGEVGMPIKMARAIQVGGPVYNWAQAAKLLDT
FAFEEEVGNSLVVREPVGVVAAITPWNYPLNQITLKVAPALAAGCTVVLKPSEVAPLNAF
VLAEVIEAAGLPPGVFNLVTGYGPVVGEVLASHPEVDMVSFTGSTRAGKRVSELGAQSVK
RVALELGGKSASVILDDADLAAAVKGTVGACFLNSGQTCSAHTRMLVPRARYDEVKAIAR
KVVEGYTVGDPLLESSRLGPLISAAQKDRVTGYIQRGINEGAELVAGGPEAPEGLDKGFF
VKPTVLGNVDPKATVAQEEIFGPVLSIICYDTEEDAVRIANDSIYGLGGGVWSGDEARAI
RVARRIRTGQVDINGGPFNMQAPFGGYKQSGNGREAGKYGLEEFLEYKSLQMKKPAA
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