SitesBLAST
Comparing BWI76_RS03795 FitnessBrowser__Koxy:BWI76_RS03795 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)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
49% identity, 99% coverage: 2:454/456 of query aligns to 1:453/455 of 4ywuA
- active site: N131 (= N132), K154 (= K155), E228 (= E229), C262 (= C263), E359 (= E360), E436 (= E437)
- binding 4-oxobutanoic acid: N131 (= N132), Q136 (= Q137), R139 (= R140), E228 (= E229), V261 (= V262), C262 (= C263), F425 (= F426)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
49% identity, 99% coverage: 2:454/456 of query aligns to 1:453/455 of 4ohtA
- active site: N131 (= N132), K154 (= K155), E228 (= E229), C262 (= C263), E359 (= E360), E436 (= E437)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (= V128), E128 (= E129), P129 (= P130), W130 (= W131), K154 (= K155), H155 (= H156), A156 (= A157), S157 (= S158), Y187 (≠ Q188), S207 (= S208), I214 (≠ V215)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
43% identity, 99% coverage: 2:452/456 of query aligns to 1:450/453 of 4itbA
- active site: N130 (= N132), K153 (= K155), E227 (= E229), C261 (= C263), E358 (= E360), E435 (= E437)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (= V128), M127 (≠ E129), P128 (= P130), W129 (= W131), N130 (= N132), K153 (= K155), A155 (= A157), S156 (= S158), A186 (≠ Q188), V189 (= V191), G205 (= G207), S206 (= S208), A209 (= A211), S212 (≠ V214), L228 (= L230), C261 (= C263), E358 (= E360), F360 (= F362)
- binding 4-oxobutanoic acid: E227 (= E229), C261 (= C263), S418 (≠ T420)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
42% identity, 99% coverage: 2:452/456 of query aligns to 1:450/453 of 3vz3A
- active site: N130 (= N132), K153 (= K155), E227 (= E229), A261 (≠ C263), E358 (= E360), E435 (= E437)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (= V128), M127 (≠ E129), W129 (= W131), N130 (= N132), Q135 (= Q137), R138 (= R140), K153 (= K155), A155 (= A157), S156 (= S158), A186 (≠ Q188), V189 (= V191), T204 (= T206), G205 (= G207), S206 (= S208), A209 (= A211), E227 (= E229), L228 (= L230), G229 (= G231), A261 (≠ C263), F360 (= F362)
- binding 4-oxobutanoic acid: F131 (= F133), W134 (≠ Y136), S260 (≠ V262), A261 (≠ C263), I262 (≠ T264), S418 (≠ T420)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
42% identity, 98% coverage: 5:452/456 of query aligns to 8:454/459 of 3efvA
- active site: N134 (= N132), E231 (= E229), C265 (= C263), E439 (= E437)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ V128), M131 (≠ E129), P132 (= P130), W133 (= W131), N134 (= N132), Q139 (= Q137), R142 (= R140), K157 (= K155), A159 (= A157), N190 (≠ Q188), V193 (= V191), T208 (= T206), G209 (= G207), S210 (= S208), A213 (= A211), E231 (= E229), L232 (= L230), G233 (= G231), C265 (= C263), E362 (= E360), F364 (= F362), F428 (= F426)
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)
34% identity, 98% coverage: 6:452/456 of query aligns to 28:482/497 of P17202
- I28 (≠ V6) binding
- D96 (≠ E73) binding
- SPW 156:158 (≠ EPW 129:131) binding
- Y160 (≠ F133) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R140) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAS 155:158) binding
- L186 (≠ I159) binding
- SSAT 236:239 (≠ SEKA 208:211) binding
- V251 (≠ I223) binding in other chain
- L258 (= L230) binding
- W285 (≠ N257) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E360) binding
- A441 (≠ M411) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ T420) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F426) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K430) binding
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
34% identity, 99% coverage: 2:454/456 of query aligns to 26:479/481 of 3jz4A
- active site: N156 (= N132), K179 (= K155), E254 (= E229), C288 (= C263), E385 (= E360), E462 (= E437)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P130), W155 (= W131), K179 (= K155), A181 (= A157), S182 (= S158), A212 (≠ Q188), G216 (≠ A192), G232 (= G207), S233 (= S208), I236 (≠ A211), C288 (= C263), K338 (≠ T313), E385 (= E360), F387 (= F362)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
34% identity, 99% coverage: 2:454/456 of query aligns to 27:480/482 of P25526
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
35% identity, 99% coverage: 6:455/456 of query aligns to 30:490/505 of O24174
- N164 (= N132) 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 (≠ R140) 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
34% identity, 98% coverage: 6:452/456 of query aligns to 26:480/495 of 4v37A
- active site: N157 (= N132), K180 (= K155), E255 (= E229), A289 (≠ C263), E388 (= E360), E465 (= E437)
- binding 3-aminopropan-1-ol: C448 (≠ T420), W454 (≠ F426)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V128), S154 (≠ E129), P155 (= P130), W156 (= W131), N157 (= N132), M162 (≠ Q137), K180 (= K155), S182 (≠ A157), E183 (≠ S158), G213 (≠ S187), G217 (≠ V191), A218 (= A192), T232 (= T206), G233 (= G207), S234 (= S208), T237 (≠ A211), E255 (= E229), L256 (= L230), A289 (≠ C263), E388 (= E360), F390 (= F362)
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)
34% identity, 99% coverage: 6:455/456 of query aligns to 28:488/503 of Q93YB2
- I28 (≠ V6) binding
- D99 (≠ E73) binding
- W161 (= W131) binding
- K185 (= K155) binding
- L189 (≠ I159) binding
- S239 (= S208) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
34% identity, 99% coverage: 6:455/456 of query aligns to 25:485/500 of 3iwjA
- active site: N159 (= N132), K182 (= K155), E257 (= E229), C291 (= C263), E390 (= E360), E467 (= E437)
- binding glycerol: D110 (≠ L87), Y160 (≠ F133), W167 (≠ R140), I290 (≠ V262), C291 (= C263), C450 (≠ T420), W456 (≠ F426)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V128), T156 (≠ E129), W158 (= W131), K182 (= K155), S184 (≠ A157), E185 (≠ S158), G215 (≠ S187), A220 (= A192), F233 (≠ L205), G235 (= G207), S236 (= S208), T239 (≠ A211), I243 (≠ V215)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 98% coverage: 7:455/456 of query aligns to 44:496/503 of O14293
- S248 (= S208) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
35% identity, 99% coverage: 2:454/456 of query aligns to 23:476/490 of 5ekcE
- active site: N154 (= N132), K177 (= K155), E252 (= E229), C286 (= C263), E381 (= E360), E459 (= E437)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (≠ V128), T151 (≠ E129), P152 (= P130), W153 (= W131), K177 (= K155), S180 (= S158), G210 (≠ D189), G214 (vs. gap), F228 (≠ L205), G230 (= G207), E231 (≠ S208), T234 (≠ A211), N331 (≠ S307), R333 (≠ D309), Q334 (≠ A310)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
35% identity, 99% coverage: 2:454/456 of query aligns to 16:469/482 of 5ek6A
- active site: N147 (= N132), K170 (= K155), E245 (= E229), C279 (= C263), E374 (= E360), E452 (= E437)
- binding 2-methylpropanal: I152 (≠ Q137), K155 (≠ R140), T222 (= T206), E245 (= E229), F441 (= F426)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (≠ V128), T144 (≠ E129), W146 (= W131), N147 (= N132), I152 (≠ Q137), K170 (= K155), A172 (= A157), S173 (= S158), P202 (≠ Q188), G203 (≠ D189), G207 (vs. gap), F221 (≠ L205), T222 (= T206), G223 (= G207), E224 (≠ S208), T227 (≠ A211), I231 (≠ V215), E245 (= E229), L246 (= L230), C279 (= C263), E374 (= E360)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
35% identity, 99% coverage: 2:454/456 of query aligns to 16:469/482 of 4h73A
- active site: N147 (= N132), K170 (= K155), E245 (= E229), C279 (= C263), E374 (= E360), E452 (= E437)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (≠ V128), T144 (≠ E129), P145 (= P130), W146 (= W131), K170 (= K155), A172 (= A157), S173 (= S158), G203 (≠ D189), G207 (vs. gap), F221 (≠ L205), G223 (= G207), E224 (≠ S208), T227 (≠ A211)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
34% identity, 99% coverage: 6:455/456 of query aligns to 24:478/489 of 4o6rA
- active site: N150 (= N132), K173 (= K155), E248 (= E229), C282 (= C263), E383 (= E360), E460 (= E437)
- binding adenosine monophosphate: I146 (≠ V128), V147 (≠ E129), K173 (= K155), G206 (≠ D189), G210 (vs. gap), Q211 (vs. gap), F224 (≠ L205), G226 (= G207), S227 (= S208), T230 (≠ A211), R233 (≠ V214)
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
36% identity, 91% coverage: 40:453/456 of query aligns to 63:483/500 of 4i8pA
- active site: N159 (= N132), K182 (= K155), E257 (= E229), C291 (= C263), E390 (= E360), E467 (= E437)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V128), T156 (≠ E129), P157 (= P130), W158 (= W131), N159 (= N132), M164 (≠ Q137), K182 (= K155), S184 (≠ A157), E185 (≠ S158), G215 (≠ S187), G219 (≠ V191), A220 (= A192), T234 (= T206), G235 (= G207), S236 (= S208), T239 (≠ A211), E257 (= E229), L258 (= L230), C291 (= C263), E390 (= E360), F392 (= F362), W456 (≠ F426)
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, 91% coverage: 40:453/456 of query aligns to 68:488/505 of C0P9J6
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
32% identity, 99% coverage: 6:455/456 of query aligns to 23:483/497 of 3iwkH
- active site: N157 (= N132), K180 (= K155), E255 (= E229), C289 (= C263), E388 (= E360), E465 (= E437)
- binding nicotinamide-adenine-dinucleotide: W156 (= W131), G213 (≠ S187), G217 (≠ V191), A218 (= A192), G233 (= G207), S234 (= S208), T237 (≠ A211), K240 (≠ V214), C289 (= C263), Q336 (≠ A310), E388 (= E360), F390 (= F362)
Query Sequence
>BWI76_RS03795 FitnessBrowser__Koxy:BWI76_RS03795
MAYQTVNPANNQLIKAYPSHSDADVEAALQKADALYHSSWSKGDIAQRLSVLHKLADLID
SRVDELAKIASQEMGKLIEQSRGEVKLCAQIARYYADNAKQFLAPVKYPSELGEAWVEHH
PIGVLMAVEPWNFPYYQLMRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGA
WTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKATLELGGNDVFVVLD
DADLAKAVKIGVQARLNNAGQVCTAAKRFILHEKIADAFLSQFTEAFRQVKIGDPLDEST
TLGPLSSKDALETLTRQVNDALKNGAKLHLGGKPAQREGSFFEPTILTGITRDNPAYFEE
FFGPVAQIYVVKDDDEAVKLANDSHYGLGGAVFSQDIERAKRMASRIETGMVYINWLTDT
APELPFGGVKRSGFGRELSDLGIKEFVNQKLVVVHK
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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