SitesBLAST
Comparing WP_017601549.1 NCBI__GCF_000341125.1:WP_017601549.1 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)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
45% identity, 98% coverage: 10:457/458 of query aligns to 22:478/487 of 4go4A
- active site: N149 (= N135), K172 (= K158), E247 (= E233), C281 (= C267), E381 (= E360), E458 (= E437)
- binding nicotinamide-adenine-dinucleotide: I145 (= I131), V146 (= V132), W148 (= W134), N149 (= N135), F154 (≠ V140), K172 (= K158), G205 (= G191), G209 (= G195), Q210 (≠ E196), F223 (= F209), T224 (= T210), G225 (= G211), S226 (= S212), T229 (≠ V215), E247 (= E233), G249 (= G235), C281 (= C267), E381 (= E360), F383 (= F362)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
45% identity, 98% coverage: 10:457/458 of query aligns to 23:480/489 of 4o6rA
- active site: N150 (= N135), K173 (= K158), E248 (= E233), C282 (= C267), E383 (= E360), E460 (= E437)
- binding adenosine monophosphate: I146 (= I131), V147 (= V132), K173 (= K158), G206 (= G191), G210 (= G195), Q211 (≠ E196), F224 (= F209), G226 (= G211), S227 (= S212), T230 (≠ V215), R233 (= R218)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
42% identity, 98% coverage: 6:455/458 of query aligns to 33:489/491 of 5gtlA
- active site: N165 (= N135), K188 (= K158), E263 (= E233), C297 (= C267), E394 (= E360), E471 (= E437)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I131), P163 (= P133), K188 (= K158), A190 (≠ S160), E191 (= E161), Q192 (≠ L162), G221 (= G191), G225 (= G195), G241 (= G211), S242 (= S212), T245 (≠ V215), L264 (= L234), C297 (= C267), E394 (= E360), F396 (= F362)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
42% identity, 98% coverage: 6:455/458 of query aligns to 33:489/491 of 5gtkA
- active site: N165 (= N135), K188 (= K158), E263 (= E233), C297 (= C267), E394 (= E360), E471 (= E437)
- binding nicotinamide-adenine-dinucleotide: I161 (= I131), I162 (≠ V132), P163 (= P133), W164 (= W134), K188 (= K158), E191 (= E161), G221 (= G191), G225 (= G195), A226 (≠ E196), F239 (= F209), G241 (= G211), S242 (= S212), T245 (≠ V215), Y248 (≠ R218), L264 (= L234), C297 (= C267), Q344 (= Q314), R347 (= R317), E394 (= E360), F396 (= F362)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
47% identity, 96% coverage: 12:452/458 of query aligns to 32:484/494 of 4pz2B
- active site: N159 (= N135), K182 (= K158), E258 (= E233), C292 (= C267), E392 (= E360), D469 (≠ E437)
- binding nicotinamide-adenine-dinucleotide: I155 (= I131), I156 (≠ V132), P157 (= P133), W158 (= W134), N159 (= N135), M164 (≠ V140), K182 (= K158), A184 (≠ S160), E185 (= E161), G215 (= G191), G219 (= G195), F233 (= F209), T234 (= T210), G235 (= G211), S236 (= S212), V239 (= V215), E258 (= E233), L259 (= L234), C292 (= C267), E392 (= E360), F394 (= F362)
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)
40% identity, 97% coverage: 10:455/458 of query aligns to 37:494/505 of 4neaA
- active site: N166 (= N135), K189 (= K158), E264 (= E233), C298 (= C267), E399 (= E360), E476 (= E437)
- binding nicotinamide-adenine-dinucleotide: P164 (= P133), K189 (= K158), E192 (= E161), G222 (= G191), G226 (= G195), G242 (= G211), G243 (≠ S212), T246 (≠ V215), H249 (≠ R218), I250 (= I219), C298 (= C267), E399 (= E360), F401 (= F362)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
40% identity, 98% coverage: 9:455/458 of query aligns to 41:496/503 of O14293
- S248 (= S212) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
40% identity, 97% coverage: 10:452/458 of query aligns to 27:482/497 of P17202
- I28 (≠ V11) binding K(+)
- D96 (≠ N77) binding K(+)
- SPW 156:158 (≠ VPW 132:134) binding NAD(+)
- Y160 (≠ F136) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W143) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 158:161) binding NAD(+)
- L186 (= L162) binding K(+)
- SSAT 236:239 (≠ STAV 212:215) binding NAD(+)
- V251 (≠ F227) binding in other chain
- L258 (= L234) binding NAD(+)
- W285 (≠ D261) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E360) binding NAD(+)
- A441 (≠ N411) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V420) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F426) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G430) binding K(+)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
41% identity, 97% coverage: 10:455/458 of query aligns to 57:512/518 of O94788
- A110 (= A60) to V: in dbSNP:rs35365164
- Q182 (≠ V130) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 132:134) binding NAD(+)
- KPAE 210:213 (≠ KPSE 158:161) binding NAD(+)
- STE 264:266 (≠ STA 212:214) binding NAD(+)
- C320 (= C267) active site, Nucleophile
- R347 (≠ I294) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ A295) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ AQRDR 313:317) binding NAD(+)
- A383 (= A326) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E360) binding NAD(+)
- E436 (≠ A379) to K: in dbSNP:rs34744827
- S461 (≠ A404) to Y: in DIH4; decreased retinoic acid biosynthetic process
Sites not aligning to the query:
- 50 E → G: in dbSNP:rs34266719
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
41% identity, 97% coverage: 10:455/458 of query aligns to 31:486/492 of 6b5hA
- active site: N161 (= N135), E260 (= E233), C294 (= C267), E468 (= E437)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (vs. gap), G116 (≠ N91), F162 (= F136), W169 (= W143), Q284 (≠ G257), F288 (≠ D261), T295 (≠ C268), N449 (≠ S418), L451 (≠ V420), N452 (≠ R421), F457 (= F426)
- binding nicotinamide-adenine-dinucleotide: I157 (= I131), I158 (≠ V132), W160 (= W134), N161 (= N135), K184 (= K158), G217 (= G191), G221 (= G195), F235 (= F209), T236 (= T210), G237 (= G211), S238 (= S212), V241 (= V215), E260 (= E233), L261 (= L234), C294 (= C267), F393 (= F362)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
41% identity, 97% coverage: 10:455/458 of query aligns to 31:486/492 of 6b5gA
- active site: N161 (= N135), E260 (= E233), C294 (= C267), E468 (= E437)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F136), L165 (≠ P139), W169 (= W143), F288 (≠ D261), C293 (≠ D266), C294 (= C267), T295 (≠ C268), N449 (≠ S418), L451 (≠ V420)
- binding nicotinamide-adenine-dinucleotide: I157 (= I131), I158 (≠ V132), P159 (= P133), W160 (= W134), N161 (= N135), M166 (≠ V140), K184 (= K158), E187 (= E161), G217 (= G191), G221 (= G195), F235 (= F209), T236 (= T210), G237 (= G211), S238 (= S212), V241 (= V215), E260 (= E233), L261 (= L234), C294 (= C267), E391 (= E360), F393 (= F362)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
41% identity, 97% coverage: 10:455/458 of query aligns to 31:486/492 of 6aljA
- active site: N161 (= N135), E260 (= E233), C294 (= C267), E468 (= E437)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ N91), F162 (= F136), L165 (≠ P139), M166 (≠ V140), W169 (= W143), E260 (= E233), C293 (≠ D266), C294 (= C267), L451 (≠ V420), N452 (≠ R421), A453 (≠ Y422)
- binding nicotinamide-adenine-dinucleotide: I157 (= I131), I158 (≠ V132), P159 (= P133), W160 (= W134), N161 (= N135), K184 (= K158), E187 (= E161), G217 (= G191), G221 (= G195), F235 (= F209), G237 (= G211), S238 (= S212), V241 (= V215), Q341 (= Q314), K344 (≠ R317), E391 (= E360), F393 (= F362)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
40% identity, 97% coverage: 10:455/458 of query aligns to 57:512/518 of Q63639
8rwkA Cryoem structure of the central ald4 filament determined by filamentid (see paper)
39% identity, 98% coverage: 6:452/458 of query aligns to 37:489/495 of 8rwkA
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
40% identity, 97% coverage: 10:452/458 of query aligns to 25:480/495 of 4v37A
- active site: N157 (= N135), K180 (= K158), E255 (= E233), A289 (≠ C267), E388 (= E360), E465 (= E437)
- binding 3-aminopropan-1-ol: C448 (≠ V420), W454 (≠ F426)
- binding nicotinamide-adenine-dinucleotide: I153 (= I131), S154 (≠ V132), P155 (= P133), W156 (= W134), N157 (= N135), M162 (≠ V140), K180 (= K158), S182 (= S160), E183 (= E161), G213 (= G191), G217 (= G195), A218 (≠ E196), T232 (= T210), G233 (= G211), S234 (= S212), T237 (≠ V215), E255 (= E233), L256 (= L234), A289 (≠ C267), E388 (= E360), F390 (= F362)
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
41% identity, 98% coverage: 10:457/458 of query aligns to 24:489/500 of 3iwjA
- active site: N159 (= N135), K182 (= K158), E257 (= E233), C291 (= C267), E390 (= E360), E467 (= E437)
- binding glycerol: D110 (≠ N91), Y160 (≠ F136), W167 (= W143), I290 (≠ D266), C291 (= C267), C450 (≠ V420), W456 (≠ F426)
- binding nicotinamide-adenine-dinucleotide: I155 (= I131), T156 (≠ V132), W158 (= W134), K182 (= K158), S184 (= S160), E185 (= E161), G215 (= G191), A220 (≠ E196), F233 (= F209), G235 (= G211), S236 (= S212), T239 (≠ V215), I243 (= I219)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
41% identity, 99% coverage: 4:457/458 of query aligns to 20:494/505 of O24174
- N164 (= N135) 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 (= W143) 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.
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, 98% coverage: 10:457/458 of query aligns to 27:492/503 of Q93YB2
- I28 (≠ V11) binding Na(+)
- D99 (≠ N77) binding Na(+)
- W161 (= W134) binding NAD(+)
- K185 (= K158) binding NAD(+)
- L189 (= L162) binding Na(+)
- S239 (= S212) binding NAD(+)
7radA Crystal structure analysis of aldh1b1
42% identity, 97% coverage: 11:455/458 of query aligns to 33:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I131), I159 (≠ V132), P160 (= P133), W161 (= W134), N162 (= N135), M167 (≠ V140), K185 (= K158), E188 (= E161), G218 (= G191), G222 (= G195), A223 (≠ E196), T237 (= T210), G238 (= G211), S239 (= S212), V242 (= V215), E261 (= E233), L262 (= L234), C295 (= C267), E392 (= E360), F394 (= F362)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ W87), E117 (≠ N91), F163 (= F136), E285 (≠ G257), F289 (≠ D261), N450 (≠ S418), V452 (= V420)
7mjdA Crystal structure analysis of aldh1b1
42% identity, 97% coverage: 11:455/458 of query aligns to 33:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I131), I159 (≠ V132), P160 (= P133), W161 (= W134), N162 (= N135), M167 (≠ V140), K185 (= K158), E188 (= E161), G218 (= G191), G222 (= G195), F236 (= F209), T237 (= T210), G238 (= G211), S239 (= S212), V242 (= V215), E261 (= E233), L262 (= L234), C295 (= C267), E392 (= E360), F394 (= F362)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ N91), E285 (≠ G257), F289 (≠ D261), N450 (≠ S418), V452 (= V420)
Query Sequence
>WP_017601549.1 NCBI__GCF_000341125.1:WP_017601549.1
MPDEPTFQRVVDPATEAVIAEVPLAGEKEVDAAVERARAAAPAWRAMAPGDRARLLRAVA
ARIDQHREELARTEVRNAGHPVEQARWEAGNARDVFEYFAAAPERATGRQIPVPGGWSVT
FAEPLGVVGVIVPWNFPMPVLSWGAAPALAAGNTVVVKPSELTPLTALRIAELALEAGLP
EGVFQVVPGTGPVAGERLVRHPGVDKVVFTGSTAVGRRIMTAAAEDFTRVTLELGGKSAN
VVFADADLERAAAGAPGGAFDNAGQDCCARSRVLVQRSVFDRFLELLEPAVTGIAVGDPS
DPATAMGPLISAAQRDRVASYVPEDAPVAFRGSAPEGPGFWFPPTVLTPTDPNARVLREE
VFGPVMCVVPFEDEAEAVALANDTEYGLAGSVWTRDVGRALRVARGVRAGNLSVNSHSAV
RYWTPFGGMGHSGIGRELGPDALEAFTETKTVFVSDDT
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