SitesBLAST
Comparing WP_025274242.1 NCBI__GCF_000527155.1:WP_025274242.1 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)
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)
55% identity, 98% coverage: 5:487/492 of query aligns to 21:503/505 of 4neaA
- active site: N166 (= N150), K189 (= K173), E264 (= E248), C298 (= C282), E399 (= E383), E476 (= E460)
- binding nicotinamide-adenine-dinucleotide: P164 (= P148), K189 (= K173), E192 (= E176), G222 (= G206), G226 (= G210), G242 (= G226), G243 (= G227), T246 (= T230), H249 (≠ R233), I250 (= I234), C298 (= C282), E399 (= E383), F401 (= F385)
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)
42% identity, 99% coverage: 3:488/492 of query aligns to 9:495/497 of P17202
- I28 (≠ L22) binding K(+)
- D96 (= D90) binding K(+)
- SPW 156:158 (≠ APW 147:149) binding NAD(+)
- Y160 (= Y151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 173:176) binding NAD(+)
- L186 (≠ V177) binding K(+)
- SSAT 236:239 (≠ GLHT 227:230) binding NAD(+)
- V251 (= V242) binding in other chain
- L258 (= L249) binding NAD(+)
- W285 (≠ F276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E383) binding NAD(+)
- A441 (≠ T434) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ Y443) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (= W449) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G453) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
42% identity, 99% coverage: 3:488/492 of query aligns to 7:493/495 of 4v37A
- active site: N157 (= N150), K180 (= K173), E255 (= E248), A289 (≠ C282), E388 (= E383), E465 (= E460)
- binding 3-aminopropan-1-ol: C448 (≠ Y443), W454 (= W449)
- binding nicotinamide-adenine-dinucleotide: I153 (= I146), S154 (≠ A147), P155 (= P148), W156 (= W149), N157 (= N150), M162 (≠ Q155), K180 (= K173), S182 (= S175), E183 (= E176), G213 (= G206), G217 (= G210), A218 (= A211), T232 (= T225), G233 (= G226), S234 (≠ G227), T237 (= T230), E255 (= E248), L256 (= L249), A289 (≠ C282), E388 (= E383), F390 (= F385)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
44% identity, 99% coverage: 4:488/492 of query aligns to 12:500/505 of O24174
- N164 (= N150) 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 (= W158) 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.
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
44% identity, 99% coverage: 3:488/492 of query aligns to 6:495/500 of 3iwjA
- active site: N159 (= N150), K182 (= K173), E257 (= E248), C291 (= C282), E390 (= E383), E467 (= E460)
- binding glycerol: D110 (= D104), Y160 (= Y151), W167 (= W158), I290 (≠ V281), C291 (= C282), C450 (≠ Y443), W456 (= W449)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), T156 (≠ A147), W158 (= W149), K182 (= K173), S184 (= S175), E185 (= E176), G215 (= G206), A220 (= A211), F233 (= F224), G235 (= G226), S236 (≠ G227), T239 (= T230), I243 (= I234)
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)
44% identity, 99% coverage: 3:488/492 of query aligns to 9:498/503 of Q93YB2
- I28 (≠ L22) binding Na(+)
- D99 (= D90) binding Na(+)
- W161 (= W149) binding NAD(+)
- K185 (= K173) binding NAD(+)
- L189 (≠ V177) binding Na(+)
- S239 (≠ G227) binding NAD(+)
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
45% identity, 99% coverage: 3:488/492 of query aligns to 9:498/503 of Q84LK3
- N162 (= N150) 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 (= W158) 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).
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
42% identity, 97% coverage: 4:479/492 of query aligns to 19:490/491 of 5gtlA
- active site: N165 (= N150), K188 (= K173), E263 (= E248), C297 (= C282), E394 (= E383), E471 (= E460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I146), P163 (= P148), K188 (= K173), A190 (≠ S175), E191 (= E176), Q192 (≠ V177), G221 (= G206), G225 (= G210), G241 (= G226), S242 (≠ G227), T245 (= T230), L264 (= L249), C297 (= C282), E394 (= E383), F396 (= F385)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
42% identity, 97% coverage: 4:479/492 of query aligns to 19:490/491 of 5gtkA
- active site: N165 (= N150), K188 (= K173), E263 (= E248), C297 (= C282), E394 (= E383), E471 (= E460)
- binding nicotinamide-adenine-dinucleotide: I161 (= I146), I162 (≠ A147), P163 (= P148), W164 (= W149), K188 (= K173), E191 (= E176), G221 (= G206), G225 (= G210), A226 (= A211), F239 (= F224), G241 (= G226), S242 (≠ G227), T245 (= T230), Y248 (≠ R233), L264 (= L249), C297 (= C282), Q344 (≠ H329), R347 (≠ K332), E394 (= E383), F396 (= F385)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
44% identity, 99% coverage: 3:488/492 of query aligns to 4:493/497 of 3iwkH
- active site: N157 (= N150), K180 (= K173), E255 (= E248), C289 (= C282), E388 (= E383), E465 (= E460)
- binding nicotinamide-adenine-dinucleotide: W156 (= W149), G213 (= G206), G217 (= G210), A218 (= A211), G233 (= G226), S234 (≠ G227), T237 (= T230), K240 (≠ R233), C289 (= C282), Q336 (≠ H329), E388 (= E383), F390 (= F385)
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)
44% identity, 99% coverage: 3:488/492 of query aligns to 9:498/503 of Q8VWZ1
- N27 (≠ V21) binding Na(+)
- I28 (≠ L22) binding Na(+)
- D99 (= D90) binding Na(+)
- L189 (≠ V177) binding Na(+)
- 238:245 (vs. 226:233, 38% identical) binding NAD(+)
- C294 (= C282) binding NAD(+)
- E393 (= E383) binding NAD(+)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
43% identity, 97% coverage: 3:479/492 of query aligns to 5:479/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E248), C282 (= C282), E383 (= E383), E460 (= E460)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ A147), K173 (= K173), G206 (= G206), G210 (= G210), Q211 (≠ A211), F224 (= F224), G226 (= G226), S227 (≠ G227), T230 (= T230), R233 (= R233)
P51977 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Ovis aries (Sheep) (see 2 papers)
43% identity, 97% coverage: 4:480/492 of query aligns to 23:497/501 of P51977
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
44% identity, 99% coverage: 3:488/492 of query aligns to 6:495/500 of 4i8pA
- active site: N159 (= N150), K182 (= K173), E257 (= E248), C291 (= C282), E390 (= E383), E467 (= E460)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), T156 (≠ A147), P157 (= P148), W158 (= W149), N159 (= N150), M164 (≠ Q155), K182 (= K173), S184 (= S175), E185 (= E176), G215 (= G206), G219 (= G210), A220 (= A211), T234 (= T225), G235 (= G226), S236 (≠ G227), T239 (= T230), E257 (= E248), L258 (= L249), C291 (= C282), E390 (= E383), F392 (= F385), W456 (= W449)
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)
44% identity, 99% coverage: 3:488/492 of query aligns to 11:500/505 of C0P9J6
5ac0A Ovis aries aldehyde dehydrogenase 1a1 in complex with a duocarmycin analog (see paper)
43% identity, 97% coverage: 4:480/492 of query aligns to 16:490/494 of 5ac0A
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E383), E470 (= E460)
- binding 1-[(1S)-1-methyl-5-oxidanyl-1,2-dihydrobenzo[e]indol-3-yl]hexan-1-one: M114 (≠ T100), F164 (≠ Y151), W171 (= W158), Y290 (≠ F276), C295 (≠ V281), C296 (= C282)
- binding nicotinamide-adenine-dinucleotide: I159 (= I146), I160 (≠ A147), P161 (= P148), W162 (= W149), K186 (= K173), E189 (= E176), G219 (= G206), G223 (= G210), A224 (= A211), F237 (= F224), G239 (= G226), S240 (≠ G227), V243 (≠ T230), G264 (= G250), C296 (= C282), Q343 (≠ H329), K346 (= K332), E393 (= E383)
5abmA Sheep aldehyde dehydrogenase 1a1 (see paper)
43% identity, 97% coverage: 4:480/492 of query aligns to 16:490/494 of 5abmA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E383), E470 (= E460)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I159 (= I146), I160 (≠ A147), P161 (= P148), W162 (= W149), K186 (= K173), E189 (= E176), G219 (= G206), G223 (= G210), F237 (= F224), G239 (= G226), S240 (≠ G227), V243 (≠ T230), G264 (= G250), Q343 (≠ H329), K346 (= K332), E393 (= E383), F395 (= F385)
1bxsA Sheep liver class 1 aldehyde dehydrogenase with NAD bound (see paper)
43% identity, 97% coverage: 4:480/492 of query aligns to 16:490/494 of 1bxsA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E383), E470 (= E460)
- binding nicotinamide-adenine-dinucleotide: I159 (= I146), I160 (≠ A147), P161 (= P148), W162 (= W149), K186 (= K173), E189 (= E176), G219 (= G206), G223 (= G210), F237 (= F224), G239 (= G226), S240 (≠ G227), V243 (≠ T230), L263 (= L249), C296 (= C282), Q343 (≠ H329), K346 (= K332), E393 (= E383), F395 (= F385)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
41% identity, 97% coverage: 4:479/492 of query aligns to 25:497/503 of O14293
- S248 (≠ G227) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
P15437 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Equus caballus (Horse) (see paper)
43% identity, 97% coverage: 4:480/492 of query aligns to 23:497/501 of P15437
Sites not aligning to the query:
- 2 modified: N-acetylserine
Query Sequence
>WP_025274242.1 NCBI__GCF_000527155.1:WP_025274242.1
MPDLFINGKWVDAINDATRTVLDPANDQPLATVAEADSDDVNAAVKAAREAFDSGPWRQT
PASERGDCLRAVASELQNRKSELTRIESLDTGKTLLEAETDVDDITNVFRYYADMADKDS
GRVTDTGVPNTVSRIVYEPIGVCSLIAPWNYPLLQMSWKLAPALAAGNTCVIKPSEVTPL
ATIELVKIIEASGVPAGVVNLVLGGGATTGAPMTEHPDVDMVSFTGGLHTGKRIMAAAAA
DVKNIALELGGKNPNVVFADADFETAVDYALNASFFHSGQVCSAGARLIIEESIKDDFIS
AVADRARKVKLGRGQDEGVEVGPMVSREHREKVENYIQTAIDEGATLVCGGKRPDDPALT
DGYFLEPTIFDDCNRDMTIVREEVFGPVLSVETFTTEDEAIALANDTEYGLAGGVWTSDA
SKAQRVSSAMRHGTIWINDFHPYVPQAEWGGFGKSGVGRELGHHGLDEYRETKHIWQNIS
PEPMRWFEGKDD
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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