SitesBLAST
Comparing WP_068173812.1 NCBI__GCF_001592305.1:WP_068173812.1 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)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
39% identity, 97% coverage: 12:478/483 of query aligns to 29:500/515 of 2d4eC
- active site: N173 (= N155), K196 (= K178), E271 (= E253), C305 (= C287), E409 (= E385), E486 (= E464)
- binding nicotinamide-adenine-dinucleotide: I169 (= I151), T170 (≠ A152), P171 (= P153), W172 (= W154), K196 (= K178), A198 (= A180), G229 (= G211), G233 (= G215), A234 (≠ Q216), T248 (= T230), G249 (= G231), E250 (≠ S232), T253 (= T235), E271 (= E253), L272 (≠ M254), C305 (= C287), E409 (= E385), F411 (= F387), F475 (= F452)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
37% identity, 98% coverage: 8:478/483 of query aligns to 4:477/489 of 4cazA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E385), E463 (= E464)
- 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: I148 (= I151), G149 (≠ A152), W151 (= W154), N152 (= N155), K175 (= K178), E178 (= E181), G208 (= G211), G212 (= G215), F226 (= F229), T227 (= T230), G228 (= G231), G229 (≠ S232), T232 (= T235), V236 (≠ I239), E251 (= E253), L252 (≠ M254), C285 (= C287), E386 (= E385), F388 (= F387)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
37% identity, 98% coverage: 8:478/483 of query aligns to 4:477/489 of 2woxA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E385), E463 (= E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I151), G149 (≠ A152), W151 (= W154), N152 (= N155), K175 (= K178), S177 (≠ A180), E178 (= E181), G208 (= G211), G212 (= G215), F226 (= F229), T227 (= T230), G228 (= G231), G229 (≠ S232), T232 (= T235), V236 (≠ I239), E251 (= E253), L252 (≠ M254), C285 (= C287), E386 (= E385), F388 (= F387)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
37% identity, 98% coverage: 8:478/483 of query aligns to 4:477/489 of 2wmeA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E385), E463 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ A152), W151 (= W154), K175 (= K178), S177 (≠ A180), E178 (= E181), G208 (= G211), G212 (= G215), F226 (= F229), G228 (= G231), G229 (≠ S232), T232 (= T235), V236 (≠ I239)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
37% identity, 98% coverage: 8:478/483 of query aligns to 5:478/490 of Q9HTJ1
- GAWN 150:153 (≠ APWN 152:155) binding NADPH
- K162 (= K164) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 178:181) binding NADPH
- G209 (= G211) binding NADPH
- GTST 230:233 (≠ SVST 232:235) binding NADPH
- E252 (= E253) active site, Proton acceptor
- C286 (= C287) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E385) binding NADPH
- E464 (= E464) active site, Charge relay system
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, 96% coverage: 13:477/483 of query aligns to 11:480/497 of P17202
- I28 (≠ T28) binding K(+)
- D96 (≠ E95) binding K(+)
- SPW 156:158 (≠ APW 152:154) binding NAD(+)
- Y160 (≠ F156) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 178:181) binding NAD(+)
- L186 (= L182) binding K(+)
- SSAT 236:239 (≠ SVST 232:235) binding NAD(+)
- V251 (≠ R247) binding in other chain
- L258 (≠ M254) binding NAD(+)
- W285 (≠ F281) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding NAD(+)
- A441 (≠ M436) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V446) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F452) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K456) binding K(+)
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)
37% identity, 100% coverage: 1:481/483 of query aligns to 1:478/482 of P25526
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 97% coverage: 13:481/483 of query aligns to 7:477/489 of 4o6rA
- active site: N150 (= N155), K173 (= K178), E248 (= E253), C282 (= C287), E383 (= E385), E460 (= E464)
- binding adenosine monophosphate: I146 (= I151), V147 (≠ A152), K173 (= K178), G206 (= G211), G210 (= G215), Q211 (= Q216), F224 (= F229), G226 (= G231), S227 (= S232), T230 (= T235), R233 (= R238)
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
36% identity, 92% coverage: 33:478/483 of query aligns to 35:481/493 of 6vr6D
- active site: N156 (= N155), E253 (= E253), C287 (= C287), E467 (= E464)
- binding nicotinamide-adenine-dinucleotide: I152 (= I151), G153 (≠ A152), W155 (= W154), K179 (= K178), A212 (≠ R212), G215 (= G215), Q216 (= Q216), F229 (= F229), G231 (= G231), S232 (= S232), T235 (= T235), I239 (= I239)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
36% identity, 92% coverage: 33:478/483 of query aligns to 36:482/494 of P49189
- C116 (≠ I113) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
37% identity, 97% coverage: 13:481/483 of query aligns to 13:477/481 of 3jz4A
- active site: N156 (= N155), K179 (= K178), E254 (= E253), C288 (= C287), E385 (= E385), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P153), W155 (= W154), K179 (= K178), A181 (= A180), S182 (≠ E181), A212 (≠ G211), G216 (= G215), G232 (= G231), S233 (= S232), I236 (≠ T235), C288 (= C287), K338 (≠ Q337), E385 (= E385), F387 (= F387)
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)
34% identity, 97% coverage: 12:478/483 of query aligns to 12:482/487 of Q9H2A2
- R109 (= R109) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N155) mutation to A: Complete loss of activity.
- R451 (≠ G445) mutation to A: Complete loss of activity.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 96% coverage: 13:477/483 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N155), K180 (= K178), E255 (= E253), A289 (≠ C287), E388 (= E385), E465 (= E464)
- binding 3-aminopropan-1-ol: C448 (≠ V446), W454 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I151), S154 (≠ A152), P155 (= P153), W156 (= W154), N157 (= N155), M162 (≠ I160), K180 (= K178), S182 (≠ A180), E183 (= E181), G213 (= G211), G217 (= G215), A218 (≠ Q216), T232 (= T230), G233 (= G231), S234 (= S232), T237 (= T235), E255 (= E253), L256 (≠ M254), A289 (≠ C287), E388 (= E385), F390 (= F387)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 97% coverage: 11:478/483 of query aligns to 12:483/494 of 4pz2B
- active site: N159 (= N155), K182 (= K178), E258 (= E253), C292 (= C287), E392 (= E385), D469 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I155 (= I151), I156 (≠ A152), P157 (= P153), W158 (= W154), N159 (= N155), M164 (≠ I160), K182 (= K178), A184 (= A180), E185 (= E181), G215 (= G211), G219 (= G215), F233 (= F229), T234 (= T230), G235 (= G231), S236 (= S232), V239 (≠ T235), E258 (= E253), L259 (≠ M254), C292 (= C287), E392 (= E385), F394 (= F387)
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)
34% identity, 97% coverage: 11:477/483 of query aligns to 19:489/505 of 4neaA
- active site: N166 (= N155), K189 (= K178), E264 (= E253), C298 (= C287), E399 (= E385), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P153), K189 (= K178), E192 (= E181), G222 (= G211), G226 (= G215), G242 (= G231), G243 (≠ S232), T246 (= T235), H249 (≠ R238), I250 (= I239), C298 (= C287), E399 (= E385), F401 (= F387)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
38% identity, 96% coverage: 13:478/483 of query aligns to 35:502/512 of P47895
- R89 (= R69) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K178) binding NAD(+)
- E207 (= E181) binding NAD(+)
- GSTEVG 257:262 (≠ GSVSTG 231:236) binding NAD(+)
- Q361 (= Q334) binding NAD(+)
- E411 (= E385) binding NAD(+)
- A493 (= A469) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
37% identity, 97% coverage: 11:478/483 of query aligns to 15:484/489 of 7a6qB
- active site: N163 (= N155), E262 (= E253), C296 (= C287), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I151), W162 (= W154), K186 (= K178), E189 (= E181), G219 (= G211), G223 (= G215), S240 (= S232), V243 (≠ T235), K342 (≠ A333)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ V26), T33 (≠ S27), C34 (≠ T28), P36 (= P30), D103 (≠ E95), E189 (= E181), Q190 (≠ L182), F218 (≠ S210), I339 (≠ V330), D340 (= D331)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ R109), D141 (≠ R133), N143 (≠ G135), N451 (≠ T443), L453 (≠ V446), A455 (≠ F448)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
37% identity, 97% coverage: 11:478/483 of query aligns to 15:484/489 of 7a6qA
- active site: N163 (= N155), E262 (= E253), C296 (= C287), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I151), T160 (≠ A152), W162 (= W154), K186 (= K178), A188 (= A180), E189 (= E181), G219 (= G211), G223 (= G215), S240 (= S232), V243 (≠ T235), K342 (≠ A333), K346 (≠ Q337)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ R109), D141 (≠ R133), N143 (≠ G135), N451 (≠ T443), L453 (≠ V446), Y454 (≠ D447)
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)
36% identity, 92% coverage: 29:474/483 of query aligns to 33:493/511 of 6fkuA
- active site: N159 (= N155), E261 (= E253), C295 (= C287), E483 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I151), T156 (≠ A152), N159 (= N155), K182 (= K178), S184 (≠ A180), E185 (= E181), G214 (≠ S210), G215 (= G211), K216 (≠ R212), G220 (= G215), Q221 (= Q216), F237 (= F229), T238 (= T230), G239 (= G231), S240 (= S232), V243 (≠ T235), E261 (= E253), L262 (≠ M254), C295 (= C287), R342 (≠ A333), F343 (≠ Q334), E404 (= E385), F406 (= F387)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
37% identity, 97% coverage: 11:478/483 of query aligns to 15:484/489 of 5fhzA
- active site: N163 (= N155), K186 (= K178), E262 (= E253), C296 (= C287), E393 (= E385), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I151), T160 (≠ A152), W162 (= W154), K186 (= K178), E189 (= E181), G219 (= G211), G223 (= G215), F237 (= F229), G239 (= G231), S240 (= S232), T241 (≠ V233), V243 (≠ T235), G264 (= G255), Q343 (= Q334), E393 (= E385)
- binding retinoic acid: G118 (≠ R109), R121 (≠ Q112), F164 (= F156), M168 (≠ I160), W171 (= W163), C295 (≠ R286), C296 (= C287), L453 (≠ V446)
Query Sequence
>WP_068173812.1 NCBI__GCF_001592305.1:WP_068173812.1
MKLGDMQQNPRHFINGRWEIGTTTGVSTNPSDTREVVAEYARADRNQTELAIRAAADALP
HWSQSSPQRRADVLDQIGSELLARKDELGALLAREEGKTLPEGVGEVARAGQIFKFFAGE
ALRIPGEVIASVRPGVRVDVTREPVGVVGIIAPWNFPFAIPAWKIAPALAYGNTVVFKPA
ELVPACGWALAEIISRCGLPAGVFNLVMGSGREVGQTLVDHPLVNALSFTGSVSTGERIL
KAATARRAKVQLEMGGKNPLVVLADADLDQAVDCALQGSYFSTGQRCTASSRLIVQAQVH
DAFVAKLRQRLSTLKVGHALERGTEMGPVVDRAQLEQNLAYIEIARNEGAEHVWGGDLLQ
RPTPGHYMSPALFLAKPEHRVAREEIFGPVACVLRADDYEHALVLANDTPFGLCAGICTT
SLKYAMHFKRHAEVGMTMVNLPTAGVDFHVPFGGRKESSHGSREQGRYAVEFYTTVKTGY
MLA
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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