SitesBLAST
Comparing WP_003292094.1 NCBI__GCF_900100495.1:WP_003292094.1 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)
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
63% identity, 100% coverage: 2:486/486 of query aligns to 1:483/483 of 4npiA
- active site: N152 (= N155), K175 (= K178), E251 (= E254), C285 (= C288), E387 (= E390), E464 (= E467)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (= L160), W160 (= W163), E251 (= E254), C285 (= C288), Y445 (≠ F448), R447 (= R450), F453 (= F456)
- binding nicotinamide-adenine-dinucleotide: I148 (= I151), S149 (= S152), P150 (= P153), W151 (= W154), K175 (= K178), E178 (= E181), G208 (= G211), G213 (= G216), E214 (≠ A217), F227 (= F230), G229 (= G232), E230 (= E233), T233 (= T236), G253 (= G256), C285 (= C288), K335 (= K338), E387 (= E390), F389 (= F392)
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
63% identity, 100% coverage: 2:486/486 of query aligns to 1:483/483 of 4i2rA
- active site: N152 (= N155), K175 (= K178), E251 (= E254), C285 (= C288), E387 (= E390), E464 (= E467)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (= L160), C285 (= C288), Y445 (≠ F448), R447 (= R450), F453 (= F456)
- binding nicotinamide-adenine-dinucleotide: I148 (= I151), S149 (= S152), W151 (= W154), N152 (= N155), K175 (= K178), E178 (= E181), G208 (= G211), F227 (= F230), T228 (= T231), G229 (= G232), E230 (= E233), T233 (= T236), E251 (= E254), L252 (= L255), G253 (= G256), C285 (= C288), E387 (= E390), F389 (= F392)
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
63% identity, 100% coverage: 2:486/486 of query aligns to 1:483/483 of 4i25A
- active site: N152 (= N155), K175 (= K178), E251 (= E254), C285 (= C288), E387 (= E390), E464 (= E467)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (= L160), C285 (= C288), Y445 (≠ F448), R447 (= R450), F453 (= F456)
- binding nicotinamide-adenine-dinucleotide: I148 (= I151), S149 (= S152), P150 (= P153), W151 (= W154), N152 (= N155), K175 (= K178), E178 (= E181), G208 (= G211), G213 (= G216), F227 (= F230), T228 (= T231), G229 (= G232), E230 (= E233), T233 (= T236), E251 (= E254), L252 (= L255), C285 (= C288), E387 (= E390), F389 (= F392)
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
63% identity, 100% coverage: 2:486/486 of query aligns to 1:483/483 of 5kllA
- active site: D152 (≠ N155), K175 (= K178), E251 (= E254), C285 (= C288), E387 (= E390), E464 (= E467)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R106), D152 (≠ N155), L157 (= L160), W160 (= W163), C285 (= C288), Y445 (≠ F448), R447 (= R450), F453 (= F456)
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
63% identity, 100% coverage: 2:486/486 of query aligns to 2:484/484 of 5kj5B
- active site: D153 (≠ N155), K176 (= K178), E252 (= E254), C286 (= C288), E388 (= E390), E465 (= E467)
- binding nicotinamide-adenine-dinucleotide: I149 (= I151), S150 (= S152), P151 (= P153), W152 (= W154), D153 (≠ N155), L158 (= L160), K176 (= K178), G209 (= G211), K210 (≠ G212), G214 (= G216), F228 (= F230), T229 (= T231), G230 (= G232), E231 (= E233), T234 (= T236), E252 (= E254), L253 (= L255), C286 (= C288), E388 (= E390), F390 (= F392), F454 (= F456)
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
63% identity, 100% coverage: 2:486/486 of query aligns to 1:483/483 of 4ou2A
- active site: N152 (= N155), K175 (= K178), A251 (≠ E254), C285 (= C288), E387 (= E390), E464 (= E467)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R106), L157 (= L160), C285 (= C288), Y445 (≠ F448), R447 (= R450), F453 (= F456)
- binding nicotinamide-adenine-dinucleotide: I148 (= I151), S149 (= S152), P150 (= P153), W151 (= W154), N152 (= N155), K175 (= K178), G208 (= G211), G213 (= G216), E214 (≠ A217), F227 (= F230), T228 (= T231), G229 (= G232), E230 (= E233), T233 (= T236), A251 (≠ E254), L252 (= L255), G253 (= G256), C285 (= C288), E387 (= E390), F389 (= F392)
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
60% identity, 99% coverage: 4:486/486 of query aligns to 4:484/485 of 4u3wA
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)
44% identity, 99% coverage: 4:485/486 of query aligns to 10:486/487 of Q9H2A2
- R109 (= R106) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N155) mutation to A: Complete loss of activity.
- R451 (= R450) mutation to A: Complete loss of activity.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
43% identity, 100% coverage: 2:486/486 of query aligns to 15:490/491 of 5gtlA
- active site: N165 (= N155), K188 (= K178), E263 (= E254), C297 (= C288), E394 (= E390), E471 (= E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I151), P163 (= P153), K188 (= K178), A190 (≠ S180), E191 (= E181), Q192 (≠ E182), G221 (= G211), G225 (= G216), G241 (= G232), S242 (≠ E233), T245 (= T236), L264 (= L255), C297 (= C288), E394 (= E390), F396 (= F392)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
43% identity, 100% coverage: 2:486/486 of query aligns to 15:490/491 of 5gtkA
- active site: N165 (= N155), K188 (= K178), E263 (= E254), C297 (= C288), E394 (= E390), E471 (= E467)
- binding nicotinamide-adenine-dinucleotide: I161 (= I151), I162 (≠ S152), P163 (= P153), W164 (= W154), K188 (= K178), E191 (= E181), G221 (= G211), G225 (= G216), A226 (= A217), F239 (= F230), G241 (= G232), S242 (≠ E233), T245 (= T236), Y248 (≠ T239), L264 (= L255), C297 (= C288), Q344 (≠ H335), R347 (≠ K338), E394 (= E390), F396 (= F392)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
43% identity, 100% coverage: 3:486/486 of query aligns to 3:479/489 of 4o6rA
- active site: N150 (= N155), K173 (= K178), E248 (= E254), C282 (= C288), E383 (= E390), E460 (= E467)
- binding adenosine monophosphate: I146 (= I151), V147 (≠ S152), K173 (= K178), G206 (= G211), G210 (= G216), Q211 (≠ A217), F224 (= F230), G226 (= G232), S227 (≠ E233), T230 (= T236), R233 (≠ T239)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
42% identity, 99% coverage: 6:486/486 of query aligns to 29:505/515 of 2d4eC
- active site: N173 (= N155), K196 (= K178), E271 (= E254), C305 (= C288), E409 (= E390), E486 (= E467)
- binding nicotinamide-adenine-dinucleotide: I169 (= I151), T170 (≠ S152), P171 (= P153), W172 (= W154), K196 (= K178), A198 (≠ S180), G229 (= G211), G233 (= G216), A234 (= A217), T248 (= T231), G249 (= G232), E250 (= E233), T253 (= T236), E271 (= E254), L272 (= L255), C305 (= C288), E409 (= E390), F411 (= F392), F475 (= F456)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
41% identity, 100% coverage: 1:486/486 of query aligns to 3:482/489 of 4cazA
- active site: N152 (= N155), K175 (= K178), E251 (= E254), C285 (= C288), E386 (= E390), E463 (= E467)
- 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 (≠ S152), W151 (= W154), N152 (= N155), K175 (= K178), E178 (= E181), G208 (= G212), G212 (= G216), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ E233), T232 (= T236), V236 (≠ I240), E251 (= E254), L252 (= L255), C285 (= C288), E386 (= E390), F388 (= F392)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
41% identity, 100% coverage: 1:486/486 of query aligns to 3:482/489 of 2woxA
- active site: N152 (= N155), K175 (= K178), E251 (= E254), C285 (= C288), E386 (= E390), E463 (= E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I151), G149 (≠ S152), W151 (= W154), N152 (= N155), K175 (= K178), S177 (= S180), E178 (= E181), G208 (= G212), G212 (= G216), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ E233), T232 (= T236), V236 (≠ I240), E251 (= E254), L252 (= L255), C285 (= C288), E386 (= E390), F388 (= F392)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
41% identity, 100% coverage: 1:486/486 of query aligns to 3:482/489 of 2wmeA
- active site: N152 (= N155), K175 (= K178), E251 (= E254), C285 (= C288), E386 (= E390), E463 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S152), W151 (= W154), K175 (= K178), S177 (= S180), E178 (= E181), G208 (= G212), G212 (= G216), F226 (= F230), G228 (= G232), G229 (≠ E233), T232 (= T236), V236 (≠ I240)
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)
41% identity, 100% coverage: 1:486/486 of query aligns to 4:483/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 152:155) binding NADPH
- K162 (= K164) active site, Charge relay system
- KPSE 176:179 (= KPSE 178:181) binding NADPH
- G209 (= G212) binding NADPH
- GTST 230:233 (≠ ETGT 233:236) binding NADPH
- E252 (= E254) active site, Proton acceptor
- C286 (= C288) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E390) binding NADPH
- E464 (= E467) active site, Charge relay system
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)
40% identity, 100% coverage: 1:486/486 of query aligns to 17:495/501 of Q56YU0
- G152 (= G135) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A407) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
41% identity, 100% coverage: 1:486/486 of query aligns to 11:490/497 of 8skfA
- binding calcium ion: T33 (≠ D23), I34 (= I24), D100 (= D91), V187 (≠ E182)
- binding nicotinamide-adenine-dinucleotide: I156 (= I151), G157 (≠ S152), A158 (≠ P153), W159 (= W154), K183 (= K178), E186 (= E181), G216 (= G211), G220 (= G216), T235 (= T231), G236 (= G232), G237 (≠ E233), S240 (≠ T236), K243 (≠ T239), E259 (= E254), C293 (= C288), F396 (= F392)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
41% identity, 100% coverage: 1:486/486 of query aligns to 2:481/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
41% identity, 100% coverage: 1:486/486 of query aligns to 2:481/488 of 8vr0A
Query Sequence
>WP_003292094.1 NCBI__GCF_900100495.1:WP_003292094.1
MKEIKHFINGAFVDSASGRTFEDINPVNGQVIGRVHEAGRAEVDAAVRAARAALKGPWGK
MTVAERAEILHRVADGVTARFDEFLEAECLDTGKPKSLASHIDIPRGAANFKVFADLIKN
VPTEAFEMATPDGAGALNYGVRRPKGVIGVISPWNLPLLLMTWKVGPALACGNCVVVKPS
EETPLTATLLGEVMQAAGVPAGVYNVVHGFGGDSAGAFLTEHPDVDAYTFTGETGTGETI
MRAAAKGVRQVSLELGGKNAGIVFADCDLDKAIEGTLRSAFANCGQVCLGTERVYVERPI
FDAFVARLKAGAEALKIGEPNDPEANFGPLISHKHREKVLSYYQQAVDDGATVVTGGGVP
EMPAHLAGGAWVQPTIWTGLTDDSAVVTEEIFGPCCHIRPFDSEEEAIELANSLPYGLAS
AIWTENASRAHRVAGQIEAGIVWVNSWFLRDLRTAFGGSKQSGIGREGGVHSLEFYTELK
NICVKL
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