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Comparing WP_011383248.1 AMB_RS04115 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase 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
46% identity, 99% coverage: 4:484/485 of query aligns to 29:514/515 of 2d4eC
- active site: N173 (= N145), K196 (= K168), E271 (= E241), C305 (= C275), E409 (= E379), E486 (= E456)
- binding nicotinamide-adenine-dinucleotide: I169 (= I141), T170 (≠ S142), P171 (= P143), W172 (= W144), K196 (= K168), A198 (≠ S170), G229 (= G201), G233 (= G205), A234 (≠ E206), T248 (= T220), G249 (= G221), E250 (≠ S222), T253 (= T225), E271 (= E241), L272 (= L242), C305 (= C275), E409 (= E379), F411 (= F381), F475 (= F445)
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)
42% identity, 98% coverage: 1:473/485 of query aligns to 9:485/487 of Q9H2A2
- R109 (= R101) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N145) mutation to A: Complete loss of activity.
- R451 (= R439) mutation to A: Complete loss of activity.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
42% identity, 97% coverage: 5:474/485 of query aligns to 7:478/489 of 4o6rA
- active site: N150 (= N145), K173 (= K168), E248 (= E241), C282 (= C275), E383 (= E379), E460 (= E456)
- binding adenosine monophosphate: I146 (= I141), V147 (≠ S142), K173 (= K168), G206 (= G201), G210 (= G205), Q211 (≠ E206), F224 (= F219), G226 (= G221), S227 (= S222), T230 (= T225), R233 (= R228)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
41% identity, 95% coverage: 12:471/485 of query aligns to 30:494/498 of 4go2A
- active site: N170 (= N145), K193 (= K168), E269 (= E241), C303 (= C275), E400 (= E379), D479 (≠ E456)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I141), I167 (≠ S142), P168 (= P143), W169 (= W144), K193 (= K168), A195 (≠ S170), Q196 (≠ E171), S225 (≠ Y200), G226 (= G201), G230 (= G205), Q231 (≠ E206), F244 (= F219), G246 (= G221), S247 (= S222), V250 (≠ T225), I254 (= I229), E269 (= E241), G271 (= G243), C303 (= C275), E400 (= E379), F402 (= F381)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
41% identity, 95% coverage: 12:471/485 of query aligns to 30:494/498 of 2o2rA
- active site: N170 (= N145), K193 (= K168), E269 (= E241), C303 (= C275), E400 (= E379), D479 (≠ E456)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I141), I167 (≠ S142), W169 (= W144), K193 (= K168), A195 (≠ S170), Q196 (≠ E171), S225 (≠ Y200), G226 (= G201), G230 (= G205), Q231 (≠ E206), F244 (= F219), S247 (= S222), V250 (≠ T225), I254 (= I229)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
41% identity, 95% coverage: 12:471/485 of query aligns to 115:579/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K168), S310 (≠ Y200), G311 (= G201), G315 (= G205), G331 (= G221), S332 (= S222), V335 (≠ T225)
- binding 4'-phosphopantetheine: K201 (= K96), F382 (≠ G269), N387 (≠ S274), C388 (= C275), N545 (= N437)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
41% identity, 95% coverage: 12:471/485 of query aligns to 434:898/902 of P28037
- IPW 571:573 (≠ SPW 142:144) binding
- KPAQ 597:600 (≠ KMSE 168:171) binding
- GSLVGQ 630:635 (≠ GSAVGE 201:206) binding
- GS 650:651 (= GS 221:222) binding
- E673 (= E241) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 241:242) binding
- C707 (= C275) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K325) binding
- ESF 804:806 (≠ EIF 379:381) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
40% identity, 96% coverage: 6:473/485 of query aligns to 7:481/483 of 4npiA
- active site: N152 (= N145), K175 (= K168), E251 (= E241), C285 (= C275), E387 (= E379), E464 (= E456)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R101), L157 (≠ T150), W160 (= W153), E251 (= E241), C285 (= C275), Y445 (≠ N437), R447 (= R439), F453 (= F445)
- binding nicotinamide-adenine-dinucleotide: I148 (= I141), S149 (= S142), P150 (= P143), W151 (= W144), K175 (= K168), E178 (= E171), G208 (= G201), G213 (= G205), E214 (= E206), F227 (= F219), G229 (= G221), E230 (≠ S222), T233 (= T225), G253 (= G243), C285 (= C275), K335 (= K325), E387 (= E379), F389 (= F381)
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
40% identity, 96% coverage: 6:473/485 of query aligns to 7:481/483 of 4i2rA
- active site: N152 (= N145), K175 (= K168), E251 (= E241), C285 (= C275), E387 (= E379), E464 (= E456)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R101), L157 (≠ T150), C285 (= C275), Y445 (≠ N437), R447 (= R439), F453 (= F445)
- binding nicotinamide-adenine-dinucleotide: I148 (= I141), S149 (= S142), W151 (= W144), N152 (= N145), K175 (= K168), E178 (= E171), G208 (= G201), F227 (= F219), T228 (= T220), G229 (= G221), E230 (≠ S222), T233 (= T225), E251 (= E241), L252 (= L242), G253 (= G243), C285 (= C275), E387 (= E379), F389 (= F381)
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
40% identity, 96% coverage: 6:473/485 of query aligns to 7:481/483 of 4i25A
- active site: N152 (= N145), K175 (= K168), E251 (= E241), C285 (= C275), E387 (= E379), E464 (= E456)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R101), L157 (≠ T150), C285 (= C275), Y445 (≠ N437), R447 (= R439), F453 (= F445)
- binding nicotinamide-adenine-dinucleotide: I148 (= I141), S149 (= S142), P150 (= P143), W151 (= W144), N152 (= N145), K175 (= K168), E178 (= E171), G208 (= G201), G213 (= G205), F227 (= F219), T228 (= T220), G229 (= G221), E230 (≠ S222), T233 (= T225), E251 (= E241), L252 (= L242), C285 (= C275), E387 (= E379), F389 (= F381)
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
40% identity, 96% coverage: 6:473/485 of query aligns to 7:481/483 of 5kllA
- active site: D152 (≠ N145), K175 (= K168), E251 (= E241), C285 (= C275), E387 (= E379), E464 (= E456)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R101), D152 (≠ N145), L157 (≠ T150), W160 (= W153), C285 (= C275), Y445 (≠ N437), R447 (= R439), F453 (= F445)
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
40% identity, 96% coverage: 6:473/485 of query aligns to 8:482/484 of 5kj5B
- active site: D153 (≠ N145), K176 (= K168), E252 (= E241), C286 (= C275), E388 (= E379), E465 (= E456)
- binding nicotinamide-adenine-dinucleotide: I149 (= I141), S150 (= S142), P151 (= P143), W152 (= W144), D153 (≠ N145), L158 (≠ T150), K176 (= K168), G209 (= G201), K210 (vs. gap), G214 (= G205), F228 (= F219), T229 (= T220), G230 (= G221), E231 (≠ S222), T234 (= T225), E252 (= E241), L253 (= L242), C286 (= C275), E388 (= E379), F390 (= F381), F454 (= F445)
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
40% identity, 96% coverage: 6:473/485 of query aligns to 7:481/483 of 4ou2A
- active site: N152 (= N145), K175 (= K168), A251 (≠ E241), C285 (= C275), E387 (= E379), E464 (= E456)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R101), L157 (≠ T150), C285 (= C275), Y445 (≠ N437), R447 (= R439), F453 (= F445)
- binding nicotinamide-adenine-dinucleotide: I148 (= I141), S149 (= S142), P150 (= P143), W151 (= W144), N152 (= N145), K175 (= K168), G208 (= G201), G213 (= G205), E214 (= E206), F227 (= F219), T228 (= T220), G229 (= G221), E230 (≠ S222), T233 (= T225), A251 (≠ E241), L252 (= L242), G253 (= G243), C285 (= C275), E387 (= E379), F389 (= F381)
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)
40% identity, 98% coverage: 3:478/485 of query aligns to 8:486/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 142:145) binding
- K162 (= K154) active site, Charge relay system
- KPSE 176:179 (≠ KMSE 168:171) binding
- G209 (= G201) binding
- GTST 230:233 (≠ STAT 222:225) binding
- E252 (= E241) active site, Proton acceptor
- C286 (= C275) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E379) binding
- E464 (= E456) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
40% identity, 98% coverage: 3:478/485 of query aligns to 7:485/489 of 4cazA
- active site: N152 (= N145), K175 (= K168), E251 (= E241), C285 (= C275), E386 (= E379), E463 (= E456)
- 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 (= I141), G149 (≠ S142), W151 (= W144), N152 (= N145), K175 (= K168), E178 (= E171), G208 (= G201), G212 (= G205), F226 (= F219), T227 (= T220), G228 (= G221), G229 (≠ S222), T232 (= T225), V236 (≠ I229), E251 (= E241), L252 (= L242), C285 (= C275), E386 (= E379), F388 (= F381)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
40% identity, 98% coverage: 3:478/485 of query aligns to 7:485/489 of 2woxA
- active site: N152 (= N145), K175 (= K168), E251 (= E241), C285 (= C275), E386 (= E379), E463 (= E456)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I141), G149 (≠ S142), W151 (= W144), N152 (= N145), K175 (= K168), S177 (= S170), E178 (= E171), G208 (= G201), G212 (= G205), F226 (= F219), T227 (= T220), G228 (= G221), G229 (≠ S222), T232 (= T225), V236 (≠ I229), E251 (= E241), L252 (= L242), C285 (= C275), E386 (= E379), F388 (= F381)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
40% identity, 98% coverage: 3:478/485 of query aligns to 7:485/489 of 2wmeA
- active site: N152 (= N145), K175 (= K168), E251 (= E241), C285 (= C275), E386 (= E379), E463 (= E456)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S142), W151 (= W144), K175 (= K168), S177 (= S170), E178 (= E171), G208 (= G201), G212 (= G205), F226 (= F219), G228 (= G221), G229 (≠ S222), T232 (= T225), V236 (≠ I229)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
43% identity, 95% coverage: 12:471/485 of query aligns to 30:494/498 of 7yjjC
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
41% identity, 99% coverage: 6:483/485 of query aligns to 7:485/487 of 4go4A
- active site: N149 (= N145), K172 (= K168), E247 (= E241), C281 (= C275), E381 (= E379), E458 (= E456)
- binding nicotinamide-adenine-dinucleotide: I145 (= I141), V146 (≠ S142), W148 (= W144), N149 (= N145), F154 (≠ T150), K172 (= K168), G205 (= G201), G209 (= G205), Q210 (≠ E206), F223 (= F219), T224 (= T220), G225 (= G221), S226 (= S222), T229 (= T225), E247 (= E241), G249 (= G243), C281 (= C275), E381 (= E379), F383 (= F381)
O75891 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; EC 1.5.1.6 from Homo sapiens (Human) (see 2 papers)
43% identity, 95% coverage: 12:471/485 of query aligns to 434:898/902 of O75891
- A511 (≠ T87) to V: in a colorectal cancer sample; somatic mutation; dbSNP:rs768309358
Sites not aligning to the query:
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation by AASDHPPT. Loss of formyltetrahydrofolate dehydrogenase activity.
Query Sequence
>WP_011383248.1 AMB_RS04115 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase
MIKHLINGRQVESASTIANLNPANNEVICQIAAGGEAEVAQAVAAAKEAFPKWAGLPASQ
RAKLLRKVGDLINQHVDEIAKLESLDTGQSYWRTKKMLVPRAADNFYFFADTCCHVDGET
YPTNDHLNYTLYQPVGVVGLISPWNVPFMTATWKTAPCLAFGNTAVLKMSELSPLSADRL
GQLILEAGIPAGVFNIVHGYGSAVGEALVKHPDVRGVSFTGSTATGNRIIQSGGLKKYSM
ELGGKSPNIIFDDCDFERAVDAAIVAVYGNNGESCTNGTRILVQDGLYDRFVAALAERTR
KVVVGDPLDEATNVGPMITRDHWKKVTSYIELGISEGARVVAGGLGTPEGLAPHLKNGNF
VRPTVLADVDNSWRVAQEEIFGPVACVIRFKDEAEALKIANATSYGLASYVWTENGARAI
RMAEGIEAGLVFVNSQNVRDLRQPFGGIKGSGTGREGGHYSYEAFLEVKNVCVSKGSHHI
PRWGV
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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