SitesBLAST
Comparing Pf1N1B4_3444 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3444 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)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
80% identity, 99% coverage: 1:485/488 of query aligns to 2:486/486 of 3ju8A
- active site: N147 (= N146), K170 (= K169), E245 (= E244), C279 (= C278), E377 (= E376), P455 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: G144 (= G143), Y146 (= Y145), N147 (= N146), L152 (= L151), K170 (= K169), S172 (= S171), F220 (= F219), T221 (= T220), G222 (= G221), S223 (= S222), T226 (= T225), E245 (= E244), M246 (= M245), G247 (= G246), C279 (= C278), E377 (= E376), F379 (= F378), F444 (= F443)
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
61% identity, 99% coverage: 3:487/488 of query aligns to 5:488/488 of 5u0mA
- active site: N148 (= N146), K171 (= K169), E246 (= E244), C280 (= C278), E377 (= E376), P455 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: F144 (= F142), Y147 (= Y145), N148 (= N146), K171 (= K169), S173 (= S171), E174 (= E172), G207 (= G205), T222 (= T220), G223 (= G221), S224 (= S222), V227 (≠ T225), E246 (= E244), M247 (= M245), G248 (= G246), C280 (= C278), E377 (= E376), F379 (= F378)
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
61% identity, 99% coverage: 3:487/488 of query aligns to 5:488/488 of 5u0lA
- active site: N148 (= N146), K171 (= K169), E246 (= E244), C280 (= C278), E377 (= E376), P455 (≠ A454)
- binding decanal: K107 (= K105), H152 (= H150), L153 (= L151), G156 (= G154), H157 (= H155), S456 (= S455), A457 (= A456)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
35% identity, 94% coverage: 6:462/488 of query aligns to 14:471/481 of 3jz4A
- active site: N156 (= N146), K179 (= K169), E254 (= E244), C288 (= C278), E385 (= E376), E462 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P144), W155 (≠ Y145), K179 (= K169), A181 (≠ S171), S182 (≠ E172), A212 (= A201), G216 (= G205), G232 (= G221), S233 (= S222), I236 (≠ T225), C288 (= C278), K338 (≠ D333), E385 (= E376), F387 (= F378)
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)
35% identity, 94% coverage: 6:462/488 of query aligns to 15:472/482 of P25526
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
32% identity, 84% coverage: 3:410/488 of query aligns to 4:415/494 of 5izdA
- active site: N149 (= N146), K172 (= K169), E247 (= E244), C281 (= C278), E381 (= E376)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ F142), T146 (≠ G143), W148 (≠ Y145), K172 (= K169), P173 (= P170), S174 (= S171), S175 (≠ E172), R204 (vs. gap), G205 (≠ A201), G209 (= G205), D210 (≠ I206), G225 (= G221), S226 (= S222), T229 (= T225)
Sites not aligning to the query:
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
30% identity, 94% coverage: 3:461/488 of query aligns to 18:478/491 of 5gtlA
- active site: N165 (= N146), K188 (= K169), E263 (= E244), C297 (= C278), E394 (= E376), E471 (≠ A454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ F142), P163 (= P144), K188 (= K169), A190 (≠ S171), E191 (= E172), Q192 (≠ L173), G221 (≠ A201), G225 (= G205), G241 (= G221), S242 (= S222), T245 (= T225), L264 (≠ M245), C297 (= C278), E394 (= E376), F396 (= F378)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
30% identity, 94% coverage: 3:461/488 of query aligns to 18:478/491 of 5gtkA
- active site: N165 (= N146), K188 (= K169), E263 (= E244), C297 (= C278), E394 (= E376), E471 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ F142), I162 (≠ G143), P163 (= P144), W164 (≠ Y145), K188 (= K169), E191 (= E172), G221 (≠ A201), G225 (= G205), A226 (≠ I206), F239 (= F219), G241 (= G221), S242 (= S222), T245 (= T225), Y248 (≠ H228), L264 (≠ M245), C297 (= C278), Q344 (≠ A327), R347 (≠ A330), E394 (= E376), F396 (= F378)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
32% identity, 94% coverage: 5:462/488 of query aligns to 30:494/515 of 2d4eC
- active site: N173 (= N146), K196 (= K169), E271 (= E244), C305 (= C278), E409 (= E376), E486 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F142), T170 (≠ G143), P171 (= P144), W172 (≠ Y145), K196 (= K169), A198 (≠ S171), G229 (≠ A201), G233 (= G205), A234 (≠ I206), T248 (= T220), G249 (= G221), E250 (≠ S222), T253 (= T225), E271 (= E244), L272 (≠ M245), C305 (= C278), E409 (= E376), F411 (= F378), F475 (= F443)
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)
32% identity, 93% coverage: 2:453/488 of query aligns to 7:463/490 of Q9HTJ1
- GAWN 150:153 (≠ GPYN 143:146) binding
- K162 (≠ H155) active site, Charge relay system
- KPSE 176:179 (= KPSE 169:172) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ SSRT 222:225) binding
- E252 (= E244) active site, Proton acceptor
- C286 (= C278) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E376) binding
Sites not aligning to the query:
- 464 active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
32% identity, 93% coverage: 2:453/488 of query aligns to 6:462/489 of 4cazA
- active site: N152 (= N146), K175 (= K169), E251 (= E244), C285 (= C278), E386 (= E376)
- 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 (≠ F142), G149 (= G143), W151 (≠ Y145), N152 (= N146), K175 (= K169), E178 (= E172), G208 (vs. gap), G212 (= G205), F226 (= F219), T227 (= T220), G228 (= G221), G229 (≠ S222), T232 (= T225), V236 (≠ L229), E251 (= E244), L252 (≠ M245), C285 (= C278), E386 (= E376), F388 (= F378)
Sites not aligning to the query:
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
32% identity, 93% coverage: 2:453/488 of query aligns to 6:462/489 of 2woxA
- active site: N152 (= N146), K175 (= K169), E251 (= E244), C285 (= C278), E386 (= E376)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F142), G149 (= G143), W151 (≠ Y145), N152 (= N146), K175 (= K169), S177 (= S171), E178 (= E172), G208 (vs. gap), G212 (= G205), F226 (= F219), T227 (= T220), G228 (= G221), G229 (≠ S222), T232 (= T225), V236 (≠ L229), E251 (= E244), L252 (≠ M245), C285 (= C278), E386 (= E376), F388 (= F378)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
32% identity, 93% coverage: 2:453/488 of query aligns to 6:462/489 of 2wmeA
- active site: N152 (= N146), K175 (= K169), E251 (= E244), C285 (= C278), E386 (= E376)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G143), W151 (≠ Y145), K175 (= K169), S177 (= S171), E178 (= E172), G208 (vs. gap), G212 (= G205), F226 (= F219), G228 (= G221), G229 (≠ S222), T232 (= T225), V236 (≠ L229)
Sites not aligning to the query:
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)
31% identity, 94% coverage: 5:462/488 of query aligns to 13:476/487 of Q9H2A2
- R109 (≠ S101) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N146) mutation to A: Complete loss of activity.
- R451 (≠ A437) mutation to A: Complete loss of activity.
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
29% identity, 94% coverage: 5:462/488 of query aligns to 6:472/483 of 4npiA
- active site: N152 (= N146), K175 (= K169), E251 (= E244), C285 (= C278), E387 (= E376), E464 (≠ A454)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (vs. gap), L157 (= L151), W160 (≠ G154), E251 (= E244), C285 (= C278), Y445 (≠ T435), R447 (≠ A437), F453 (= F443)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F142), S149 (≠ G143), P150 (= P144), W151 (≠ Y145), K175 (= K169), E178 (= E172), G208 (= G200), G213 (= G205), E214 (≠ I206), F227 (= F219), G229 (= G221), E230 (≠ S222), T233 (= T225), G253 (= G246), C285 (= C278), K335 (≠ A330), E387 (= E376), F389 (= F378)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
32% identity, 93% coverage: 1:453/488 of query aligns to 5:461/489 of 6wsbA
- active site: N152 (= N146), E250 (= E244), C284 (= C278)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F142), G149 (= G143), A150 (≠ P144), W151 (≠ Y145), N152 (= N146), K175 (= K169), E178 (= E172), G208 (≠ R202), G211 (= G205), A212 (≠ I206), F225 (= F219), T226 (= T220), G227 (= G221), G228 (≠ S222), T231 (= T225), V235 (≠ L229), E250 (= E244), L251 (≠ M245), G252 (= G246), C284 (= C278), E385 (= E376), F387 (= F378)
Sites not aligning to the query:
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
34% identity, 83% coverage: 54:458/488 of query aligns to 63:466/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F142), T153 (≠ G143), P154 (= P144), K179 (= K169), A212 (= A201), K213 (≠ R202), F230 (= F219), T231 (= T220), G232 (= G221), S233 (= S222), V236 (≠ T225), W239 (≠ H228), G256 (= G246)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 93% coverage: 5:459/488 of query aligns to 4:461/476 of 4yweA
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
32% identity, 94% coverage: 5:461/488 of query aligns to 21:483/495 of 5iuwA
- active site: N166 (= N146), K189 (= K169), E265 (= E244), C300 (= C278), E399 (= E376), D476 (≠ A454)
- binding 1h-indol-3-ylacetic acid: F167 (= F147), M170 (≠ H150), C300 (= C278), D457 (≠ T435), F465 (= F443)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ F142), V163 (≠ G143), P164 (= P144), W165 (≠ Y145), N166 (= N146), K189 (= K169), G222 (≠ R202), G226 (= G205), K227 (≠ I206), F240 (= F219), T241 (= T220), G242 (= G221), S243 (= S222), I246 (≠ T225), Y253 (≠ Q232), E265 (= E244), A266 (≠ M245), C300 (= C278), E399 (= E376), F401 (= F378)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
32% identity, 94% coverage: 5:461/488 of query aligns to 21:483/495 of 5iuvA
- active site: N166 (= N146), K189 (= K169), E265 (= E244), C300 (= C278), E399 (= E376), D476 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ F142), V163 (≠ G143), P164 (= P144), W165 (≠ Y145), N166 (= N146), K189 (= K169), S191 (= S171), G222 (≠ R202), G226 (= G205), K227 (≠ I206), F240 (= F219), T241 (= T220), G242 (= G221), S243 (= S222), I246 (≠ T225), Y253 (≠ Q232), E265 (= E244), A266 (≠ M245), C300 (= C278), E399 (= E376), F401 (= F378)
Query Sequence
>Pf1N1B4_3444 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3444
MNSLYIAGEWLAGQGESFQSVNPVTQQVLWAGEGATTGQVESAVQAARQAFPGWARRTLE
ERIGVLEAFAAALKNHADELARTIGEETGKPLWEAATEVTSMVNKIAISVQSYRERTGEK
SGPLGDATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNSVLFKPSELTPKVAEL
TVKCWIEAGLPAGVLNLLQGARETGIALAANPGIDGLFFTGSSRTGNHLHKQFSGRPDKI
LALEMGGNNPLVVDQVADLDAAVYTIIQSAFISAGQRCTCARRLLVPQGAWGDTLLARLV
AVSSTIEVGAFDQQPAPFMGSVISLGAAKALMDAQEHLLANGAVALLEMTQPQAQAALLT
PGILDVTAVADRPDEELFGPLLQVIRYADFEAAIAEANDTDYGLAAGLLSDSEARYQQFW
LESRAGIVNWNKQLTGAASSAPFGGVGASGNHRASAYYAADYCAYPVASLETPSLVLPAT
LTPGVKMV
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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