SitesBLAST
Comparing WP_011763950.1 NCBI__GCF_000061505.1:WP_011763950.1 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)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
40% identity, 96% coverage: 16:490/494 of query aligns to 21:495/495 of 5iuwA
- active site: N166 (= N160), K189 (= K183), E265 (= E259), C300 (= C294), E399 (= E393), D476 (= D471)
- binding 1h-indol-3-ylacetic acid: F167 (= F161), M170 (≠ V164), C300 (= C294), D457 (≠ R452), F465 (≠ T460)
- binding nicotinamide-adenine-dinucleotide: I162 (= I156), V163 (≠ T157), P164 (= P158), W165 (= W159), N166 (= N160), K189 (= K183), G222 (= G216), G226 (= G220), K227 (≠ E221), F240 (= F234), T241 (= T235), G242 (= G236), S243 (= S237), I246 (≠ T240), Y253 (≠ A247), E265 (= E259), A266 (≠ L260), C300 (= C294), E399 (= E393), F401 (= F395)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
40% identity, 96% coverage: 16:490/494 of query aligns to 21:495/495 of 5iuvA
- active site: N166 (= N160), K189 (= K183), E265 (= E259), C300 (= C294), E399 (= E393), D476 (= D471)
- binding nicotinamide-adenine-dinucleotide: I162 (= I156), V163 (≠ T157), P164 (= P158), W165 (= W159), N166 (= N160), K189 (= K183), S191 (= S185), G222 (= G216), G226 (= G220), K227 (≠ E221), F240 (= F234), T241 (= T235), G242 (= G236), S243 (= S237), I246 (≠ T240), Y253 (≠ A247), E265 (= E259), A266 (≠ L260), C300 (= C294), E399 (= E393), F401 (= F395)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
40% identity, 96% coverage: 16:490/494 of query aligns to 21:495/495 of 7jsoA
- active site: N166 (= N160), E265 (= E259), A300 (≠ C294), D476 (= D471)
- binding 1h-indol-3-ylacetic acid: F167 (= F161), W174 (= W168), V299 (= V293), A300 (≠ C294), T301 (≠ V295), D457 (≠ R452), F465 (≠ T460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I156), V163 (≠ T157), P164 (= P158), W165 (= W159), K189 (= K183), E192 (= E186), G222 (= G216), G226 (= G220), K227 (≠ E221), F240 (= F234), G242 (= G236), S243 (= S237), I246 (≠ T240), A266 (≠ L260), G267 (= G261), A300 (≠ C294), E399 (= E393), F401 (= F395)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
41% identity, 96% coverage: 16:490/494 of query aligns to 7:479/489 of 4o6rA
- active site: N150 (= N160), K173 (= K183), E248 (= E259), C282 (= C294), E383 (= E393), E460 (≠ D471)
- binding adenosine monophosphate: I146 (= I156), V147 (≠ T157), K173 (= K183), G206 (= G216), G210 (= G220), Q211 (≠ E221), F224 (= F234), G226 (= G236), S227 (= S237), T230 (= T240), R233 (≠ A243)
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)
38% identity, 96% coverage: 16:491/494 of query aligns to 10:484/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 157:160) binding NADPH
- K162 (= K169) active site, Charge relay system
- KPSE 176:179 (= KPSE 183:186) binding NADPH
- G209 (= G216) binding NADPH
- GTST 230:233 (≠ STRT 237:240) binding NADPH
- E252 (= E259) active site, Proton acceptor
- C286 (= C294) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E393) binding NADPH
- E464 (≠ D471) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
38% identity, 96% coverage: 16:491/494 of query aligns to 9:483/489 of 4cazA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C294), E386 (= E393), E463 (≠ D471)
- 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 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), E178 (= E186), G208 (= G216), G212 (= G220), F226 (= F234), T227 (= T235), G228 (= G236), G229 (≠ S237), T232 (= T240), V236 (≠ I244), E251 (= E259), L252 (= L260), C285 (= C294), E386 (= E393), F388 (= F395)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
38% identity, 96% coverage: 16:491/494 of query aligns to 9:483/489 of 2woxA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C294), E386 (= E393), E463 (≠ D471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), S177 (= S185), E178 (= E186), G208 (= G216), G212 (= G220), F226 (= F234), T227 (= T235), G228 (= G236), G229 (≠ S237), T232 (= T240), V236 (≠ I244), E251 (= E259), L252 (= L260), C285 (= C294), E386 (= E393), F388 (= F395)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
38% identity, 96% coverage: 16:491/494 of query aligns to 9:483/489 of 2wmeA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C294), E386 (= E393), E463 (≠ D471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T157), W151 (= W159), K175 (= K183), S177 (= S185), E178 (= E186), G208 (= G216), G212 (= G220), F226 (= F234), G228 (= G236), G229 (≠ S237), T232 (= T240), V236 (≠ I244)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 97% coverage: 12:491/494 of query aligns to 22:498/503 of O14293
- S248 (= S237) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 97% coverage: 13:490/494 of query aligns to 17:490/491 of 5gtlA
- active site: N165 (= N160), K188 (= K183), E263 (= E259), C297 (= C294), E394 (= E393), E471 (≠ D471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I156), P163 (= P158), K188 (= K183), A190 (≠ S185), E191 (= E186), Q192 (≠ L187), G221 (= G216), G225 (= G220), G241 (= G236), S242 (= S237), T245 (= T240), L264 (= L260), C297 (= C294), E394 (= E393), F396 (= F395)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 97% coverage: 13:490/494 of query aligns to 17:490/491 of 5gtkA
- active site: N165 (= N160), K188 (= K183), E263 (= E259), C297 (= C294), E394 (= E393), E471 (≠ D471)
- binding nicotinamide-adenine-dinucleotide: I161 (= I156), I162 (≠ T157), P163 (= P158), W164 (= W159), K188 (= K183), E191 (= E186), G221 (= G216), G225 (= G220), A226 (≠ E221), F239 (= F234), G241 (= G236), S242 (= S237), T245 (= T240), Y248 (≠ A243), L264 (= L260), C297 (= C294), Q344 (= Q341), R347 (= R344), E394 (= E393), F396 (= F395)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
35% identity, 97% coverage: 9:489/494 of query aligns to 14:497/498 of 4go2A
- active site: N170 (= N160), K193 (= K183), E269 (= E259), C303 (= C294), E400 (= E393), D479 (= D471)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I156), I167 (≠ T157), P168 (= P158), W169 (= W159), K193 (= K183), A195 (≠ S185), Q196 (≠ E186), S225 (≠ D215), G226 (= G216), G230 (= G220), Q231 (≠ E221), F244 (= F234), G246 (= G236), S247 (= S237), V250 (≠ T240), I254 (= I244), E269 (= E259), G271 (= G261), C303 (= C294), E400 (= E393), F402 (= F395)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
35% identity, 97% coverage: 9:489/494 of query aligns to 14:497/498 of 2o2rA
- active site: N170 (= N160), K193 (= K183), E269 (= E259), C303 (= C294), E400 (= E393), D479 (= D471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I156), I167 (≠ T157), W169 (= W159), K193 (= K183), A195 (≠ S185), Q196 (≠ E186), S225 (≠ D215), G226 (= G216), G230 (= G220), Q231 (≠ E221), F244 (= F234), S247 (= S237), V250 (≠ T240), I254 (= I244)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
35% identity, 97% coverage: 9:489/494 of query aligns to 99:582/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K183), S310 (≠ D215), G311 (= G216), G315 (= G220), G331 (= G236), S332 (= S237), V335 (≠ T240)
- binding 4'-phosphopantetheine: K201 (≠ A110), F382 (≠ G288), N387 (≠ V293), C388 (= C294), N545 (≠ G451)
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)
35% identity, 97% coverage: 9:489/494 of query aligns to 418:901/902 of P28037
- IPW 571:573 (≠ TPW 157:159) binding NADP(+)
- KPAQ 597:600 (≠ KPSE 183:186) binding NADP(+)
- GSLVGQ 630:635 (≠ GRTTGE 216:221) binding NADP(+)
- GS 650:651 (= GS 236:237) binding NADP(+)
- E673 (= E259) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 259:260) binding NADP(+)
- C707 (= C294) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ R344) binding NADP(+)
- ESF 804:806 (≠ EIF 393:395) binding NADP(+)
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.
P54115 Magnesium-activated aldehyde dehydrogenase, cytosolic; Mg(2+)-activated acetaldehyde dehydrogenase; Mg(2+)-ACDH; EC 1.2.1.-; EC 1.2.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
36% identity, 97% coverage: 12:490/494 of query aligns to 25:500/500 of P54115
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 3 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8rwkA Cryoem structure of the central ald4 filament determined by filamentid (see paper)
36% identity, 98% coverage: 1:486/494 of query aligns to 7:489/495 of 8rwkA
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 98% coverage: 3:487/494 of query aligns to 2:485/494 of 4pz2B
- active site: N159 (= N160), K182 (= K183), E258 (= E259), C292 (= C294), E392 (= E393), D469 (= D471)
- binding nicotinamide-adenine-dinucleotide: I155 (= I156), I156 (≠ T157), P157 (= P158), W158 (= W159), N159 (= N160), M164 (= M165), K182 (= K183), A184 (≠ S185), E185 (= E186), G215 (= G216), G219 (= G220), F233 (= F234), T234 (= T235), G235 (= G236), S236 (= S237), V239 (≠ T240), E258 (= E259), L259 (= L260), C292 (= C294), E392 (= E393), F394 (= F395)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
37% identity, 96% coverage: 16:487/494 of query aligns to 9:477/486 of 4pxlA
- active site: N154 (= N160), K177 (= K183), E253 (= E259), C287 (= C294), E384 (= E393), D461 (= D471)
- binding nicotinamide-adenine-dinucleotide: I150 (= I156), V151 (≠ T157), P152 (= P158), W153 (= W159), K177 (= K183), E180 (= E186), G210 (= G216), G214 (= G220), A215 (≠ E221), F228 (= F234), G230 (= G236), S231 (= S237), V234 (≠ T240), E253 (= E259), G255 (= G261), C287 (= C294), Q334 (= Q341), K337 (≠ R344), E384 (= E393), F386 (= F395)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex (see paper)
35% identity, 97% coverage: 9:489/494 of query aligns to 14:497/498 of 7yjjC
Query Sequence
>WP_011763950.1 NCBI__GCF_000061505.1:WP_011763950.1
MPIFDPDQIQVPVGHFIGGRLQTPAGAALEVQRPSDGKVYAALPVADEALVDIAAENAWT
AWKESDWARCAPRDRARVLRRWADLVEAEAPRLGVLEALGSTRPVRDAIAWDVPFTAEGL
RFFAEYADKLGGEVAATRHDHLGMVIAEPYGLIGAITPWNFPLVMVSWKVGAALAAGNAV
LLKPSELTPFSALRLAELAIQAGVPAGIFNIVQGDGRTTGEAITRHPRVSKMTFTGSTRT
GAAIMSACALHGPKPVTLELGGKSPQLVFDDVRDLDKLAATIAGAITGNAGQVCVAGSRL
IVQRRVAGALVERIRAIFTGHRPGATWDEDATLPPIISAQQAARIAAIVERAQAAGGRVK
CGGRIVDGGYGGAYYLPTLIDGVDTANPAVSEEIFGPVLTVQTFDDEEEGFALASHDSYG
LAAGVHTSDVGRAMRAVRRIEAGTVWVNRYGRSADFVIPTGGYHQSGIGKDLGRQAVEAN
LRFKSVLMDIGSPQ
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