SitesBLAST
Comparing GFF3174 PGA1_c32250 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC 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)
51% identity, 96% coverage: 20:494/494 of query aligns to 21:495/495 of 5iuwA
- active site: N166 (= N165), K189 (= K188), E265 (= E264), C300 (= C299), E399 (= E398), D476 (= D475)
- binding 1h-indol-3-ylacetic acid: F167 (= F166), M170 (= M169), C300 (= C299), D457 (≠ G456), F465 (≠ L464)
- binding nicotinamide-adenine-dinucleotide: I162 (= I161), V163 (≠ I162), P164 (= P163), W165 (= W164), N166 (= N165), K189 (= K188), G222 (= G221), G226 (= G225), K227 (≠ E226), F240 (= F239), T241 (= T240), G242 (= G241), S243 (= S242), I246 (≠ T245), Y253 (= Y252), E265 (= E264), A266 (≠ L265), C300 (= C299), E399 (= E398), F401 (= F400)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
51% identity, 96% coverage: 20:494/494 of query aligns to 21:495/495 of 5iuvA
- active site: N166 (= N165), K189 (= K188), E265 (= E264), C300 (= C299), E399 (= E398), D476 (= D475)
- binding nicotinamide-adenine-dinucleotide: I162 (= I161), V163 (≠ I162), P164 (= P163), W165 (= W164), N166 (= N165), K189 (= K188), S191 (= S190), G222 (= G221), G226 (= G225), K227 (≠ E226), F240 (= F239), T241 (= T240), G242 (= G241), S243 (= S242), I246 (≠ T245), Y253 (= Y252), E265 (= E264), A266 (≠ L265), C300 (= C299), E399 (= E398), F401 (= F400)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
50% identity, 96% coverage: 20:494/494 of query aligns to 21:495/495 of 7jsoA
- active site: N166 (= N165), E265 (= E264), A300 (≠ C299), D476 (= D475)
- binding 1h-indol-3-ylacetic acid: F167 (= F166), W174 (= W173), V299 (= V298), A300 (≠ C299), T301 (≠ V300), D457 (≠ G456), F465 (≠ L464)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I161), V163 (≠ I162), P164 (= P163), W165 (= W164), K189 (= K188), E192 (= E191), G222 (= G221), G226 (= G225), K227 (≠ E226), F240 (= F239), G242 (= G241), S243 (= S242), I246 (≠ T245), A266 (≠ L265), G267 (= G266), A300 (≠ C299), E399 (= E398), F401 (= F400)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
43% identity, 96% coverage: 20:494/494 of query aligns to 7:479/489 of 4o6rA
- active site: N150 (= N165), K173 (= K188), E248 (= E264), C282 (= C299), E383 (= E398), E460 (≠ D475)
- binding adenosine monophosphate: I146 (= I161), V147 (≠ I162), K173 (= K188), G206 (= G221), G210 (= G225), Q211 (≠ E226), F224 (= F239), G226 (= G241), S227 (= S242), T230 (= T245), R233 (= R248)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
43% identity, 96% coverage: 20:492/494 of query aligns to 24:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I161), L166 (≠ I162), P167 (= P163), W168 (= W164), K192 (= K188), G225 (= G221), G229 (= G225), F243 (= F239), G245 (= G241), S246 (= S242), T249 (= T245), L252 (≠ R248), F253 (≠ L249), Y256 (= Y252), C269 (≠ L265), G270 (= G266), C303 (= C299), H350 (≠ Q346), K353 (≠ R349), F400 (= F400)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
42% identity, 96% coverage: 21:494/494 of query aligns to 7:477/487 of 4go4A
- active site: N149 (= N165), K172 (= K188), E247 (= E264), C281 (= C299), E381 (= E398), E458 (≠ D475)
- binding nicotinamide-adenine-dinucleotide: I145 (= I161), V146 (≠ I162), W148 (= W164), N149 (= N165), F154 (≠ I170), K172 (= K188), G205 (= G221), G209 (= G225), Q210 (≠ E226), F223 (= F239), T224 (= T240), G225 (= G241), S226 (= S242), T229 (= T245), E247 (= E264), G249 (= G266), C281 (= C299), E381 (= E398), F383 (= F400)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
40% identity, 98% coverage: 12:494/494 of query aligns to 21:497/503 of O14293
- S248 (= S242) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
39% identity, 96% coverage: 20:494/494 of query aligns to 23:495/501 of Q56YU0
- G152 (= G148) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A415) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 96% coverage: 17:489/494 of query aligns to 18:493/498 of 4go2A
- active site: N170 (= N165), K193 (= K188), E269 (= E264), C303 (= C299), E400 (= E398), D479 (= D475)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I161), I167 (= I162), P168 (= P163), W169 (= W164), K193 (= K188), A195 (≠ S190), Q196 (≠ E191), S225 (≠ E220), G226 (= G221), G230 (= G225), Q231 (≠ E226), F244 (= F239), G246 (= G241), S247 (= S242), V250 (≠ T245), I254 (≠ L249), E269 (= E264), G271 (= G266), C303 (= C299), E400 (= E398), F402 (= F400)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 96% coverage: 17:489/494 of query aligns to 18:493/498 of 2o2rA
- active site: N170 (= N165), K193 (= K188), E269 (= E264), C303 (= C299), E400 (= E398), D479 (= D475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I161), I167 (= I162), W169 (= W164), K193 (= K188), A195 (≠ S190), Q196 (≠ E191), S225 (≠ E220), G226 (= G221), G230 (= G225), Q231 (≠ E226), F244 (= F239), S247 (= S242), V250 (≠ T245), I254 (≠ L249)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
41% identity, 95% coverage: 20:489/494 of query aligns to 14:483/494 of 4pz2B
- active site: N159 (= N165), K182 (= K188), E258 (= E264), C292 (= C299), E392 (= E398), D469 (= D475)
- binding nicotinamide-adenine-dinucleotide: I155 (= I161), I156 (= I162), P157 (= P163), W158 (= W164), N159 (= N165), M164 (≠ I170), K182 (= K188), A184 (≠ S190), E185 (= E191), G215 (= G221), G219 (= G225), F233 (= F239), T234 (= T240), G235 (= G241), S236 (= S242), V239 (≠ T245), E258 (= E264), L259 (= L265), C292 (= C299), E392 (= E398), F394 (= F400)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 96% coverage: 17:489/494 of query aligns to 103:578/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K188), S310 (≠ E220), G311 (= G221), G315 (= G225), G331 (= G241), S332 (= S242), V335 (≠ T245)
- binding 4'-phosphopantetheine: K201 (= K115), F382 (≠ R293), N387 (≠ V298), C388 (= C299), N545 (≠ G456)
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)
38% identity, 96% coverage: 17:489/494 of query aligns to 422:897/902 of P28037
- IPW 571:573 (= IPW 162:164) binding
- KPAQ 597:600 (≠ KPSE 188:191) binding
- GSLVGQ 630:635 (≠ GAVVGE 221:226) binding
- GS 650:651 (= GS 241:242) binding
- E673 (= E264) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 264:265) binding
- C707 (= C299) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ R349) binding
- ESF 804:806 (≠ EVF 398:400) 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.
7radA Crystal structure analysis of aldh1b1
38% identity, 97% coverage: 14:494/494 of query aligns to 10:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I161), I159 (= I162), P160 (= P163), W161 (= W164), N162 (= N165), M167 (≠ I170), K185 (= K188), E188 (= E191), G218 (= G221), G222 (= G225), A223 (≠ E226), T237 (= T240), G238 (= G241), S239 (= S242), V242 (≠ T245), E261 (= E264), L262 (= L265), C295 (= C299), E392 (= E398), F394 (= F400)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ A116), E117 (≠ S120), F163 (= F166), E285 (≠ A289), F289 (≠ R293), N450 (≠ G456), V452 (≠ A458)
7mjdA Crystal structure analysis of aldh1b1
38% identity, 97% coverage: 14:494/494 of query aligns to 10:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I161), I159 (= I162), P160 (= P163), W161 (= W164), N162 (= N165), M167 (≠ I170), K185 (= K188), E188 (= E191), G218 (= G221), G222 (= G225), F236 (= F239), T237 (= T240), G238 (= G241), S239 (= S242), V242 (≠ T245), E261 (= E264), L262 (= L265), C295 (= C299), E392 (= E398), F394 (= F400)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ S120), E285 (≠ A289), F289 (≠ R293), N450 (≠ G456), V452 (≠ A458)
7mjcA Crystal structure analysis of aldh1b1
38% identity, 97% coverage: 14:494/494 of query aligns to 10:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I161), I159 (= I162), P160 (= P163), W161 (= W164), N162 (= N165), K185 (= K188), E188 (= E191), G218 (= G221), G222 (= G225), T237 (= T240), G238 (= G241), S239 (= S242), V242 (≠ T245), E261 (= E264), L262 (= L265), C295 (= C299), E392 (= E398), F394 (= F400)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 99% coverage: 5:494/494 of query aligns to 8:490/491 of 5gtlA
- active site: N165 (= N165), K188 (= K188), E263 (= E264), C297 (= C299), E394 (= E398), E471 (≠ D475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I161), P163 (= P163), K188 (= K188), A190 (≠ S190), E191 (= E191), Q192 (≠ T192), G221 (= G221), G225 (= G225), G241 (= G241), S242 (= S242), T245 (= T245), L264 (= L265), C297 (= C299), E394 (= E398), F396 (= F400)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 99% coverage: 5:494/494 of query aligns to 8:490/491 of 5gtkA
- active site: N165 (= N165), K188 (= K188), E263 (= E264), C297 (= C299), E394 (= E398), E471 (≠ D475)
- binding nicotinamide-adenine-dinucleotide: I161 (= I161), I162 (= I162), P163 (= P163), W164 (= W164), K188 (= K188), E191 (= E191), G221 (= G221), G225 (= G225), A226 (≠ E226), F239 (= F239), G241 (= G241), S242 (= S242), T245 (= T245), Y248 (≠ R248), L264 (= L265), C297 (= C299), Q344 (= Q346), R347 (= R349), E394 (= E398), F396 (= F400)
Q3SY69 Mitochondrial 10-formyltetrahydrofolate dehydrogenase; Mitochondrial 10-FTHFDH; mtFDH; Aldehyde dehydrogenase family 1 member L2; EC 1.5.1.6 from Homo sapiens (Human) (see paper)
38% identity, 97% coverage: 13:489/494 of query aligns to 442:918/923 of Q3SY69
Sites not aligning to the query:
- 374 S→A: No effect on phosphopantetheinylation.
- 375 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 95% coverage: 20:489/494 of query aligns to 9:475/486 of 4pxlA
- active site: N154 (= N165), K177 (= K188), E253 (= E264), C287 (= C299), E384 (= E398), D461 (= D475)
- binding nicotinamide-adenine-dinucleotide: I150 (= I161), V151 (≠ I162), P152 (= P163), W153 (= W164), K177 (= K188), E180 (= E191), G210 (= G221), G214 (= G225), A215 (≠ E226), F228 (= F239), G230 (= G241), S231 (= S242), V234 (≠ T245), E253 (= E264), G255 (= G266), C287 (= C299), Q334 (= Q346), K337 (≠ R349), E384 (= E398), F386 (= F400)
Query Sequence
>GFF3174 PGA1_c32250 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC
MDQTKIDTLRAQPVPCFSHLIDGQQVAASDGATMDVLSPIDGRLLTQIARGTVRDMERAI
ASARAAFEDRRWAGQPPAARKKVLMKWAELIEADALNLAVLGVRDNGTEITMALKAEPGS
AAATIRYYAEALDKIYGEIAPTSSDVLGMVHKEPVGVVGAIIPWNFPMMIGAWKLAPALA
MGNSVVLKPSETASLSLMRMVELALEAGLPPGVLNAVTGEGAVVGEALGLSMDVDVLVFT
GSGQTGRRLMEYAARSNLKRVYLELGGKSPNIVFADAPDLADAAKVTAAGIFRNSGQVCV
AGSRLLVEASIHDAFVEEVAKAAQMMRVGDPLRLDTQIGAINSEAQLARNLQFVARAEVE
GGQIITGGQRLLSETGGSYMAPTIVTGVTPDATLAQEEVFGPVLAVTPFETDAEALRIAN
ATVYGLAGAVWTSGLTRAHRMVQGVRTGVMHVNTYGGADGTVPLGGVGQSGNGADKSLHA
IDKYINLKTAWMKL
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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