SitesBLAST
Comparing AO356_18740 AO356_18740 succinylglutamate-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)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
82% 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)
34% 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)
34% 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:
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)
30% identity, 94% coverage: 2:462/488 of query aligns to 5:476/487 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.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
29% 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
29% 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 (≠ L228), L264 (≠ M245), C297 (= C278), Q344 (≠ A327), R347 (≠ A330), E394 (= E376), F396 (= F378)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 94% coverage: 4:461/488 of query aligns to 12:479/505 of O24174
- N164 (= N146) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ G154) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
31% 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)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
31% 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:
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
31% identity, 92% coverage: 4:453/488 of query aligns to 10:469/503 of Q8VWZ1
- N27 (≠ S20) binding
- I28 (≠ L21) binding
- D99 (≠ E87) binding
- L189 (= L173) binding
- 238:245 (vs. 221:228, 63% identical) binding
- C294 (= C278) binding
- E393 (= E376) binding
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 94% coverage: 4:463/488 of query aligns to 6:470/489 of 4o6rA
- active site: N150 (= N146), K173 (= K169), E248 (= E244), C282 (= C278), E383 (= E376), E460 (≠ A454)
- binding adenosine monophosphate: I146 (≠ F142), V147 (≠ G143), K173 (= K169), G206 (≠ R202), G210 (= G205), Q211 (≠ I206), F224 (= F219), G226 (= G221), S227 (= S222), T230 (= T225), R233 (≠ L228)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
31% identity, 92% coverage: 4:453/488 of query aligns to 5:464/497 of 3iwkH
- active site: N157 (= N146), K180 (= K169), E255 (= E244), C289 (= C278), E388 (= E376)
- binding nicotinamide-adenine-dinucleotide: W156 (≠ Y145), G213 (≠ A201), G217 (= G205), A218 (≠ I206), G233 (= G221), S234 (= S222), T237 (= T225), K240 (≠ L228), C289 (= C278), Q336 (≠ A327), E388 (= E376), F390 (= F378)
Sites not aligning to the query:
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
32% 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 (≠ L228), 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
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
31% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2eiwA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding proline: E137 (≠ S101), F185 (= F147), S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
Q93YB2 Aminoaldehyde dehydrogenase 2, peroxisomal; PsAMADH2; Aminobutyraldehyde dehydrogenase AMADH2; Gamma-guanidinobutyraldehyde dehydrogenase AMADH2; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
32% identity, 94% coverage: 4:461/488 of query aligns to 10:477/503 of Q93YB2
- I28 (≠ L21) binding
- D99 (≠ E87) binding
- W161 (≠ Y145) binding
- K185 (= K169) binding
- L189 (= L173) binding
- S239 (= S222) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
32% identity, 94% coverage: 4:461/488 of query aligns to 7:474/500 of 3iwjA
- active site: N159 (= N146), K182 (= K169), E257 (= E244), C291 (= C278), E390 (= E376), E467 (≠ A454)
- binding glycerol: D110 (≠ K105), Y160 (≠ F147), W167 (≠ G154), I290 (≠ R277), C291 (= C278), C450 (≠ A437), W456 (≠ F443)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F142), T156 (≠ G143), W158 (≠ Y145), K182 (= K169), S184 (= S171), E185 (= E172), G215 (≠ A201), A220 (≠ I206), F233 (= F219), G235 (= G221), S236 (= S222), T239 (= T225), I243 (≠ L229)
Query Sequence
>AO356_18740 AO356_18740 succinylglutamate-semialdehyde dehydrogenase
MNSLYIAGSWLEGQGDLFESLNPVTQQVLWSGNGATAAQVESAVQAARQAFPDWARRSLD
ERIQVLEAFAAALKSHADELAQCIGEETGKPLWEAATEVTSMVNKVAISVQSYRERTGEK
SGPLGDATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNSVLFKPSELTPKVAEL
TVKCWVEAGLPAGVLNLLQGARETGIALAANPGIDGLFFTGSSRTGNLLHQQFSGRPDKI
LALEMGGNNPLVVDEVADVDAAVYTIIQSAFISAGQRCTCARRLLVPEGAWGDALLARLV
AVSSTLEVGAFDQQPAPFMGSVISLGAAKALMDAQNHLLGKGAVPLLAMTQPQPQAALLT
PGILDVTAVAERPDEELFGPLLQVIRYTDFAAAITEANNTQYGLAAGLLSDSQARYQQFW
LQSRAGIVNWNKQLTGAASSAPFGGVGASGNHRASAYYAADYCAYPVASLETPSLVMPAA
LTPGVRMS
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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