SitesBLAST
Comparing RR42_RS27835 FitnessBrowser__Cup4G11:RR42_RS27835 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
49% identity, 99% coverage: 4:485/486 of query aligns to 29:514/515 of 2d4eC
- active site: N173 (= N146), K196 (= K169), E271 (= E242), C305 (= C276), E409 (= E380), E486 (= E457)
- binding nicotinamide-adenine-dinucleotide: I169 (= I142), T170 (≠ S143), P171 (= P144), W172 (= W145), K196 (= K169), A198 (≠ S171), G229 (= G202), G233 (= G206), A234 (≠ D207), T248 (= T221), G249 (= G222), E250 (≠ G223), T253 (= T226), E271 (= E242), L272 (= L243), C305 (= C276), E409 (= E380), F411 (= F382), F475 (= F446)
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)
40% identity, 98% coverage: 1:474/486 of query aligns to 9:485/487 of Q9H2A2
- R109 (= R101) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N146) mutation to A: Complete loss of activity.
- R451 (= R440) mutation to A: Complete loss of activity.
7radA Crystal structure analysis of aldh1b1
42% identity, 97% coverage: 5:476/486 of query aligns to 16:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I142), I159 (≠ S143), P160 (= P144), W161 (= W145), N162 (= N146), M167 (≠ T151), K185 (= K169), E188 (= E172), G218 (= G202), G222 (= G206), A223 (≠ D207), T237 (= T221), G238 (= G222), S239 (≠ G223), V242 (≠ T226), E261 (= E242), L262 (= L243), C295 (= C276), E392 (= E380), F394 (= F382)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ Q97), E117 (≠ R101), F163 (≠ V147), E285 (≠ F266), F289 (≠ S270), N450 (= N438), V452 (≠ R440)
7mjdA Crystal structure analysis of aldh1b1
42% identity, 97% coverage: 5:476/486 of query aligns to 16:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I142), I159 (≠ S143), P160 (= P144), W161 (= W145), N162 (= N146), M167 (≠ T151), K185 (= K169), E188 (= E172), G218 (= G202), G222 (= G206), F236 (= F220), T237 (= T221), G238 (= G222), S239 (≠ G223), V242 (≠ T226), E261 (= E242), L262 (= L243), C295 (= C276), E392 (= E380), F394 (= F382)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R101), E285 (≠ F266), F289 (≠ S270), N450 (= N438), V452 (≠ R440)
7mjcA Crystal structure analysis of aldh1b1
42% identity, 97% coverage: 5:476/486 of query aligns to 16:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I142), I159 (≠ S143), P160 (= P144), W161 (= W145), N162 (= N146), K185 (= K169), E188 (= E172), G218 (= G202), G222 (= G206), T237 (= T221), G238 (= G222), S239 (≠ G223), V242 (≠ T226), E261 (= E242), L262 (= L243), C295 (= C276), E392 (= E380), F394 (= F382)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
41% identity, 99% coverage: 5:484/486 of query aligns to 7:487/489 of 4o6rA
- active site: N150 (= N146), K173 (= K169), E248 (= E242), C282 (= C276), E383 (= E380), E460 (= E457)
- binding adenosine monophosphate: I146 (= I142), V147 (≠ S143), K173 (= K169), G206 (= G202), G210 (= G206), Q211 (≠ D207), F224 (= F220), G226 (= G222), S227 (≠ G223), T230 (= T226), R233 (= R229)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 26:488/493 of 4fr8A
- active site: N162 (= N146), K185 (= K169), Q261 (≠ E242), C295 (= C276), E392 (= E380), E469 (= E457)
- binding nicotinamide-adenine-dinucleotide: I158 (= I142), I159 (≠ S143), W161 (= W145), K185 (= K169), G218 (= G202), G222 (= G206), A223 (≠ D207), F236 (= F220), G238 (= G222), S239 (≠ G223), I242 (≠ T226), Q342 (≠ H323), K345 (= K326), E392 (= E380), F394 (= F382)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ V147), L166 (≠ M150), W170 (= W154), F289 (≠ S270), S294 (≠ R275), C295 (= C276), D450 (≠ N438), F452 (≠ R440)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 29:491/496 of 4fr8C
- active site: N165 (= N146), K188 (= K169), Q264 (≠ E242), C298 (= C276), E395 (= E380), E472 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I142), I162 (≠ S143), W164 (= W145), K188 (= K169), G221 (= G202), G225 (= G206), A226 (≠ D207), F239 (= F220), G241 (= G222), S242 (≠ G223), I245 (≠ T226), Q345 (≠ H323), E395 (= E380), F397 (= F382)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 5l13A
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ V147), M168 (≠ T151), W171 (= W154), F290 (≠ S270), C295 (≠ R275), C296 (= C276), C297 (≠ T277), D451 (≠ N438), F453 (≠ R440)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 4kwgA
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ V147), M168 (≠ T151), C295 (≠ R275), C296 (= C276), C297 (≠ T277), D451 (≠ N438), F453 (≠ R440)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 4kwfA
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ V147), M168 (≠ T151), W171 (= W154), E262 (= E242), C295 (≠ R275), C296 (= C276), C297 (≠ T277), D451 (≠ N438), F453 (≠ R440), F459 (= F446)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 3sz9A
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ V147), C295 (≠ R275), C296 (= C276), D451 (≠ N438), F453 (≠ R440), F459 (= F446)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 3injA
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ R101), F164 (≠ V147), L167 (≠ M150), F286 (= F266), F290 (≠ S270), D451 (≠ N438), F453 (≠ R440)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 2vleA
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding daidzin: M118 (≠ R101), F164 (≠ V147), M168 (≠ T151), W171 (= W154), F286 (= F266), F290 (≠ S270), C295 (≠ R275), C296 (= C276), D451 (≠ N438), V452 (= V439), F453 (≠ R440)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 1o01B
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding (2e)-but-2-enal: C296 (= C276), C297 (≠ T277), F453 (≠ R440)
- binding nicotinamide-adenine-dinucleotide: I159 (= I142), I160 (≠ S143), P161 (= P144), W162 (= W145), K186 (= K169), E189 (= E172), G219 (= G202), G223 (= G206), A224 (≠ D207), F237 (= F220), G239 (= G222), S240 (≠ G223), I243 (≠ T226), L263 (= L243), G264 (= G244), C296 (= C276), Q343 (≠ H323), E393 (= E380), F395 (= F382)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 1cw3A
- active site: N163 (= N146), K186 (= K169), E262 (= E242), C296 (= C276), E393 (= E380), E470 (= E457)
- binding magnesium ion: V34 (≠ W20), D103 (= D86), Q190 (≠ L173)
- binding nicotinamide-adenine-dinucleotide: I159 (= I142), I160 (≠ S143), P161 (= P144), W162 (= W145), K186 (= K169), G219 (= G202), G223 (= G206), A224 (≠ D207), F237 (= F220), G239 (= G222), S240 (≠ G223), I243 (≠ T226), L263 (= L243), G264 (= G244), C296 (= C276), Q343 (≠ H323), K346 (= K326), E393 (= E380), F395 (= F382)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
42% identity, 95% coverage: 13:476/486 of query aligns to 53:515/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
41% identity, 95% coverage: 13:476/486 of query aligns to 27:489/494 of 1nzwA
- active site: N163 (= N146), K186 (= K169), E262 (= E242), S296 (≠ C276), E393 (= E380), E470 (= E457)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I142), I160 (≠ S143), P161 (= P144), K186 (= K169), E189 (= E172), G219 (= G202), P220 (≠ A203), G223 (= G206), A224 (≠ D207), F237 (= F220), G239 (= G222), S240 (≠ G223), I243 (≠ T226), E262 (= E242), G264 (= G244), S296 (≠ C276), Q343 (≠ H323), E393 (= E380), F395 (= F382)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 98% coverage: 2:476/486 of query aligns to 17:490/491 of 5gtlA
- active site: N165 (= N146), K188 (= K169), E263 (= E242), C297 (= C276), E394 (= E380), E471 (= E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I142), P163 (= P144), K188 (= K169), A190 (≠ S171), E191 (= E172), Q192 (≠ L173), G221 (= G202), G225 (= G206), G241 (= G222), S242 (≠ G223), T245 (= T226), L264 (= L243), C297 (= C276), E394 (= E380), F396 (= F382)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 98% coverage: 2:476/486 of query aligns to 17:490/491 of 5gtkA
- active site: N165 (= N146), K188 (= K169), E263 (= E242), C297 (= C276), E394 (= E380), E471 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I142), I162 (≠ S143), P163 (= P144), W164 (= W145), K188 (= K169), E191 (= E172), G221 (= G202), G225 (= G206), A226 (≠ D207), F239 (= F220), G241 (= G222), S242 (≠ G223), T245 (= T226), Y248 (≠ R229), L264 (= L243), C297 (= C276), Q344 (≠ H323), R347 (≠ K326), E394 (= E380), F396 (= F382)
Query Sequence
>RR42_RS27835 FitnessBrowser__Cup4G11:RR42_RS27835
MIKHWINGKQVDSKDTFTTWNPATGEEIATVAAGGEAEVNAAVAAAKAAFPKWANTPAKE
RARIMRRLADLITEHVPHLAALETQDTGLPIAQTGKQLIPRAAENFNFFAEVCVQMNGRT
YPVDDQMLNYTLYQPVGVCALISPWNVPFMTATWKVAPCLALGNTAVLKMSELSPLTADQ
LGMLALEAGVPAGVLNVVQGYGASAGDALVRHPDVRAVSFTGGTATGKRIIERAGLKKFS
MELGGKSPVLVFDDADLERALDAALFTIFSINGERCTAGSRIFVQDTVYDDFAGKFAERA
RRLRVGDPTSEQTHVGAMITQQHWEKVTGYIRLGEQEGATILAGGAERPSDLPAHLRNGN
FVQPTVLANVENHMRVAQEEIFGPVACLIPFKGEDDGLAMANDTAYGLASYIWTQDVGKV
HRLARGIEAGMVFVNSQNVRDLRQPFGGTKASGTGREGGEFSFEVFAEVKNVCISMGGHH
IPRWGV
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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