SitesBLAST
Comparing CCNA_00865 CCNA_00865 alpha-ketoglutaric semialdehyde dehydrogenase xylA 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)
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)
38% identity, 98% coverage: 6:473/478 of query aligns to 21:490/501 of Q56YU0
- G152 (≠ I133) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A397) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
34% identity, 98% coverage: 5:473/478 of query aligns to 10:482/487 of Q9H2A2
- R109 (= R104) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N150) mutation to A: Complete loss of activity.
- R451 (≠ G440) mutation to A: Complete loss of activity.
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
37% identity, 97% coverage: 7:469/478 of query aligns to 16:493/511 of 6fkuA
- active site: N159 (= N150), E261 (= E247), C295 (= C281), E483 (= E459)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I146), T156 (= T147), N159 (= N150), K182 (= K173), S184 (≠ A175), E185 (≠ G176), G214 (vs. gap), G215 (= G204), K216 (≠ R205), G220 (= G209), Q221 (≠ D210), F237 (= F223), T238 (= T224), G239 (= G225), S240 (= S226), V243 (= V229), E261 (= E247), L262 (≠ M248), C295 (= C281), R342 (≠ D327), F343 (≠ Q328), E404 (= E380), F406 (= F382)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
38% identity, 95% coverage: 21:475/478 of query aligns to 22:476/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E247), C282 (= C281), E383 (= E380), E460 (= E459)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ T147), K173 (= K173), G206 (= G206), G210 (= G209), Q211 (≠ D210), F224 (= F223), G226 (= G225), S227 (= S226), T230 (≠ V229), R233 (≠ Q232)
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
35% identity, 98% coverage: 6:472/478 of query aligns to 19:489/505 of 4neaA
- active site: N166 (= N150), K189 (= K173), E264 (= E247), C298 (= C281), E399 (= E380), E476 (= E459)
- binding nicotinamide-adenine-dinucleotide: P164 (= P148), K189 (= K173), E192 (≠ G176), G222 (= G206), G226 (= G209), G242 (= G225), G243 (≠ S226), T246 (≠ V229), H249 (≠ Q232), I250 (≠ V233), C298 (= C281), E399 (= E380), F401 (= F382)
P42412 Malonate-semialdehyde dehydrogenase; MSA dehydrogenase; Methylmalonate-semialdehyde dehydrogenase; MMSA dehydrogenase; MMSDH; MSDH; EC 1.2.1.27 from Bacillus subtilis (strain 168) (see 3 papers)
34% identity, 98% coverage: 5:472/478 of query aligns to 7:475/487 of P42412
- C36 (≠ A33) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-160; A-287; A-351 and A-413.
- R107 (= R104) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T147) binding
- F152 (≠ W149) binding
- C160 (≠ A157) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-287; A-351 and A-413.
- K176 (= K173) binding
- E179 (≠ G176) binding
- R180 (≠ P177) binding
- S229 (= S226) binding
- T251 (≠ M248) binding
- R283 (= R280) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ S284) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-351 and A-413.
- C351 (≠ T348) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-413.
- E382 (= E380) binding
- C413 (≠ G411) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
34% identity, 98% coverage: 5:472/478 of query aligns to 5:473/484 of 1t90A
- active site: N151 (= N150), K174 (= K173), L248 (≠ E247), C282 (= C281), E380 (= E380), A460 (≠ E459)
- binding nicotinamide-adenine-dinucleotide: I147 (= I146), A148 (≠ T147), P149 (= P148), F150 (≠ W149), N151 (= N150), W159 (= W158), K174 (= K173), E177 (≠ G176), R178 (≠ P177), H207 (≠ G206), V225 (≠ T224), G226 (= G225), S227 (= S226), V230 (= V229), L248 (≠ E247), T249 (≠ M248), C282 (= C281), E380 (= E380), F382 (= F382)
7radA Crystal structure analysis of aldh1b1
38% identity, 95% coverage: 22:473/478 of query aligns to 32:483/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (= W149), N162 (= N150), M167 (≠ I155), K185 (= K173), E188 (≠ G176), G218 (= G206), G222 (= G209), A223 (≠ D210), T237 (= T224), G238 (= G225), S239 (= S226), V242 (= V229), E261 (= E247), L262 (≠ M248), C295 (= C281), 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 (≠ E101), E117 (≠ R104), F163 (= F151), E285 (≠ D271), F289 (= F275), N450 (≠ T438), V452 (= V441)
7mjdA Crystal structure analysis of aldh1b1
38% identity, 95% coverage: 22:473/478 of query aligns to 32:483/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (= W149), N162 (= N150), M167 (≠ I155), K185 (= K173), E188 (≠ G176), G218 (= G206), G222 (= G209), F236 (= F223), T237 (= T224), G238 (= G225), S239 (= S226), V242 (= V229), E261 (= E247), L262 (≠ M248), C295 (= C281), 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 (≠ R104), E285 (≠ D271), F289 (= F275), N450 (≠ T438), V452 (= V441)
7mjcA Crystal structure analysis of aldh1b1
38% identity, 95% coverage: 22:473/478 of query aligns to 32:483/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (= W149), N162 (= N150), K185 (= K173), E188 (≠ G176), G218 (= G206), G222 (= G209), T237 (= T224), G238 (= G225), S239 (= S226), V242 (= V229), E261 (= E247), L262 (≠ M248), C295 (= C281), E392 (= E380), F394 (= F382)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 95% coverage: 21:473/478 of query aligns to 24:475/486 of 4pxlA
- active site: N154 (= N150), K177 (= K173), E253 (= E247), C287 (= C281), E384 (= E380), D461 (≠ E459)
- binding nicotinamide-adenine-dinucleotide: I150 (= I146), V151 (≠ T147), P152 (= P148), W153 (= W149), K177 (= K173), E180 (≠ G176), G210 (= G206), G214 (= G209), A215 (≠ D210), F228 (= F223), G230 (= G225), S231 (= S226), V234 (= V229), E253 (= E247), G255 (= G249), C287 (= C281), Q334 (= Q328), K337 (≠ T331), E384 (= E380), F386 (= F382)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
38% identity, 98% coverage: 8:475/478 of query aligns to 14:481/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W149), K180 (= K173), A182 (= A175), T212 (≠ R205), G213 (= G206), G217 (= G209), F231 (= F223), G233 (= G225), S234 (= S226), V237 (= V229), Q337 (= Q328), E388 (= E380), F390 (= F382)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
38% identity, 98% coverage: 8:475/478 of query aligns to 13:480/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I146), T153 (= T147), P154 (= P148), W155 (= W149), N156 (= N150), I161 (= I155), K179 (= K173), A181 (= A175), E182 (≠ G176), T211 (≠ R205), G212 (= G206), G216 (= G209), Q217 (≠ D210), F230 (= F223), T231 (= T224), G232 (= G225), S233 (= S226), V236 (= V229), E255 (= E247), L256 (≠ M248), G257 (= G249), A289 (≠ C281), E387 (= E380), F389 (= F382)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 97% coverage: 9:472/478 of query aligns to 35:491/503 of O14293
- S248 (= S226) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
37% identity, 94% coverage: 24:472/478 of query aligns to 32:476/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
37% identity, 94% coverage: 24:472/478 of query aligns to 31:475/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E247), C288 (= C281), E385 (= E380), E462 (= E459)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P148), W155 (= W149), K179 (= K173), A181 (= A175), S182 (≠ G176), A212 (vs. gap), G216 (= G209), G232 (= G225), S233 (= S226), I236 (≠ V229), C288 (= C281), K338 (≠ T331), E385 (= E380), F387 (= F382)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 93% coverage: 28:473/478 of query aligns to 35:483/494 of 4pz2B
- active site: N159 (= N150), K182 (= K173), E258 (= E247), C292 (= C281), E392 (= E380), D469 (≠ E459)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), I156 (≠ T147), P157 (= P148), W158 (= W149), N159 (= N150), M164 (≠ I155), K182 (= K173), A184 (= A175), E185 (≠ G176), G215 (= G206), G219 (= G209), F233 (= F223), T234 (= T224), G235 (= G225), S236 (= S226), V239 (= V229), E258 (= E247), L259 (≠ M248), C292 (= C281), E392 (= E380), F394 (= F382)
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)
36% identity, 98% coverage: 6:473/478 of query aligns to 8:478/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 147:150) binding
- K162 (= K159) active site, Charge relay system
- KPSE 176:179 (≠ KPAG 173:176) binding
- G209 (= G206) binding
- GTST 230:233 (≠ SQGV 226:229) binding
- E252 (= E247) active site, Proton acceptor
- C286 (= C281) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E380) binding
- E464 (= E459) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
36% identity, 98% coverage: 6:473/478 of query aligns to 7:477/489 of 4cazA
- active site: N152 (= N150), K175 (= K173), E251 (= E247), C285 (= C281), E386 (= E380), E463 (= E459)
- 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 (= I146), G149 (≠ T147), W151 (= W149), N152 (= N150), K175 (= K173), E178 (≠ G176), G208 (= G206), G212 (= G209), F226 (= F223), T227 (= T224), G228 (= G225), G229 (≠ S226), T232 (≠ V229), V236 (= V233), E251 (= E247), L252 (≠ M248), C285 (= C281), E386 (= E380), F388 (= F382)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
36% identity, 98% coverage: 6:473/478 of query aligns to 7:477/489 of 2woxA
- active site: N152 (= N150), K175 (= K173), E251 (= E247), C285 (= C281), E386 (= E380), E463 (= E459)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I146), G149 (≠ T147), W151 (= W149), N152 (= N150), K175 (= K173), S177 (≠ A175), E178 (≠ G176), G208 (= G206), G212 (= G209), F226 (= F223), T227 (= T224), G228 (= G225), G229 (≠ S226), T232 (≠ V229), V236 (= V233), E251 (= E247), L252 (≠ M248), C285 (= C281), E386 (= E380), F388 (= F382)
Query Sequence
>CCNA_00865 CCNA_00865 alpha-ketoglutaric semialdehyde dehydrogenase xylA
MTDTLRHYIGGERVAADAPAESLNPSNTNDVVAKVPMGGQAEVDAAVDAARKAFPAWADA
SPEVRSDLLDKVGSTIIARSADIGRLLAREEGKTLAEGIGETVRAGRIFKYFAGEALRRH
GQNLESTRPGVEIQTYRQAVGVYGLITPWNFPIAIPAWKAAPALAFGNTVVIKPAGPTPA
TANVLADIMAECGAPAGVFNMLFGRGSMGDALIKHKDVDGVSFTGSQGVGAQVAAAAVAR
QARVQLEMGGKNPLIVLDDADLERAVAIALDGSFFATGQRCTASSRLIVQDGIHDKFVAL
LAEKVAALRVGDALDPNTQIGPAVSEDQMETSYRYIDIAASEGGRVVTGGDRIKLDNPGW
YVRPTLIADTQAGMRINNEEVFGPVASTIRVKSYEEALEIANGVEFGLSAGIATTSLKHA
RHFQRYARAGMTMVNLATAGVDYHVPFGGTKSSSYGAREQGFAAVEFFTQTKTSYSWS
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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