SitesBLAST
Comparing CCNA_00618 CCNA_00618 succinylglutamic 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)
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
52% identity, 99% coverage: 8:472/472 of query aligns to 22:484/488 of 5u0mA
- active site: N148 (= N134), K171 (= K157), E246 (= E232), C280 (= C266), E377 (= E363), P455 (= P441)
- binding nicotinamide-adenine-dinucleotide: F144 (≠ I130), Y147 (≠ F133), N148 (= N134), K171 (= K157), S173 (= S159), E174 (= E160), G207 (= G193), T222 (= T208), G223 (= G209), S224 (≠ G210), V227 (≠ A213), E246 (= E232), M247 (≠ L233), G248 (= G234), C280 (= C266), E377 (= E363), F379 (= F365)
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
52% identity, 99% coverage: 8:472/472 of query aligns to 22:484/488 of 5u0lA
- active site: N148 (= N134), K171 (= K157), E246 (= E232), C280 (= C266), E377 (= E363), P455 (= P441)
- binding decanal: K107 (= K93), H152 (= H138), L153 (= L139), G156 (= G142), H157 (= H143), S456 (= S442), A457 (= A443)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
56% identity, 95% coverage: 24:472/472 of query aligns to 37:484/486 of 3ju8A
- active site: N147 (= N134), K170 (= K157), E245 (= E232), C279 (= C266), E377 (= E363), P455 (= P441)
- binding nicotinamide-adenine-dinucleotide: G144 (= G131), Y146 (≠ F133), N147 (= N134), L152 (= L139), K170 (= K157), S172 (= S159), F220 (= F207), T221 (= T208), G222 (= G209), S223 (≠ G210), T226 (≠ A213), E245 (= E232), M246 (≠ L233), G247 (= G234), C279 (= C266), E377 (= E363), F379 (= F365), F444 (= F430)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
34% identity, 95% coverage: 1:448/472 of query aligns to 23:476/494 of 4pz2B
- active site: N159 (= N134), K182 (= K157), E258 (= E232), C292 (= C266), E392 (= E363), D469 (≠ P441)
- binding nicotinamide-adenine-dinucleotide: I155 (= I130), I156 (≠ G131), P157 (= P132), W158 (≠ F133), N159 (= N134), M164 (≠ L139), K182 (= K157), A184 (≠ S159), E185 (= E160), G215 (= G190), G219 (= G193), F233 (= F207), T234 (= T208), G235 (= G209), S236 (≠ G210), V239 (≠ A213), E258 (= E232), L259 (= L233), C292 (= C266), E392 (= E363), F394 (= F365)
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)
32% identity, 95% coverage: 2:448/472 of query aligns to 33:483/501 of Q56YU0
- G152 (≠ A117) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A380) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
32% identity, 93% coverage: 1:437/472 of query aligns to 18:457/486 of 4pxlA
- active site: N154 (= N134), K177 (= K157), E253 (= E232), C287 (= C266), E384 (= E363)
- binding nicotinamide-adenine-dinucleotide: I150 (= I130), V151 (≠ G131), P152 (= P132), W153 (≠ F133), K177 (= K157), E180 (= E160), G210 (= G190), G214 (= G193), A215 (≠ E194), F228 (= F207), G230 (= G209), S231 (≠ G210), V234 (≠ A213), E253 (= E232), G255 (= G234), C287 (= C266), Q334 (≠ A315), K337 (≠ Q318), E384 (= E363), F386 (= F365)
Sites not aligning to the query:
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
34% identity, 92% coverage: 10:442/472 of query aligns to 27:463/489 of 6wsbA
- active site: N152 (= N134), E250 (= E232), C284 (= C266), E462 (≠ P441)
- binding nicotinamide-adenine-dinucleotide: I148 (= I130), G149 (= G131), A150 (≠ P132), W151 (≠ F133), N152 (= N134), K175 (= K157), E178 (= E160), G208 (= G190), G211 (= G193), A212 (≠ E194), F225 (= F207), T226 (= T208), G227 (= G209), G228 (= G210), T231 (≠ A213), V235 (≠ I217), E250 (= E232), L251 (= L233), G252 (= G234), C284 (= C266), E385 (= E363), F387 (= F365)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 93% coverage: 10:450/472 of query aligns to 25:470/489 of 4o6rA
- active site: N150 (= N134), K173 (= K157), E248 (= E232), C282 (= C266), E383 (= E363), E460 (≠ P441)
- binding adenosine monophosphate: I146 (= I130), V147 (≠ G131), K173 (= K157), G206 (= G190), G210 (= G193), Q211 (≠ E194), F224 (= F207), G226 (= G209), S227 (≠ G210), T230 (≠ A213), R233 (≠ A216)
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
34% identity, 93% coverage: 10:448/472 of query aligns to 32:471/484 of Q8NMB0
- N157 (= N134) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K157) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (≠ A175) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E232) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C266) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
34% identity, 93% coverage: 10:446/472 of query aligns to 22:461/476 of 4yweA
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
31% identity, 92% coverage: 10:442/472 of query aligns to 27:464/489 of 4cazA
- active site: N152 (= N134), K175 (= K157), E251 (= E232), C285 (= C266), E386 (= E363), E463 (≠ P441)
- 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 (= I130), G149 (= G131), W151 (≠ F133), N152 (= N134), K175 (= K157), E178 (= E160), G208 (= G190), G212 (= G193), F226 (= F207), T227 (= T208), G228 (= G209), G229 (= G210), T232 (≠ A213), V236 (≠ I217), E251 (= E232), L252 (= L233), C285 (= C266), E386 (= E363), F388 (= F365)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
31% identity, 92% coverage: 10:442/472 of query aligns to 27:464/489 of 2woxA
- active site: N152 (= N134), K175 (= K157), E251 (= E232), C285 (= C266), E386 (= E363), E463 (≠ P441)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I130), G149 (= G131), W151 (≠ F133), N152 (= N134), K175 (= K157), S177 (= S159), E178 (= E160), G208 (= G190), G212 (= G193), F226 (= F207), T227 (= T208), G228 (= G209), G229 (= G210), T232 (≠ A213), V236 (≠ I217), E251 (= E232), L252 (= L233), C285 (= C266), E386 (= E363), F388 (= F365)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
31% identity, 92% coverage: 10:442/472 of query aligns to 27:464/489 of 2wmeA
- active site: N152 (= N134), K175 (= K157), E251 (= E232), C285 (= C266), E386 (= E363), E463 (≠ P441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G131), W151 (≠ F133), K175 (= K157), S177 (= S159), E178 (= E160), G208 (= G190), G212 (= G193), F226 (= F207), G228 (= G209), G229 (= G210), T232 (≠ A213), V236 (≠ I217)
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)
31% identity, 92% coverage: 10:442/472 of query aligns to 28:465/490 of Q9HTJ1
- GAWN 150:153 (≠ GPFN 131:134) binding
- K162 (≠ H143) active site, Charge relay system
- KPSE 176:179 (= KPSE 157:160) binding
- G209 (= G190) binding
- GTST 230:233 (≠ GVQA 210:213) binding
- E252 (= E232) active site, Proton acceptor
- C286 (= C266) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E363) binding
- E464 (≠ P441) active site, Charge relay system
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
30% identity, 98% coverage: 10:472/472 of query aligns to 35:492/497 of 8skfA
- binding calcium ion: D100 (≠ E75), V187 (≠ K161)
- binding nicotinamide-adenine-dinucleotide: I156 (= I130), G157 (= G131), A158 (≠ P132), W159 (≠ F133), K183 (= K157), E186 (= E160), G216 (= G189), G220 (= G193), T235 (= T208), G236 (= G209), G237 (= G210), S240 (≠ A213), K243 (≠ A216), E259 (= E232), C293 (= C266), F396 (= F365)
Sites not aligning to the query:
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
30% identity, 98% coverage: 10:472/472 of query aligns to 26:483/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
30% identity, 98% coverage: 10:472/472 of query aligns to 26:483/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
30% identity, 98% coverage: 10:472/472 of query aligns to 26:483/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
30% identity, 98% coverage: 10:472/472 of query aligns to 26:483/488 of 8vqwC
- binding coenzyme a: I147 (= I130), W150 (≠ F133), K174 (= K157), S176 (= S159), E177 (= E160), G207 (= G189), G211 (= G193), F225 (= F207), G227 (= G209), G228 (= G210), S231 (≠ A213), H331 (≠ A315), F387 (= F365)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
30% identity, 98% coverage: 10:472/472 of query aligns to 26:483/488 of 8vj3A
Query Sequence
>CCNA_00618 CCNA_00618 succinylglutamic semialdehyde dehydrogenase
MSASRLISRDPYTGEAIADFAVNDARSIDAACHSARAAFAEWAMTPLAERRAIALRFAET
VRARREEIATLIARETGKPMWEALTEADSVAAKVAISIRAQDERAGERSEPMADATARLA
HRPHGVLAVIGPFNFPMHLANGHIVPALLAGNAVVFKPSEKTPACGQLMGELWRAAGLPD
HVLTIVIGGGEAGEALVRHEALDGVLFTGGVQAGRAIHRALADAPHKILALELGGNAPLV
VWDVADIEAAAHLIVQSAYVTAGQRCTCARRLILPEGARGDALLEALTMLMDRLVIGGPF
QSPAPFMGPVIDAHAAAQVLAAQDRMTADGGRPLRLAAVREARSALLSPGLIELTDAPLR
DEEIFGPLLQVRRAADFDAALALANATRFGLAAGLISDDEALYRRFWTSVRAGIVNWNRP
TTGASSAAPFGGVGGSGNHRPSAYYAADYSAYPVAGLESPSPVYRLPIGLNP
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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