SitesBLAST
Comparing 5208068 Shew_0580 succinylglutamic semialdehyde dehydrogenase (RefSeq) 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)
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
60% identity, 99% coverage: 5:487/487 of query aligns to 7:488/488 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)
60% identity, 99% coverage: 5:487/487 of query aligns to 7:488/488 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)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
59% identity, 100% coverage: 1:485/487 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)
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)
32% identity, 94% coverage: 5:462/487 of query aligns to 14:472/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
32% identity, 93% coverage: 5:458/487 of query aligns to 13:466/481 of 3jz4A
- active site: N156 (= N146), K179 (= K169), E254 (= E244), C288 (= C278), E385 (= E376), E462 (≠ A454)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P144), W155 (≠ Y145), K179 (= K169), A181 (≠ S171), S182 (≠ E172), A212 (≠ V202), G216 (= G205), G232 (= G221), S233 (= S222), I236 (≠ T225), C288 (= C278), K338 (≠ G330), E385 (= E376), F387 (= F378)
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)
31% identity, 98% coverage: 5:483/487 of query aligns to 23:499/501 of Q56YU0
- G152 (≠ A129) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A393) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
29% identity, 83% coverage: 5:409/487 of query aligns to 6:414/494 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 (≠ E201), G205 (vs. gap), G209 (= G205), D210 (≠ K206), G225 (= G221), S226 (= S222), T229 (= T225)
Sites not aligning to the query:
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
31% identity, 94% coverage: 5:461/487 of query aligns to 14:476/494 of 4pz2B
- active site: N159 (= N146), K182 (= K169), E258 (= E244), C292 (= C278), E392 (= E376), D469 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F142), I156 (≠ G143), P157 (= P144), W158 (≠ Y145), N159 (= N146), M164 (≠ L151), K182 (= K169), A184 (≠ S171), E185 (= E172), G215 (≠ V202), G219 (= G205), F233 (= F219), T234 (= T220), G235 (= G221), S236 (= S222), V239 (≠ T225), E258 (= E244), L259 (≠ M245), C292 (= C278), E392 (= E376), F394 (= F378)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
34% identity, 83% coverage: 5:408/487 of query aligns to 8:413/477 of 2opxA
- active site: N151 (= N146), K174 (= K169), E249 (= E244), C283 (= C278), E381 (= E376)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ A101), F152 (= F147), N284 (≠ T279), F312 (≠ V308), G313 (= G309), R318 (≠ Q314), D320 (≠ Q316), I321 (≠ P317), A322 (≠ F318), Y362 (≠ V359)
Sites not aligning to the query:
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 83% coverage: 5:408/487 of query aligns to 10:415/479 of P25553
- L150 (≠ G143) binding
- R161 (≠ G154) binding
- KPSE 176:179 (= KPSE 169:172) binding
- F180 (≠ L173) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ K206) binding
- S230 (= S222) binding
- E251 (= E244) binding
- N286 (≠ T279) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ G330) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 443 binding
- 449 binding
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
34% identity, 83% coverage: 5:408/487 of query aligns to 8:413/477 of 2impA
- active site: N151 (= N146), K174 (= K169), E249 (= E244), C283 (= C278), E381 (= E376)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ F142), L148 (≠ G143), P149 (= P144), W150 (≠ Y145), K174 (= K169), E177 (= E172), F178 (≠ L173), G207 (≠ V202), G211 (= G205), Q212 (≠ K206), S228 (= S222), A231 (≠ T225), K234 (≠ I228), R334 (≠ G330)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
34% identity, 83% coverage: 5:408/487 of query aligns to 8:413/477 of 2iluA
- active site: N151 (= N146), K174 (= K169), E249 (= E244), C283 (= C278), E381 (= E376)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ F142), L148 (≠ G143), P149 (= P144), W150 (≠ Y145), K174 (= K169), S176 (= S171), E177 (= E172), R206 (≠ E201), G207 (≠ V202), G211 (= G205), Q212 (≠ K206), S228 (= S222), A231 (≠ T225), K234 (≠ I228), I235 (≠ L229), N328 (≠ S324), R334 (≠ G330), F383 (= F378)
Sites not aligning to the query:
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)
33% identity, 94% coverage: 4:459/487 of query aligns to 13:469/484 of Q8NMB0
- N157 (= N146) 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 (= K169) 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 (≠ K187) 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 (= E244) 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 (= C278) 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.
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
33% identity, 91% coverage: 15:455/487 of query aligns to 29:477/508 of 6rttA
- active site: N161 (= N146), E262 (= E244), C296 (= C278), E476 (≠ A454)
- binding pyridine-2-carboxylic acid: A159 (≠ P144), F162 (= F147), V166 (≠ L151), W169 (≠ G154), G240 (= G221), S241 (= S222), R295 (= R277), C296 (= C278), T297 (= T279), E396 (= E376), F398 (= F378), P421 (≠ R401), K469 (≠ G447), E470 (≠ A448)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
33% identity, 91% coverage: 15:455/487 of query aligns to 30:478/509 of 6rtsA
- active site: N162 (= N146), E263 (= E244), C297 (= C278), E477 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I158 (≠ F142), S159 (≠ G143), A160 (≠ P144), F161 (≠ Y145), N162 (= N146), K185 (= K169), S187 (= S171), E188 (= E172), A222 (≠ V202), G225 (= G205), T240 (= T220), G241 (= G221), S242 (= S222), M245 (≠ T225), E263 (= E244), L264 (≠ M245), C297 (= C278), E397 (= E376), F399 (= F378)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
30% identity, 88% coverage: 3:432/487 of query aligns to 7:436/454 of 3ty7B
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)
29% identity, 95% coverage: 1:462/487 of query aligns to 9:476/487 of Q9H2A2
- R109 (≠ L108) 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.
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
29% identity, 92% coverage: 2:449/487 of query aligns to 5:453/484 of 1t90A
- active site: N151 (= N146), K174 (= K169), L248 (= L243), C282 (= C278), E380 (= E376)
- binding nicotinamide-adenine-dinucleotide: I147 (≠ F142), A148 (≠ G143), P149 (= P144), F150 (≠ Y145), N151 (= N146), W159 (≠ G154), K174 (= K169), E177 (= E172), R178 (≠ L173), H207 (≠ V202), V225 (≠ T220), G226 (= G221), S227 (= S222), V230 (≠ T225), L248 (= L243), T249 (≠ E244), C282 (= C278), E380 (= E376), F382 (= F378)
Sites not aligning to the query:
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)
29% identity, 92% coverage: 2:449/487 of query aligns to 7:455/487 of P42412
- C36 (≠ W30) 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 (≠ A101) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ G143) binding
- F152 (≠ Y145) binding
- C160 (≠ N153) 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 (= K169) binding
- E179 (= E172) binding
- R180 (≠ L173) binding
- S229 (= S222) binding
- T251 (≠ E244) binding
- R283 (= R277) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ A281) 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 (≠ V347) 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 (= E376) binding
- C413 (≠ G407) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
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: 5:453/487 of query aligns to 10:463/490 of Q9HTJ1
- GAWN 150:153 (≠ GPYN 143:146) binding
- K162 (≠ H155) active site, Charge relay system
- KPSE 176:179 (= KPSE 169:172) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ SSRT 222:225) binding
- E252 (= E244) active site, Proton acceptor
- C286 (= C278) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E376) binding
Sites not aligning to the query:
- 464 active site, Charge relay system
Query Sequence
>5208068 Shew_0580 succinylglutamic semialdehyde dehydrogenase (RefSeq)
MMSQFINGQWVAGLGHDVVSKNPANQEVIWESKTATPEQVNAAVEAARAAQFDWFMLGFD
ARLAIVEAYRDQLEAHKGDIAEVIAQETGKPQWETATEAGAMIGKIGLSVAAYHKRTGTS
ENDTPAGRAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPKTAEL
MLKLWEKAGLPAGVINLVQGEVETGKALASHPQIDGLFFTGSSRTGHILHQQYAGHPGKI
LALEMGGNNPLIIKGVKDTLAAVHDIIQSAYISSGQRCTCARRLYVEKGAEGDALLAKLA
EAVKQIKVGPWNAQPQPFMGSMISEAAAKGMVEAQRNLINLGGTPLVELKHLEAGTGLVS
PGLIDVTQVIELPDEEYFGPLLQVVRYTDFDEAIKLANDTRYGLSAGILADSREDYDYFL
ARIRAGIVNWNKQITGASGSAPFGGVGASGNHRASAFYAADYCAYPVASVEADALAMPAS
LSPGLTL
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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