SitesBLAST
Comparing Ac3H11_1480 Aldehyde dehydrogenase B (EC 1.2.1.22) 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)
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)
64% identity, 99% coverage: 4:484/486 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
64% identity, 99% coverage: 6:484/486 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E258), C288 (= C292), E385 (= E389), E462 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (= A185), S182 (≠ T186), A212 (= A216), G216 (= G220), G232 (= G236), S233 (= S237), I236 (= I240), C288 (= C292), K338 (= K342), E385 (= E389), F387 (= F391)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
58% identity, 99% coverage: 5:486/486 of query aligns to 1:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (= A216), K213 (≠ R217), F230 (= F234), T231 (= T235), G232 (= G236), S233 (= S237), V236 (≠ I240), W239 (≠ V243), G256 (= G260)
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
53% identity, 99% coverage: 4:486/486 of query aligns to 51:535/535 of P51649
- C93 (≠ A48) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G131) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P135) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P137) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R168) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C178) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAT 183:186) binding
- T233 (= T188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A192) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G220) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEIG 236:241) binding
- R334 (= R286) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N287) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C292) modified: Disulfide link with 342, In inhibited form
- C342 (= C294) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ H323) natural variant: N -> S
- P382 (= P333) to L: in SSADHD; 2% of activity
- V406 (= V357) to I: in dbSNP:rs143741652
- G409 (= G360) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S449) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G484) to R: in SSADHD; <1% of activity; dbSNP:rs72552284
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
53% identity, 99% coverage: 4:486/486 of query aligns to 1:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
53% identity, 99% coverage: 4:486/486 of query aligns to 1:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 97% coverage: 15:483/486 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E380 (= E389), E457 (= E466)
- binding glycerol: D15 (= D24), A16 (= A25), A17 (≠ D26), G19 (= G28)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (≠ A216), A208 (≠ R217), S211 (≠ G220), G227 (= G236), S228 (= S237), V231 (≠ I240), R329 (≠ A338), R330 (≠ S339), E380 (= E389), F382 (= F391)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 97% coverage: 15:483/486 of query aligns to 6:474/476 of 5x5tA
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 96% coverage: 15:479/486 of query aligns to 7:474/486 of 4pxlA
- active site: N154 (= N160), K177 (= K183), E253 (= E258), C287 (= C292), E384 (= E389), D461 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I150 (= I156), V151 (≠ T157), P152 (= P158), W153 (= W159), K177 (= K183), E180 (≠ T186), G210 (≠ A216), G214 (= G220), A215 (= A221), F228 (= F234), G230 (= G236), S231 (= S237), V234 (≠ I240), E253 (= E258), G255 (= G260), C287 (= C292), Q334 (≠ S339), K337 (= K342), E384 (= E389), F386 (= F391)
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)
38% identity, 97% coverage: 12:482/486 of query aligns to 16:492/505 of 4neaA
- active site: N166 (= N160), K189 (= K183), E264 (= E258), C298 (= C292), E399 (= E389), E476 (= E466)
- binding nicotinamide-adenine-dinucleotide: P164 (= P158), K189 (= K183), E192 (≠ T186), G222 (≠ A216), G226 (= G220), G242 (= G236), G243 (≠ S237), T246 (≠ I240), H249 (≠ V243), I250 (≠ L244), C298 (= C292), E399 (= E389), F401 (= F391)
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: 9:483/486 of query aligns to 15:493/501 of Q56YU0
- G152 (≠ I143) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A406) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 96% coverage: 13:479/486 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N160), E246 (= E258), C280 (= C292), E458 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I156), T145 (= T157), A146 (≠ P158), W147 (= W159), N148 (= N160), K171 (= K183), T173 (≠ A185), S174 (≠ T186), G204 (≠ A216), G208 (= G220), T223 (= T235), G224 (= G236), S225 (= S237), A228 (≠ I240), S231 (≠ V243), I232 (≠ L244), E246 (= E258), L247 (= L259), C280 (= C292), E381 (= E389), F383 (= F391), H447 (≠ F455)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 98% coverage: 4:479/486 of query aligns to 1:482/494 of 4pz2B
- active site: N159 (= N160), K182 (= K183), E258 (= E258), C292 (= C292), E392 (= E389), D469 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I155 (= I156), I156 (≠ T157), P157 (= P158), W158 (= W159), N159 (= N160), M164 (= M165), K182 (= K183), A184 (= A185), E185 (≠ T186), G215 (≠ A216), G219 (= G220), F233 (= F234), T234 (= T235), G235 (= G236), S236 (= S237), V239 (≠ I240), E258 (= E258), L259 (= L259), C292 (= C292), E392 (= E389), F394 (= F391)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 99% coverage: 1:479/486 of query aligns to 94:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K183), S310 (≠ D215), G311 (≠ A216), G315 (= G220), G331 (= G236), S332 (= S237), V335 (≠ I240)
- binding 4'-phosphopantetheine: K201 (≠ R109), F382 (≠ R286), N387 (≠ T291), C388 (= C292), N545 (≠ V447)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 99% coverage: 1:479/486 of query aligns to 9:492/498 of 4go2A
- active site: N170 (= N160), K193 (= K183), E269 (= E258), C303 (= C292), E400 (= E389), D479 (≠ E466)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I156), I167 (≠ T157), P168 (= P158), W169 (= W159), K193 (= K183), A195 (= A185), Q196 (≠ T186), S225 (≠ D215), G226 (≠ A216), G230 (= G220), Q231 (≠ A221), F244 (= F234), G246 (= G236), S247 (= S237), V250 (≠ I240), I254 (≠ L244), E269 (= E258), G271 (= G260), C303 (= C292), E400 (= E389), F402 (= F391)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 99% coverage: 1:479/486 of query aligns to 9:492/498 of 2o2rA
- active site: N170 (= N160), K193 (= K183), E269 (= E258), C303 (= C292), E400 (= E389), D479 (≠ E466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I156), I167 (≠ T157), W169 (= W159), K193 (= K183), A195 (= A185), Q196 (≠ T186), S225 (≠ D215), G226 (≠ A216), G230 (= G220), Q231 (≠ A221), F244 (= F234), S247 (= S237), V250 (≠ I240), I254 (≠ L244)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
38% identity, 99% coverage: 1:479/486 of query aligns to 413:896/902 of P28037
- IPW 571:573 (≠ TPW 157:159) binding
- KPAQ 597:600 (≠ KPAT 183:186) binding
- GSLVGQ 630:635 (≠ ARPIGA 216:221) binding
- GS 650:651 (= GS 236:237) binding
- E673 (= E258) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 258:259) binding
- C707 (= C292) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K342) binding
- ESF 804:806 (≠ EIF 389:391) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 95% coverage: 17:479/486 of query aligns to 26:491/503 of O14293
- S248 (= S237) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 97% coverage: 9:479/486 of query aligns to 4:485/505 of O24174
- N164 (= N160) 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 (≠ R168) 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.
7radA Crystal structure analysis of aldh1b1
37% identity, 98% coverage: 8:483/486 of query aligns to 7:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (≠ T157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (≠ T186), G218 (≠ A216), G222 (= G220), A223 (= A221), T237 (= T235), G238 (= G236), S239 (= S237), V242 (≠ I240), E261 (= E258), L262 (= L259), C295 (= C292), E392 (= E389), F394 (= F391)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ Y114), F163 (= F161), E285 (≠ A282), F289 (≠ R286), N450 (≠ V447), V452 (≠ S449)
Query Sequence
>Ac3H11_1480 Aldehyde dehydrogenase B (EC 1.2.1.22)
MHTLALQDPSLLKARCYIDGQWVDADNGATLAVNNPANGALIGTIPNAGAAQTQTAIAAA
DRAFGPWKDRTAEDRARILRRWFELMLQHQEDLALIMTSEQGKPLAEARGEIAYAASYIE
WFAEEARRIYGEVIPSPWLDKRIVVTREPVGVCAAITPWNFPAAMITRKVAPALAAGCTI
IVKPATQTPLSALAMAELAARAGVPAGVFSVITGDARPIGAELTASPVVRKLTFTGSTEI
GRVLAAQCAPTLKKMSLELGGNAPFIVFEDADLDAAVAGAMASKYRNTGQTCVCANRLLV
QDGVYDAFAEKLARTVAALKVGHGLEEGVEQGPLIDEASLTKVEALVADAKARGARVVTG
GRRHALGGTFYEPTILADITPDMRMAREEIFGPVAPLFRFHTEAEAIQMANDTEFGLAAY
FYSRDVGRVWRVSGALQYGMVGINAGVISTAVAPFGGVKQSGMGREGSVHGIEEYVDTKY
LCMGGV
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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