SitesBLAST
Comparing BPHYT_RS10925 BPHYT_RS10925 aldehyde 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
86% identity, 99% coverage: 5:480/481 of query aligns to 1:476/476 of 5x5uA
- active site: N151 (= N155), K174 (= K178), E249 (= E253), C283 (= C287), E380 (= E384), E457 (= E461)
- binding glycerol: D15 (= D19), A16 (= A20), A17 (= A21), G19 (= G23)
- binding nicotinamide-adenine-dinucleotide: P149 (= P153), P207 (= P211), A208 (= A212), S211 (= S215), G227 (= G231), S228 (= S232), V231 (= V235), R329 (= R333), R330 (= R334), E380 (= E384), F382 (= F386)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
86% identity, 99% coverage: 5:480/481 of query aligns to 1:476/476 of 5x5tA
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)
42% identity, 97% coverage: 12:478/481 of query aligns to 14:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
42% identity, 97% coverage: 12:478/481 of query aligns to 13:479/481 of 3jz4A
- active site: N156 (= N155), K179 (= K178), E254 (= E253), C288 (= C287), E385 (= E384), E462 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P153), W155 (= W154), K179 (= K178), A181 (≠ P180), S182 (≠ E181), A212 (≠ P211), G216 (≠ S215), G232 (= G231), S233 (= S232), I236 (≠ V235), C288 (= C287), K338 (≠ A337), E385 (= E384), F387 (= F386)
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)
42% identity, 98% coverage: 9:477/481 of query aligns to 61:531/535 of P51649
- C93 (≠ A43) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G126) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P130) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ R132) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R163) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C173) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KAPE 178:181) binding
- T233 (= T183) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ P187) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ G205) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S215) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 231:236) binding
- R334 (= R281) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N282) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C287) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S289) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D318) natural variant: N -> S
- P382 (= P328) to L: in SSADHD; 2% of activity
- V406 (= V352) to I: in dbSNP:rs143741652
- G409 (= G355) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ P444) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
41% identity, 98% coverage: 9:477/481 of query aligns to 11:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
41% identity, 98% coverage: 9:477/481 of query aligns to 11:481/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
40% identity, 98% coverage: 10:478/481 of query aligns to 11:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F151), T153 (= T152), P154 (= P153), K179 (= K178), A212 (≠ P211), K213 (≠ A212), F230 (= F229), T231 (= T230), G232 (= G231), S233 (= S232), V236 (= V235), W239 (≠ Q238), G256 (= G255)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
35% identity, 98% coverage: 8:478/481 of query aligns to 2:475/494 of 5izdA
- active site: N149 (= N155), K172 (= K178), E247 (= E253), C281 (= C287), E381 (= E384), E458 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ F151), T146 (= T152), W148 (= W154), K172 (= K178), P173 (≠ A179), S174 (≠ P180), S175 (≠ E181), R204 (≠ D210), G205 (≠ P211), G209 (≠ S215), D210 (≠ S216), G225 (= G231), S226 (= S232), T229 (≠ V235)
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)
35% identity, 98% coverage: 6:478/481 of query aligns to 4:481/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 152:155) binding
- K162 (= K164) active site, Charge relay system
- KPSE 176:179 (≠ KAPE 178:181) binding
- G209 (≠ P211) binding
- GTST 230:233 (≠ STPV 232:235) binding
- E252 (= E253) active site, Proton acceptor
- C286 (= C287) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E384) binding
- E464 (= E461) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
35% identity, 98% coverage: 6:478/481 of query aligns to 3:480/489 of 4cazA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E384), E463 (= E461)
- 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 (≠ F151), G149 (≠ T152), W151 (= W154), N152 (= N155), K175 (= K178), E178 (= E181), G208 (≠ P211), G212 (≠ S215), F226 (= F229), T227 (= T230), G228 (= G231), G229 (≠ S232), T232 (≠ V235), V236 (vs. gap), E251 (= E253), L252 (= L254), C285 (= C287), E386 (= E384), F388 (= F386)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
35% identity, 98% coverage: 6:478/481 of query aligns to 3:480/489 of 2woxA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E384), E463 (= E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F151), G149 (≠ T152), W151 (= W154), N152 (= N155), K175 (= K178), S177 (≠ P180), E178 (= E181), G208 (≠ P211), G212 (≠ S215), F226 (= F229), T227 (= T230), G228 (= G231), G229 (≠ S232), T232 (≠ V235), V236 (vs. gap), E251 (= E253), L252 (= L254), C285 (= C287), E386 (= E384), F388 (= F386)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
35% identity, 98% coverage: 6:478/481 of query aligns to 3:480/489 of 2wmeA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E384), E463 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T152), W151 (= W154), K175 (= K178), S177 (≠ P180), E178 (= E181), G208 (≠ P211), G212 (≠ S215), F226 (= F229), G228 (= G231), G229 (≠ S232), T232 (≠ V235), V236 (vs. gap)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
36% identity, 99% coverage: 4:478/481 of query aligns to 9:488/497 of 8skfA
- binding calcium ion: T33 (≠ V28), I34 (= I29), D100 (≠ E95), V187 (≠ E182)
- binding nicotinamide-adenine-dinucleotide: I156 (≠ F151), G157 (≠ T152), A158 (≠ P153), W159 (= W154), K183 (= K178), E186 (= E181), G216 (≠ P211), G220 (≠ S215), T235 (= T230), G236 (= G231), G237 (≠ S232), S240 (≠ V235), K243 (≠ Q238), E259 (= E253), C293 (= C287), F396 (= F386)
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)
34% identity, 99% coverage: 1:476/481 of query aligns to 10:491/505 of 4neaA
- active site: N166 (= N155), K189 (= K178), E264 (= E253), C298 (= C287), E399 (= E384), E476 (= E461)
- binding nicotinamide-adenine-dinucleotide: P164 (= P153), K189 (= K178), E192 (= E181), G222 (≠ P211), G226 (≠ S215), G242 (= G231), G243 (≠ S232), T246 (≠ V235), H249 (≠ Q238), I250 (≠ L239), C298 (= C287), E399 (= E384), F401 (= F386)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
36% identity, 98% coverage: 8:478/481 of query aligns to 4:479/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
36% identity, 98% coverage: 8:478/481 of query aligns to 4:479/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
36% identity, 98% coverage: 8:478/481 of query aligns to 4:479/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
36% identity, 98% coverage: 8:478/481 of query aligns to 4:479/488 of 8vqwC
- binding coenzyme a: I147 (≠ F151), W150 (= W154), K174 (= K178), S176 (≠ P180), E177 (= E181), G207 (≠ P211), G211 (≠ S215), F225 (= F229), G227 (= G231), G228 (≠ S232), S231 (≠ V235), H331 (≠ R334), F387 (= F386)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
36% identity, 98% coverage: 8:478/481 of query aligns to 4:479/488 of 8vj3A
Query Sequence
>BPHYT_RS10925 BPHYT_RS10925 aldehyde dehydrogenase
MATSSYTDTRLLINGEWCDAASGKTLDVINPATGKAIGKVAHAGIADLDRALAAAQRGFE
AWRKVPANERATTMRKAAALVRERASDIGRLMTLEQGKPFAEARIEVLAAADIIEWFADE
GRRVYGRIVPSRNLAAQQLVLKEPIGPVAAFTPWNFPVNQVVRKLSAALACGCSFLVKAP
EETPASPAALLQAFVEAGVPAGTVGLVFGDPAEISSYLIPHPVIRKVTFTGSTPVGKQLA
ALAGSHMKRATMELGGHAPVIVAEDADVALAVKAAGGAKFRNAGQVCISPTRFLVHNSIR
EEFAAALVKHAEGLKLGDGLAEGTTLGPLANARRLTAMSKVLDDARKTGAKVETGGERVG
SEGNFFAPTVLTNVSLESDVFNNEPFGPIAAIRGFDKLEEAIAEANRLPFGLAGYAFTKS
FTNVHLLSQQLEVGMLWINQPATPSPEMPFGGVKDSGYGSEGGPEAMEGYLVTKAVSVMS
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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