SitesBLAST
Comparing GFF2918 FitnessBrowser__Phaeo:GFF2918 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)
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, 98% coverage: 12:491/491 of query aligns to 3:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
63% identity, 98% coverage: 12:491/491 of query aligns to 2:481/481 of 3jz4A
- active site: N156 (= N165), K179 (≠ R188), E254 (= E264), C288 (= C298), E385 (= E395), E462 (= E472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P163), W155 (= W164), K179 (≠ R188), A181 (= A190), S182 (≠ E191), A212 (= A222), G216 (= G226), G232 (= G242), S233 (= S243), I236 (≠ V246), C288 (= C298), K338 (= K348), E385 (= E395), F387 (= F397)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
61% identity, 97% coverage: 12:489/491 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I161), T153 (= T162), P154 (= P163), K179 (≠ R188), A212 (= A222), K213 (≠ S223), F230 (= F240), T231 (= T241), G232 (= G242), S233 (= S243), V236 (= V246), W239 (≠ I249), G256 (= G266)
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)
55% identity, 96% coverage: 16:488/491 of query aligns to 57:531/535 of P51649
- C93 (≠ V53) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G136) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P140) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H142) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R173) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C183) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ RPAE 188:191) binding
- T233 (= T193) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A197) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N215) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G226) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 242:247) binding
- R334 (= R292) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N293) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C298) modified: Disulfide link with 342, In inhibited form
- C342 (= C300) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D329) natural variant: N -> S
- P382 (= P339) to L: in SSADHD; 2% of activity
- V406 (= V363) to I: in dbSNP:rs143741652
- G409 (= G366) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S455) 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)
54% identity, 96% coverage: 16:488/491 of query aligns to 7:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 96% coverage: 16:488/491 of query aligns to 7:481/485 of 2w8qA
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 95% coverage: 21:488/491 of query aligns to 7:477/486 of 4pxlA
- active site: N154 (= N165), K177 (≠ R188), E253 (= E264), C287 (= C298), E384 (= E395), D461 (≠ E472)
- binding nicotinamide-adenine-dinucleotide: I150 (= I161), V151 (≠ T162), P152 (= P163), W153 (= W164), K177 (≠ R188), E180 (= E191), G210 (≠ N221), G214 (= G226), A215 (≠ K227), F228 (= F240), G230 (= G242), S231 (= S243), V234 (= V246), E253 (= E264), G255 (= G266), C287 (= C298), Q334 (≠ A345), K337 (= K348), E384 (= E395), F386 (= F397)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 97% coverage: 11:487/491 of query aligns to 1:484/494 of 4pz2B
- active site: N159 (= N165), K182 (≠ R188), E258 (= E264), C292 (= C298), E392 (= E395), D469 (≠ E472)
- binding nicotinamide-adenine-dinucleotide: I155 (= I161), I156 (≠ T162), P157 (= P163), W158 (= W164), N159 (= N165), M164 (= M170), K182 (≠ R188), A184 (= A190), E185 (= E191), G215 (≠ N221), G219 (= G226), F233 (= F240), T234 (= T241), G235 (= G242), S236 (= S243), V239 (= V246), E258 (= E264), L259 (= L265), C292 (= C298), E392 (= E395), F394 (= F397)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 95% coverage: 21:485/491 of query aligns to 3:471/477 of 6j76A
- active site: N148 (= N165), E246 (= E264), C280 (= C298), E458 (= E472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I161), T145 (= T162), A146 (≠ P163), W147 (= W164), N148 (= N165), K171 (≠ R188), T173 (≠ A190), S174 (≠ E191), G204 (≠ N221), G208 (= G226), T223 (= T241), G224 (= G242), S225 (= S243), A228 (≠ V246), S231 (≠ I249), I232 (≠ L250), E246 (= E264), L247 (= L265), C280 (= C298), E381 (= E395), F383 (= F397), H447 (≠ F461)
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)
38% identity, 96% coverage: 19:487/491 of query aligns to 6:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 162:165) binding
- K162 (= K174) active site, Charge relay system
- KPSE 176:179 (≠ RPAE 188:191) binding
- G209 (≠ A222) binding
- GTST 230:233 (≠ STEV 243:246) binding
- E252 (= E264) active site, Proton acceptor
- C286 (= C298) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E395) binding
- E464 (= E472) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
38% identity, 96% coverage: 19:487/491 of query aligns to 5:478/489 of 4cazA
- active site: N152 (= N165), K175 (≠ R188), E251 (= E264), C285 (= C298), E386 (= E395), E463 (= E472)
- 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 (= I161), G149 (≠ T162), W151 (= W164), N152 (= N165), K175 (≠ R188), E178 (= E191), G208 (≠ A222), G212 (= G226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (≠ V246), V236 (≠ L250), E251 (= E264), L252 (= L265), C285 (= C298), E386 (= E395), F388 (= F397)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
38% identity, 96% coverage: 19:487/491 of query aligns to 5:478/489 of 2woxA
- active site: N152 (= N165), K175 (≠ R188), E251 (= E264), C285 (= C298), E386 (= E395), E463 (= E472)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I161), G149 (≠ T162), W151 (= W164), N152 (= N165), K175 (≠ R188), S177 (≠ A190), E178 (= E191), G208 (≠ A222), G212 (= G226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (≠ V246), V236 (≠ L250), E251 (= E264), L252 (= L265), C285 (= C298), E386 (= E395), F388 (= F397)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
38% identity, 96% coverage: 19:487/491 of query aligns to 5:478/489 of 2wmeA
- active site: N152 (= N165), K175 (≠ R188), E251 (= E264), C285 (= C298), E386 (= E395), E463 (= E472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T162), W151 (= W164), K175 (≠ R188), S177 (≠ A190), E178 (= E191), G208 (≠ A222), G212 (= G226), F226 (= F240), G228 (= G242), G229 (≠ S243), T232 (≠ V246), V236 (≠ L250)
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, 97% coverage: 15:491/491 of query aligns to 15:495/501 of Q56YU0
- G152 (≠ I148) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V412) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
35% identity, 96% coverage: 19:491/491 of query aligns to 10:487/494 of P49189
- C116 (≠ F123) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
35% identity, 96% coverage: 19:491/491 of query aligns to 9:486/493 of 6vr6D
- active site: N156 (= N165), E253 (= E264), C287 (= C298), E467 (= E472)
- binding nicotinamide-adenine-dinucleotide: I152 (= I161), G153 (≠ T162), W155 (= W164), K179 (≠ R188), A212 (≠ N221), G215 (= G226), Q216 (≠ K227), F229 (= F240), G231 (= G242), S232 (= S243), T235 (≠ V246), I239 (≠ L250)
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)
36% identity, 95% coverage: 23:490/491 of query aligns to 8:476/477 of 2impA
- active site: N151 (= N165), K174 (≠ R188), E249 (= E264), C283 (= C298), E381 (= E395), A458 (≠ E472)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I161), L148 (≠ T162), P149 (= P163), W150 (= W164), K174 (≠ R188), E177 (= E191), F178 (≠ L192), G207 (≠ N221), G211 (= G226), Q212 (≠ K227), S228 (= S243), A231 (≠ V246), K234 (≠ I249), R334 (≠ K348)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
36% identity, 95% coverage: 23:490/491 of query aligns to 8:476/477 of 2iluA
- active site: N151 (= N165), K174 (≠ R188), E249 (= E264), C283 (= C298), E381 (= E395), A458 (≠ E472)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I161), L148 (≠ T162), P149 (= P163), W150 (= W164), K174 (≠ R188), S176 (≠ A190), E177 (= E191), R206 (≠ S220), G207 (≠ N221), G211 (= G226), Q212 (≠ K227), S228 (= S243), A231 (≠ V246), K234 (≠ I249), I235 (≠ L250), N328 (= N342), R334 (≠ K348), F383 (= F397)
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)
36% identity, 95% coverage: 23:490/491 of query aligns to 10:478/479 of P25553
- L150 (≠ T162) binding
- R161 (= R173) binding
- KPSE 176:179 (≠ RPAE 188:191) binding
- F180 (≠ L192) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ K227) binding
- S230 (= S243) binding
- E251 (= E264) binding
- N286 (≠ V299) 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 (≠ K348) binding
- E443 (≠ S455) binding
- H449 (≠ F461) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
36% identity, 95% coverage: 23:490/491 of query aligns to 8:476/477 of 2opxA
- active site: N151 (= N165), K174 (≠ R188), E249 (= E264), C283 (= C298), E381 (= E395), A458 (≠ E472)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y119), F152 (= F166), N284 (≠ V299), F312 (≠ V327), G313 (= G328), R318 (≠ E333), D320 (vs. gap), I321 (≠ T335), A322 (≠ Q336), Y362 (≠ F376), F440 (≠ I454), F440 (≠ I454), E441 (≠ S455)
Query Sequence
>GFF2918 FitnessBrowser__Phaeo:GFF2918
MLDATTDLKSLLTDPSLLEPRAYIGGAFVDGADGTFAVKNPARGDVIANVADVSRSQVAG
AIAQAEVAQKDWAKWTGKERANVLRKWFDLMMENQEDLAVILTAEMGKPLAESRGEIGYG
ASFIEFFAEEAKRIYGETIPGHQRDKRITVLKQPIGVAASITPWNFPNAMITRKAGPALA
AGCAFVARPAELTPLSATALAVLADRAGIPAGVFNVVTSSNASETGKEFCENNAVRKLTF
TGSTEVGRILMRQAADTVMKCSMELGGNAPFIVFDDADLDAAVEGAIMCKFRNNGQTCVC
ANRIYVQAGVYDAFAAKLKEAVAKMTVGDGLAEGTQFGPLINEKAVEKVQAHIADAKEKG
AEVILGGNPSELGGTFFEPTIITGATQDMVFSQDETFGPMAPLFKFETEDDVIEMANDTI
FGLASYFYAKDLSRVYKVAEALEYGIVGVNTGIISTELAPFGGVKQSGLGREGSHHGIED
YLEMKYICMSV
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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