SitesBLAST
Comparing HSERO_RS05645 FitnessBrowser__HerbieS:HSERO_RS05645 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)
53% identity, 99% coverage: 4:491/493 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
53% identity, 99% coverage: 6:491/493 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E261), C288 (= C295), E385 (= E396), E462 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (= A185), S182 (≠ E186), A212 (≠ T219), G216 (≠ V223), G232 (= G239), S233 (= S240), I236 (≠ V243), C288 (= C295), K338 (= K345), E385 (= E396), F387 (= F398)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
52% identity, 99% coverage: 6:493/493 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ R218), K213 (≠ T219), F230 (= F237), T231 (= T238), G232 (= G239), S233 (= S240), V236 (= V243), W239 (≠ H246), G256 (= G263)
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)
51% identity, 98% coverage: 11:493/493 of query aligns to 58:535/535 of P51649
- C93 (≠ G48) 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 (= KPAE 183:186) binding
- T233 (= T188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ S192) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ V223) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTAVG 239:244) binding
- R334 (= R289) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N290) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C295) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S297) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P326) natural variant: N -> S
- P382 (= P336) to L: in SSADHD; 2% of activity
- V406 (= V360) to I: in dbSNP:rs143741652
- G409 (= G363) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A456) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G491) 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)
51% identity, 98% coverage: 11:493/493 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
51% identity, 98% coverage: 11:493/493 of query aligns to 8:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 95% coverage: 18:486/493 of query aligns to 6:471/477 of 6j76A
- active site: N148 (= N160), E246 (= E261), C280 (= C295), E458 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I156), T145 (= T157), A146 (≠ P158), W147 (= W159), N148 (= N160), K171 (= K183), T173 (≠ A185), S174 (≠ E186), G204 (vs. gap), G208 (≠ T219), T223 (= T238), G224 (= G239), S225 (= S240), A228 (≠ V243), S231 (≠ H246), I232 (≠ L247), E246 (= E261), L247 (= L262), C280 (= C295), E381 (= E396), F383 (= F398), H447 (≠ F462)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 96% coverage: 17:489/493 of query aligns to 8:473/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E380 (= E396), E457 (= E473)
- binding glycerol: D15 (≠ G24), A16 (= A25), A17 (= A26), G19 (= G28)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (≠ T219), A208 (≠ P220), S211 (≠ V223), G227 (= G239), S228 (= S240), V231 (= V243), R329 (= R341), R330 (≠ A342), E380 (= E396), F382 (= F398)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 96% coverage: 17:489/493 of query aligns to 8:473/476 of 5x5tA
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 95% coverage: 22:488/493 of query aligns to 16:473/477 of 2opxA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E381 (= E396), A458 (≠ E473)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y114), F152 (= F161), N284 (≠ V296), F312 (≠ V324), G313 (= G325), R318 (≠ D329), D320 (≠ A331), I321 (≠ S332), A322 (≠ Q333), Y362 (= Y377), F440 (≠ L455), F440 (≠ L455), E441 (≠ A456)
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)
38% identity, 95% coverage: 22:488/493 of query aligns to 18:475/479 of P25553
- L150 (≠ T157) binding
- R161 (= R168) binding
- KPSE 176:179 (≠ KPAE 183:186) binding
- F180 (≠ D187) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E221) binding
- S230 (= S240) binding
- E251 (= E261) binding
- N286 (≠ V296) 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 (≠ K345) binding
- E443 (≠ A456) binding
- H449 (≠ F462) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
38% identity, 95% coverage: 22:488/493 of query aligns to 16:473/477 of 2impA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E381 (= E396), A458 (≠ E473)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), E177 (= E186), F178 (≠ D187), G207 (≠ R216), G211 (≠ P220), Q212 (≠ E221), S228 (= S240), A231 (≠ V243), K234 (≠ H246), R334 (≠ K345)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
38% identity, 95% coverage: 22:488/493 of query aligns to 16:473/477 of 2iluA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E381 (= E396), A458 (≠ E473)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), S176 (≠ A185), E177 (= E186), R206 (≠ S215), G207 (≠ R216), G211 (≠ P220), Q212 (≠ E221), S228 (= S240), A231 (≠ V243), K234 (≠ H246), I235 (≠ L247), N328 (= N339), R334 (≠ K345), F383 (= F398)
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)
37% identity, 96% coverage: 17:488/493 of query aligns to 23:491/501 of Q56YU0
- G152 (≠ M143) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V413) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 94% coverage: 25:488/493 of query aligns to 15:475/489 of 4o6rA
- active site: N150 (= N160), K173 (= K183), E248 (= E261), C282 (= C295), E383 (= E396), E460 (= E473)
- binding adenosine monophosphate: I146 (= I156), V147 (≠ T157), K173 (= K183), G206 (vs. gap), G210 (≠ R216), Q211 (≠ E217), F224 (= F237), G226 (= G239), S227 (= S240), T230 (≠ V243), R233 (≠ H246)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 96% coverage: 17:488/493 of query aligns to 14:484/494 of 4pz2B
- active site: N159 (= N160), K182 (= K183), E258 (= E261), C292 (= C295), E392 (= E396), D469 (≠ E473)
- binding nicotinamide-adenine-dinucleotide: I155 (= I156), I156 (≠ T157), P157 (= P158), W158 (= W159), N159 (= N160), M164 (= M165), K182 (= K183), A184 (= A185), E185 (= E186), G215 (≠ T219), G219 (≠ V223), F233 (= F237), T234 (= T238), G235 (= G239), S236 (= S240), V239 (= V243), E258 (= E261), L259 (= L262), C292 (= C295), E392 (= E396), F394 (= F398)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
41% identity, 94% coverage: 25:488/493 of query aligns to 13:470/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
40% identity, 94% coverage: 25:488/493 of query aligns to 13:470/474 of 1wndA
- active site: N149 (= N160), K172 (= K183), E246 (= E261), C280 (= C295), E378 (= E396), D455 (≠ E473)
- binding calcium ion: G249 (= G264), K250 (≠ N265), A251 (= A266), G405 (= G423), L406 (= L424), A407 (= A425), Y427 (≠ S445)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
40% identity, 94% coverage: 25:488/493 of query aligns to 13:470/474 of 1wnbB
- active site: N149 (= N160), K172 (= K183), E246 (= E261), C280 (= C295), E378 (= E396), D455 (≠ E473)
- binding betaine aldehyde: D279 (≠ T294), F436 (≠ A454), L438 (≠ A456)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I156), A146 (≠ T157), W148 (= W159), K172 (= K183), G204 (≠ T219), G208 (≠ V223), D209 (= D224), T223 (= T238), G224 (= G239), S225 (= S240), T228 (≠ V243), H231 (= H246), G248 (= G263), E378 (= E396)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
40% identity, 94% coverage: 25:488/493 of query aligns to 13:470/474 of 1wnbA
- active site: N149 (= N160), K172 (= K183), E246 (= E261), C280 (= C295), E378 (= E396), D455 (≠ E473)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I156), A146 (≠ T157), W148 (= W159), K172 (= K183), G204 (≠ T219), G208 (≠ V223), D209 (= D224), G224 (= G239), S225 (= S240), T228 (≠ V243), H231 (= H246), G248 (= G263), F380 (= F398)
Query Sequence
>HSERO_RS05645 FitnessBrowser__HerbieS:HSERO_RS05645
MTSLTLQRQDLMPGAQLIGADWRGAADGRQLDVSDPATGQVFASVPDGGAADARAAVEAA
VAAFAAWRATPAKQRAGIIKRWNDLLLAHQDDLGRLISREQGKPLAEAKGEVAYAASYVE
WFGEEATRANGDIIPAPVTGRRMMALKEPVGVVAAITPWNFPAAMIARKIAPALAAGCTV
VCKPAEDTPLTSLALVRLAQEAGVPVGVINIVTASRERTPEVVDVWLADGRVRKISFTGS
TAVGKHLARHSADTLKKLSLELGGNAPFIVFDDADVDAAIDGVMAAKFRNGGQTCVSPNR
IYVQEKVYDAFVDKLGARVAALKVGPATDPASQIGPMINARAIAKIDQHVRDAIARGARV
ITGGKRLQGPGFGSDNYYAPTVLADVTGAMQCSCEETFGPVAPITRFATEDEVIAAANAT
PFGLAAYFYSTDVRRIHRVTDALESGIVGVNEGALAAEAAPFGGVKESGYGREGSVHGLD
DYLHTKYVCQGQL
Or try a new SitesBLAST search
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