SitesBLAST
Comparing WP_085124768.1 NCBI__GCF_900177295.1:WP_085124768.1 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)
53% identity, 95% coverage: 24:500/504 of query aligns to 3:479/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
53% identity, 95% coverage: 24:500/504 of query aligns to 2:478/481 of 3jz4A
- active site: N156 (= N178), K179 (≠ H201), E254 (= E276), C288 (= C310), E385 (= E407), E462 (= E484)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P176), W155 (= W177), K179 (≠ H201), A181 (≠ S203), S182 (= S204), A212 (= A234), G216 (≠ V238), G232 (= G254), S233 (= S255), I236 (= I258), C288 (= C310), K338 (= K360), E385 (= E407), F387 (= F409)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
50% identity, 94% coverage: 24:499/504 of query aligns to 2:477/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ V174), T153 (= T175), P154 (= P176), K179 (≠ H201), A212 (= A234), K213 (≠ A235), F230 (= F252), T231 (≠ N253), G232 (= G254), S233 (= S255), V236 (≠ I258), W239 (≠ L261), G256 (= G278)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
47% identity, 97% coverage: 12:500/504 of query aligns to 8:496/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (≠ V174), A171 (≠ T175), P172 (= P176), W173 (= W177), K197 (≠ H201), A230 (= A234), F248 (= F252), G250 (= G254), S251 (= S255), V254 (≠ I258), M257 (≠ L261), L273 (= L277), C306 (= C310), K356 (= K360), E403 (= E407), F405 (= F409)
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)
49% identity, 94% coverage: 29:500/504 of query aligns to 58:531/535 of P51649
- C93 (≠ L66) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (≠ A149) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P153) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H155) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R186) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C196) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ HPSS 201:204) binding NAD(+)
- T233 (= T206) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A210) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N228) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ V238) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEIG 254:259) binding NAD(+)
- R334 (≠ A304) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ T305) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C310) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A312) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P341) natural variant: N -> S
- P382 (= P351) to L: in SSADHD; 2% of activity
- V406 (≠ L375) to I: in dbSNP:rs143741652
- G409 (= G378) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ T467) binding substrate; 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)
49% identity, 94% coverage: 29:500/504 of query aligns to 8:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
49% identity, 94% coverage: 29:500/504 of query aligns to 8:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 92% coverage: 36:500/504 of query aligns to 9:473/476 of 5x5uA
- active site: N151 (= N178), K174 (≠ H201), E249 (= E276), C283 (= C310), E380 (= E407), E457 (= E484)
- binding glycerol: D15 (≠ A42), A16 (= A43), A17 (≠ G44), G19 (≠ A46)
- binding nicotinamide-adenine-dinucleotide: P149 (= P176), P207 (≠ A234), A208 (= A235), S211 (≠ V238), G227 (= G254), S228 (= S255), V231 (≠ I258), R329 (= R356), R330 (≠ A357), E380 (= E407), F382 (= F409)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 92% coverage: 36:500/504 of query aligns to 9:473/476 of 5x5tA
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)
35% identity, 92% coverage: 34:499/504 of query aligns to 12:483/487 of Q9H2A2
- R109 (≠ Y132) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N178) mutation to A: Complete loss of activity.
- R451 (≠ T467) mutation to A: Complete loss of activity.
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 92% coverage: 35:497/504 of query aligns to 5:471/477 of 6j76A
- active site: N148 (= N178), E246 (= E276), C280 (= C310), E458 (= E484)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ V174), T145 (= T175), A146 (≠ P176), W147 (= W177), N148 (= N178), K171 (≠ H201), T173 (≠ S203), S174 (= S204), G204 (≠ A234), G208 (≠ V238), T223 (≠ N253), G224 (= G254), S225 (= S255), A228 (≠ I258), S231 (≠ L261), I232 (≠ L262), E246 (= E276), L247 (= L277), C280 (= C310), E381 (= E407), F383 (= F409), H447 (≠ F473)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
38% identity, 94% coverage: 32:503/504 of query aligns to 20:496/503 of 1bpwA
- active site: N166 (= N178), K189 (≠ H201), E263 (= E276), C297 (= C310), E400 (= E407), E477 (= E484)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V174), L163 (≠ T175), W165 (= W177), N166 (= N178), K189 (≠ H201), G221 (≠ A234), G225 (≠ V238), T240 (≠ N253), G241 (= G254), S242 (= S255), T245 (≠ I258), E263 (= E276), L264 (= L277), C297 (= C310), E400 (= E407), F402 (= F409), F466 (= F473)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
38% identity, 94% coverage: 32:503/504 of query aligns to 20:496/503 of P56533
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
34% identity, 93% coverage: 35:504/504 of query aligns to 6:478/494 of 5izdA
- active site: N149 (= N178), K172 (≠ H201), E247 (= E276), C281 (= C310), E381 (= E407), E458 (= E484)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ V174), T146 (= T175), W148 (= W177), K172 (≠ H201), P173 (= P202), S174 (= S203), S175 (= S204), R204 (= R233), G205 (≠ A234), G209 (≠ V238), D210 (≠ P239), G225 (= G254), S226 (= S255), T229 (≠ I258)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
35% identity, 93% coverage: 35:502/504 of query aligns to 21:497/498 of 4go2A
- active site: N170 (= N178), K193 (≠ H201), E269 (= E276), C303 (= C310), E400 (= E407), D479 (≠ E484)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (= V174), I167 (≠ T175), P168 (= P176), W169 (= W177), K193 (≠ H201), A195 (≠ S203), Q196 (≠ S204), S225 (≠ R233), G226 (≠ A234), G230 (≠ V238), Q231 (≠ P239), F244 (= F252), G246 (= G254), S247 (= S255), V250 (≠ I258), I254 (≠ L262), E269 (= E276), G271 (= G278), C303 (= C310), E400 (= E407), F402 (= F409)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
35% identity, 93% coverage: 35:502/504 of query aligns to 21:497/498 of 2o2rA
- active site: N170 (= N178), K193 (≠ H201), E269 (= E276), C303 (= C310), E400 (= E407), D479 (≠ E484)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (= V174), I167 (≠ T175), W169 (= W177), K193 (≠ H201), A195 (≠ S203), Q196 (≠ S204), S225 (≠ R233), G226 (≠ A234), G230 (≠ V238), Q231 (≠ P239), F244 (= F252), S247 (= S255), V250 (≠ I258), I254 (≠ L262)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
35% identity, 93% coverage: 35:502/504 of query aligns to 106:582/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (≠ H201), S310 (≠ R233), G311 (≠ A234), G315 (≠ V238), G331 (= G254), S332 (= S255), V335 (≠ I258)
- binding 4'-phosphopantetheine: K201 (≠ E127), F382 (≠ A304), N387 (≠ D309), C388 (= C310), N545 (≠ K465)
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)
35% identity, 93% coverage: 35:502/504 of query aligns to 425:901/902 of P28037
- IPW 571:573 (≠ TPW 175:177) binding NADP(+)
- KPAQ 597:600 (≠ HPSS 201:204) binding NADP(+)
- GSLVGQ 630:635 (≠ AAEIVP 234:239) binding NADP(+)
- GS 650:651 (= GS 254:255) binding NADP(+)
- E673 (= E276) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 276:277) binding NADP(+)
- C707 (= C310) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K360) binding NADP(+)
- ESF 804:806 (≠ ETF 407:409) binding NADP(+)
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.
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 92% coverage: 35:499/504 of query aligns to 11:485/503 of Q84LK3
- N162 (= N178) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ R186) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex (see paper)
36% identity, 93% coverage: 35:502/504 of query aligns to 21:497/498 of 7yjjC
Query Sequence
>WP_085124768.1 NCBI__GCF_900177295.1:WP_085124768.1
MAPSATASLRSVPAPARAGGQPDLADRRLFRELSYIGGRWTAAGDAGTLEVLDPADGCLV
GRVPTLGAKAATAAVAAAQAAFPAWRKRLARERAELLRAWHALIVANRRDLALLMVAEQG
KPLAEAEGEIDYAAGFLAWYAEEAVRVSAESLPSHLPGAETAVRREPIGVAALVTPWNFP
TAMITRKAAAALAAGCSVVVHPSSETPFSALALAELADRAGLPAGVFNVVTGRAAEIVPA
WCADTRVRALSFNGSTEIGRLLAEQCAPTVKQLILELGGHAPFVVFADADLERAVESCLS
AKFATSGQDCLAANRIYVERPVYQAFLARFLERVRDLKVGPGLEPGVEIGPLIHERALAK
MAEQVEDATARGARLLLGGARHALGGCFFEPTVLADVPDAALVFNEETFGPIAALAPFDS
EAEVLAKANATEYGLIAYLHSGDRARIARVVEALEYGMVAVNRTKVTGAPVPFGGVKQSG
LAREGGRAGLEAFTELKYVCSEVA
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