SitesBLAST
Comparing WP_052591776.1 NCBI__GCF_001190945.1:WP_052591776.1 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
51% identity, 98% coverage: 13:486/486 of query aligns to 9:481/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E259), C288 (= C293), E385 (= E390), E462 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (= A185), S182 (≠ A186), A212 (≠ S217), G216 (≠ M221), G232 (= G237), S233 (= S238), I236 (= I241), C288 (= C293), K338 (= K343), E385 (= E390), F387 (= F392)
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)
50% identity, 98% coverage: 13:486/486 of query aligns to 10:482/482 of P25526
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
45% identity, 97% coverage: 13:484/486 of query aligns to 27:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I156), A171 (≠ T157), P172 (= P158), W173 (= W159), K197 (= K183), A230 (≠ T216), F248 (= F235), G250 (= G237), S251 (= S238), V254 (≠ I241), M257 (≠ K244), L273 (= L260), C306 (= C293), K356 (= K343), E403 (= E390), F405 (= F392)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
48% identity, 96% coverage: 17:484/486 of query aligns to 13:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ T216), K213 (≠ S217), F230 (= F235), T231 (= T236), G232 (= G237), S233 (= S238), V236 (≠ I241), W239 (≠ K244), G256 (= G261)
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)
47% identity, 96% coverage: 17:482/486 of query aligns to 64:530/535 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 (≠ T135) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P137) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R168) binding substrate; 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 (≠ KPAA 183:186) binding NAD(+)
- T233 (= T188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ M192) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ M221) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPIG 237:242) binding NAD(+)
- R334 (= R287) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N288) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C293) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A295) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D324) natural variant: N -> S
- P382 (= P334) to L: in SSADHD; 2% of activity
- V406 (= V358) to I: in dbSNP:rs143741652
- G409 (= G361) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S450) 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)
47% identity, 96% coverage: 17:482/486 of query aligns to 14:480/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
47% identity, 96% coverage: 17:482/486 of query aligns to 14:480/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 96% coverage: 15:482/486 of query aligns to 6:472/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E259), C283 (= C293), E380 (= E390), E457 (= E467)
- binding glycerol: D15 (= D24), A16 (= A25), A17 (≠ E26), G19 (= G28)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (≠ T216), A208 (≠ S217), S211 (≠ M221), G227 (= G237), S228 (= S238), V231 (≠ I241), R329 (≠ K339), R330 (≠ A340), E380 (= E390), F382 (= F392)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 96% coverage: 15:482/486 of query aligns to 6:472/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 13:480/486 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N160), E246 (= E259), C280 (= C293), E458 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I156), T145 (= T157), A146 (≠ P158), W147 (= W159), N148 (= N160), K171 (= K183), T173 (≠ A185), S174 (≠ A186), G204 (= G218), G208 (vs. gap), T223 (= T236), G224 (= G237), S225 (= S238), A228 (≠ I241), S231 (≠ K244), I232 (≠ L245), E246 (= E259), L247 (= L260), C280 (= C293), E381 (= E390), F383 (= F392), H447 (≠ F456)
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
36% identity, 97% coverage: 14:482/486 of query aligns to 8:482/497 of P17202
- I28 (≠ D34) binding K(+)
- D96 (≠ E100) binding K(+)
- SPW 156:158 (≠ TPW 157:159) binding NAD(+)
- Y160 (≠ F161) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R168) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAA 183:186) binding NAD(+)
- L186 (≠ E187) binding K(+)
- SSAT 236:239 (≠ STPI 238:241) binding NAD(+)
- V251 (≠ L253) binding in other chain
- L258 (= L260) binding NAD(+)
- W285 (≠ R287) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E390) binding NAD(+)
- A441 (≠ M441) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S450) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F456) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K460) binding K(+)
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 97% coverage: 13:482/486 of query aligns to 7:485/503 of Q84LK3
- N162 (= N160) 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 (≠ R168) 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).
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 98% coverage: 13:486/486 of query aligns to 5:482/489 of 4cazA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C293), E386 (= E390), E463 (= E467)
- 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 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), E178 (≠ A186), G208 (≠ T216), G212 (≠ M221), F226 (= F235), T227 (= T236), G228 (= G237), G229 (≠ S238), T232 (≠ I241), V236 (≠ L245), E251 (= E259), L252 (= L260), C285 (= C293), E386 (= E390), F388 (= F392)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 98% coverage: 13:486/486 of query aligns to 5:482/489 of 2woxA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C293), E386 (= E390), E463 (= E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), S177 (≠ A185), E178 (≠ A186), G208 (≠ T216), G212 (≠ M221), F226 (= F235), T227 (= T236), G228 (= G237), G229 (≠ S238), T232 (≠ I241), V236 (≠ L245), E251 (= E259), L252 (= L260), C285 (= C293), E386 (= E390), F388 (= F392)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 98% coverage: 13:486/486 of query aligns to 5:482/489 of 2wmeA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C293), E386 (= E390), E463 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T157), W151 (= W159), K175 (= K183), S177 (≠ A185), E178 (≠ A186), G208 (≠ T216), G212 (≠ M221), F226 (= F235), G228 (= G237), G229 (≠ S238), T232 (≠ I241), V236 (≠ L245)
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)
39% identity, 98% coverage: 13:486/486 of query aligns to 6:483/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 157:160) binding NADPH
- K162 (= K169) active site, Charge relay system
- KPSE 176:179 (≠ KPAA 183:186) binding NADPH
- G209 (≠ T216) binding NADPH
- GTST 230:233 (≠ STPI 238:241) binding NADPH
- E252 (= E259) active site, Proton acceptor
- C286 (= C293) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E390) binding NADPH
- E464 (= E467) active site, Charge relay system
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 97% coverage: 15:486/486 of query aligns to 18:490/491 of 5gtlA
- active site: N165 (= N160), K188 (= K183), E263 (= E259), C297 (= C293), E394 (= E390), E471 (= E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I156), P163 (= P158), K188 (= K183), A190 (= A185), E191 (≠ A186), Q192 (≠ E187), G221 (≠ S217), G225 (≠ M221), G241 (= G237), S242 (= S238), T245 (≠ I241), L264 (= L260), C297 (= C293), E394 (= E390), F396 (= F392)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 97% coverage: 15:486/486 of query aligns to 18:490/491 of 5gtkA
- active site: N165 (= N160), K188 (= K183), E263 (= E259), C297 (= C293), E394 (= E390), E471 (= E467)
- binding nicotinamide-adenine-dinucleotide: I161 (= I156), I162 (≠ T157), P163 (= P158), W164 (= W159), K188 (= K183), E191 (≠ A186), G221 (≠ S217), G225 (≠ M221), A226 (≠ E222), F239 (= F235), G241 (= G237), S242 (= S238), T245 (≠ I241), Y248 (≠ K244), L264 (= L260), C297 (= C293), Q344 (≠ A340), R347 (≠ K343), E394 (= E390), F396 (= F392)
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
38% identity, 97% coverage: 14:482/486 of query aligns to 5:482/500 of 4i8pA
- active site: N159 (= N160), K182 (= K183), E257 (= E259), C291 (= C293), E390 (= E390), E467 (= E467)
- binding nicotinamide-adenine-dinucleotide: I155 (= I156), T156 (= T157), P157 (= P158), W158 (= W159), N159 (= N160), M164 (= M165), K182 (= K183), S184 (≠ A185), E185 (≠ A186), G215 (≠ S217), G219 (≠ M221), A220 (≠ E222), T234 (= T236), G235 (= G237), S236 (= S238), T239 (≠ I241), E257 (= E259), L258 (= L260), C291 (= C293), E390 (= E390), F392 (= F392), W456 (≠ F456)
C0P9J6 Aminoaldehyde dehydrogenase 1a; ZmAMADH1a; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a; Aminobutyraldehyde dehydrogenase AMADH1a; Betaine aldehyde dehydrogenase AMADH1a; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Zea mays (Maize) (see paper)
38% identity, 97% coverage: 14:482/486 of query aligns to 10:487/505 of C0P9J6
Query Sequence
>WP_052591776.1 NCBI__GCF_001190945.1:WP_052591776.1
MGETKTSVLERVKKQLFIAGEWRDAEGGATLEVDNPATGEALTHVADGSVKDGDAALAAA
AAAQADWAKTPPRDRGELLRSAYEMLVERTEDLATLMTLEMGKPLAESRGEVAYGSEFFR
WFSEEAVRISGRWSTAPNGATRLVTMKQPVGPTLMITPWNFPLAMGTRKIGPAIAAGCTM
VVKPAAETPLTMLLLAQILEEVGLPKGVLNVITTSTSGQVMEPLIRDPRSRKLTFTGSTP
IGQKLIEQSAEQLLRVSMELGGNAPFLVFEDADLDAAVEGAMLAKMRNIGEACTAANRFL
VHADVADEFSRRLAERMGALTVGDGMDDDTKVGPLINAKAVDKVKALVEDAKGRGARVVT
GGETVGDRGFFYAPTVLTDVTGEADMAREEIFGPVAGIQTFTDEADAIERANSTEYGLVA
YFFTKDFSRAIRVSEALEYGMVGVNQGIVSNPAAPFGGVKASGFGREGGFEGIDEYLETK
YVGLAL
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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