SitesBLAST
Comparing WP_028742935.1 NCBI__GCF_000009265.1:WP_028742935.1 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)
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)
58% identity, 99% coverage: 4:482/485 of query aligns to 3:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
58% identity, 99% coverage: 4:482/485 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E256), C288 (= C290), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P156), W155 (= W157), K179 (= K181), A181 (≠ S183), S182 (≠ D184), A212 (≠ P214), G216 (= G218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C290), K338 (= K340), E385 (= E387), F387 (= F389)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
54% identity, 100% coverage: 1:485/485 of query aligns to 17:501/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I154), A171 (≠ T155), P172 (= P156), W173 (= W157), K197 (= K181), A230 (≠ P214), F248 (= F232), G250 (= G234), S251 (= S235), V254 (= V238), M257 (≠ L241), L273 (= L257), C306 (= C290), K356 (= K340), E403 (= E387), F405 (= F389)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
55% identity, 99% coverage: 4:484/485 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I154), T153 (= T155), P154 (= P156), K179 (= K181), A212 (≠ P214), K213 (≠ A215), F230 (= F232), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), W239 (≠ L241), G256 (= G258)
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)
54% identity, 99% coverage: 6:484/485 of query aligns to 55:535/535 of P51649
- C93 (≠ M46) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G129) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P133) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P135) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R166) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C176) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPSD 181:184) binding NAD(+)
- T233 (= T186) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A190) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N208) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G218) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTRVG 234:239) binding NAD(+)
- R334 (= R284) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N285) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C290) modified: Disulfide link with 342, In inhibited form
- C342 (= C292) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ A321) natural variant: N -> S
- P382 (= P331) to L: in SSADHD; 2% of activity
- V406 (≠ I355) to I: in dbSNP:rs143741652
- G409 (≠ T358) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S447) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G482) 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)
54% identity, 99% coverage: 7:484/485 of query aligns to 6:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 99% coverage: 7:484/485 of query aligns to 6:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 97% coverage: 11:481/485 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N158), E246 (= E256), C280 (= C290), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I154), T145 (= T155), A146 (≠ P156), W147 (= W157), N148 (= N158), K171 (= K181), T173 (≠ S183), S174 (≠ D184), G204 (≠ P214), G208 (= G218), T223 (= T233), G224 (= G234), S225 (= S235), A228 (≠ V238), S231 (≠ L241), I232 (≠ L242), E246 (= E256), L247 (= L257), C280 (= C290), E381 (= E387), F383 (= F389), H447 (≠ F453)
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)
38% identity, 97% coverage: 10:481/485 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (= E256), C298 (= C290), E399 (= E387), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P156), K189 (= K181), E192 (≠ D184), G222 (≠ P214), G226 (= G218), G242 (= G234), G243 (≠ S235), T246 (≠ V238), H249 (≠ L241), I250 (≠ L242), C298 (= C290), E399 (= E387), F401 (= F389)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 97% coverage: 13:481/485 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (≠ G22), A16 (= A23), A17 (= A24), G19 (= G26)
- binding nicotinamide-adenine-dinucleotide: P149 (= P156), P207 (= P214), A208 (= A215), S211 (≠ G218), G227 (= G234), S228 (= S235), V231 (= V238), R329 (≠ A336), R330 (≠ A337), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 97% coverage: 13:481/485 of query aligns to 6:474/476 of 5x5tA
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 96% coverage: 15:478/485 of query aligns to 9:475/486 of 4pxlA
- active site: N154 (= N158), K177 (= K181), E253 (= E256), C287 (= C290), E384 (= E387), D461 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (≠ T155), P152 (= P156), W153 (= W157), K177 (= K181), E180 (≠ D184), G210 (≠ P214), G214 (= G218), A215 (≠ D219), F228 (= F232), G230 (= G234), S231 (= S235), V234 (= V238), E253 (= E256), G255 (= G258), C287 (= C290), Q334 (≠ A337), K337 (= K340), E384 (= E387), F386 (= F389)
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)
38% identity, 96% coverage: 12:477/485 of query aligns to 8:480/497 of P17202
- I28 (= I32) binding K(+)
- D96 (≠ E98) binding K(+)
- SPW 156:158 (≠ TPW 155:157) binding NAD(+)
- Y160 (≠ F159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R166) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSD 181:184) binding NAD(+)
- L186 (= L185) binding K(+)
- SSAT 236:239 (≠ STRV 235:238) binding NAD(+)
- V251 (= V250) binding in other chain
- L258 (= L257) binding NAD(+)
- W285 (≠ R284) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E387) binding NAD(+)
- A441 (≠ M438) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S447) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F453) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K457) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 96% coverage: 12:477/485 of query aligns to 6:478/495 of 4v37A
- active site: N157 (= N158), K180 (= K181), E255 (= E256), A289 (≠ C290), E388 (= E387), E465 (= E464)
- binding 3-aminopropan-1-ol: C448 (≠ S447), W454 (≠ F453)
- binding nicotinamide-adenine-dinucleotide: I153 (= I154), S154 (≠ T155), P155 (= P156), W156 (= W157), N157 (= N158), M162 (= M163), K180 (= K181), S182 (= S183), E183 (≠ D184), G213 (≠ P214), G217 (= G218), A218 (≠ D219), T232 (= T233), G233 (= G234), S234 (= S235), T237 (≠ V238), E255 (= E256), L256 (= L257), A289 (≠ C290), E388 (= E387), F390 (= F389)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 97% coverage: 7:478/485 of query aligns to 5:486/505 of O24174
- N164 (= N158) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ R166) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 96% coverage: 15:478/485 of query aligns to 14:483/494 of 4pz2B
- active site: N159 (= N158), K182 (= K181), E258 (= E256), C292 (= C290), E392 (= E387), D469 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I155 (= I154), I156 (≠ T155), P157 (= P156), W158 (= W157), N159 (= N158), M164 (= M163), K182 (= K181), A184 (≠ S183), E185 (≠ D184), G215 (≠ P214), G219 (= G218), F233 (= F232), T234 (= T233), G235 (= G234), S236 (= S235), V239 (= V238), E258 (= E256), L259 (= L257), C292 (= C290), E392 (= E387), F394 (= F389)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
38% identity, 96% coverage: 15:481/485 of query aligns to 35:505/512 of P47895
- R89 (= R66) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K181) binding NAD(+)
- E207 (≠ D184) binding NAD(+)
- GSTEVG 257:262 (≠ GSTRVG 234:239) binding NAD(+)
- Q361 (≠ A337) binding NAD(+)
- E411 (= E387) binding NAD(+)
- A493 (≠ G469) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
38% identity, 96% coverage: 15:481/485 of query aligns to 17:487/489 of 7a6qB
- active site: N163 (= N158), E262 (= E256), C296 (= C290), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), W162 (= W157), K186 (= K181), E189 (≠ D184), G219 (≠ P214), G223 (= G218), S240 (= S235), V243 (= V238), K342 (≠ A336)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ E30), T33 (≠ V31), C34 (≠ I32), P36 (= P34), D103 (≠ E98), E189 (≠ D184), Q190 (≠ L185), F218 (≠ M213), I339 (= I333), D340 (≠ N334)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G108), D141 (= D138), N143 (≠ R140), N451 (≠ A445), L453 (≠ S447), A455 (≠ E449)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
38% identity, 96% coverage: 15:481/485 of query aligns to 17:487/489 of 7a6qA
- active site: N163 (= N158), E262 (= E256), C296 (= C290), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), T160 (= T155), W162 (= W157), K186 (= K181), A188 (≠ S183), E189 (≠ D184), G219 (≠ P214), G223 (= G218), S240 (= S235), V243 (= V238), K342 (≠ A336), K346 (= K340)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G108), D141 (= D138), N143 (≠ R140), N451 (≠ A445), L453 (≠ S447), Y454 (≠ T448)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
38% identity, 96% coverage: 15:481/485 of query aligns to 17:487/489 of 5fhzA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), T160 (= T155), W162 (= W157), K186 (= K181), E189 (≠ D184), G219 (≠ P214), G223 (= G218), F237 (= F232), G239 (= G234), S240 (= S235), T241 (= T236), V243 (= V238), G264 (= G258), Q343 (≠ A337), E393 (= E387)
- binding retinoic acid: G118 (= G108), R121 (= R111), F164 (= F159), M168 (= M163), W171 (≠ R166), C295 (≠ T289), C296 (= C290), L453 (≠ S447)
Query Sequence
>WP_028742935.1 NCBI__GCF_000009265.1:WP_028742935.1
MNGLRDSSLLRQQGLIDGEWRGAAAGHTIEVIDPATQHVLGTVPDMDGADTRAAIVAAEK
AFGPWRAKTNAERGALLEAWHDLMLDNIEDLALILTREQGKPLTEARGEIRYGASFIRWF
SEEARRIGGTTIPSPTADRRIVVLKEPVGVSAIITPWNFPNAMITRKVGPALAAGCTVVV
KPSDLTPFSALALGVLAERAGIPKGVINIVTGMPAGIGDELMANQTVRKISFTGSTRVGS
LLMRGAADSVKRLSLELGGNAPFIVFDDADLDLAVEGAIASKFRNGGQTCVCANRLLVQS
GVYEAFAAKLSARVSAMKVGAGTDAGTDIGPMINKAAIEKIRRHVDDAVEKGARILATAG
FMPEGDQYAVPMVLGGATTEMQLASEETFGPVAPLFRFDNEEEAIRIANATPFGLAAYFY
TGSLKRSWRVAEALEFGMVGLNTGAISTEVAPFGGVKQSGLGREGAQCGIEEYLEMKSFH
IGGLA
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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