SitesBLAST
Comparing NP_662456.1 NCBI__GCF_000006985.1:NP_662456.1 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)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
46% identity, 100% coverage: 2:456/457 of query aligns to 2:452/453 of 4itbA
- active site: N130 (= N130), K153 (= K153), E227 (= E231), C261 (= C265), E358 (= E362), E435 (= E439)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (= V126), M127 (= M127), P128 (= P128), W129 (= W129), N130 (= N130), K153 (= K153), A155 (= A155), S156 (≠ P156), A186 (≠ L186), V189 (= V189), G205 (= G209), S206 (= S210), A209 (= A213), S212 (≠ A216), L228 (= L232), C261 (= C265), E358 (= E362), F360 (= F364)
- binding 4-oxobutanoic acid: E227 (= E231), C261 (= C265), S418 (= S422)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
49% identity, 99% coverage: 3:455/457 of query aligns to 7:455/459 of 3efvA
- active site: N134 (= N130), E231 (= E231), C265 (= C265), E439 (= E439)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ V126), M131 (= M127), P132 (= P128), W133 (= W129), N134 (= N130), Q139 (= Q135), R142 (= R138), K157 (= K153), A159 (= A155), N190 (≠ L186), V193 (= V189), T208 (= T208), G209 (= G209), S210 (= S210), A213 (= A213), E231 (= E231), L232 (= L232), G233 (= G233), C265 (= C265), E362 (= E362), F364 (= F364), F428 (= F428)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
46% identity, 100% coverage: 2:456/457 of query aligns to 2:452/453 of 3vz3A
- active site: N130 (= N130), K153 (= K153), E227 (= E231), A261 (≠ C265), E358 (= E362), E435 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (= V126), M127 (= M127), W129 (= W129), N130 (= N130), Q135 (= Q135), R138 (= R138), K153 (= K153), A155 (= A155), S156 (≠ P156), A186 (≠ L186), V189 (= V189), T204 (= T208), G205 (= G209), S206 (= S210), A209 (= A213), E227 (= E231), L228 (= L232), G229 (= G233), A261 (≠ C265), F360 (= F364)
- binding 4-oxobutanoic acid: F131 (= F131), W134 (= W134), S260 (= S264), A261 (≠ C265), I262 (= I266), S418 (= S422)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
39% identity, 99% coverage: 4:457/457 of query aligns to 4:454/455 of 4ywuA
- active site: N131 (= N130), K154 (= K153), E228 (= E231), C262 (= C265), E359 (= E362), E436 (= E439)
- binding 4-oxobutanoic acid: N131 (= N130), Q136 (= Q135), R139 (= R138), E228 (= E231), V261 (≠ S264), C262 (= C265), F425 (= F428)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
39% identity, 99% coverage: 4:457/457 of query aligns to 4:454/455 of 4ohtA
- active site: N131 (= N130), K154 (= K153), E228 (= E231), C262 (= C265), E359 (= E362), E436 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (= V126), E128 (≠ M127), P129 (= P128), W130 (= W129), K154 (= K153), H155 (= H154), A156 (= A155), S157 (≠ P156), Y187 (≠ L186), S207 (= S210), I214 (≠ V217)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 99% coverage: 2:452/457 of query aligns to 27:475/481 of 3jz4A
- active site: N156 (= N130), K179 (= K153), E254 (= E231), C288 (= C265), E385 (= E362), E462 (= E439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P128), W155 (= W129), K179 (= K153), A181 (= A155), S182 (≠ P156), A212 (≠ L186), G216 (vs. gap), G232 (= G209), S233 (= S210), I236 (≠ A213), C288 (= C265), K338 (≠ L315), E385 (= E362), F387 (= F364)
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)
33% identity, 99% coverage: 2:452/457 of query aligns to 28:476/482 of P25526
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)
32% identity, 99% coverage: 2:452/457 of query aligns to 25:480/497 of P17202
- I28 (= I5) binding K(+)
- D96 (≠ E71) binding K(+)
- SPW 156:158 (≠ MPW 127:129) binding NAD(+)
- Y160 (≠ F131) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R138) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAP 153:156) binding NAD(+)
- L186 (≠ N157) binding K(+)
- SSAT 236:239 (≠ STGA 210:213) binding NAD(+)
- V251 (≠ L225) binding in other chain
- L258 (= L232) binding NAD(+)
- W285 (≠ L259) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E362) binding NAD(+)
- A441 (≠ S413) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S422) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F428) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K432) binding K(+)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
35% identity, 92% coverage: 38:456/457 of query aligns to 64:482/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W129), K180 (= K153), A182 (= A155), T212 (≠ V189), G213 (≠ D190), G217 (= G194), F231 (≠ V207), G233 (= G209), S234 (= S210), V237 (≠ A213), Q337 (≠ L312), E388 (= E362), F390 (= F364)
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)
33% identity, 98% coverage: 7:453/457 of query aligns to 34:482/494 of P49189
- C116 (= C90) 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)
33% identity, 98% coverage: 7:453/457 of query aligns to 33:481/493 of 6vr6D
- active site: N156 (= N130), E253 (= E231), C287 (= C265), E467 (= E439)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ V126), G153 (≠ M127), W155 (= W129), K179 (= K153), A212 (≠ R191), G215 (= G194), Q216 (vs. gap), F229 (≠ V207), G231 (= G209), S232 (= S210), T235 (≠ A213), I239 (≠ V217)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
31% identity, 99% coverage: 2:452/457 of query aligns to 23:478/495 of 4v37A
- active site: N157 (= N130), K180 (= K153), E255 (= E231), A289 (≠ C265), E388 (= E362), E465 (= E439)
- binding 3-aminopropan-1-ol: C448 (≠ S422), W454 (≠ F428)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V126), S154 (≠ M127), P155 (= P128), W156 (= W129), N157 (= N130), M162 (≠ Q135), K180 (= K153), S182 (≠ A155), E183 (≠ P156), G213 (vs. gap), G217 (vs. gap), A218 (vs. gap), T232 (= T208), G233 (= G209), S234 (= S210), T237 (≠ A213), E255 (= E231), L256 (= L232), A289 (≠ C265), E388 (= E362), F390 (= F364)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
33% identity, 99% coverage: 6:456/457 of query aligns to 49:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (≠ V126), A171 (≠ M127), P172 (= P128), W173 (= W129), K197 (= K153), A230 (≠ V189), F248 (≠ V207), G250 (= G209), S251 (= S210), V254 (≠ A213), M257 (≠ A216), L273 (= L232), C306 (= C265), K356 (≠ L315), E403 (= E362), F405 (= F364)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
35% identity, 92% coverage: 38:456/457 of query aligns to 63:481/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (≠ V126), T153 (≠ M127), P154 (= P128), W155 (= W129), N156 (= N130), I161 (≠ Q135), K179 (= K153), A181 (= A155), E182 (≠ P156), T211 (≠ V189), G212 (≠ D190), G216 (= G194), Q217 (vs. gap), F230 (≠ V207), T231 (= T208), G232 (= G209), S233 (= S210), V236 (≠ A213), E255 (= E231), L256 (= L232), G257 (= G233), A289 (≠ C265), E387 (= E362), F389 (= F364)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
33% identity, 94% coverage: 19:447/457 of query aligns to 20:450/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (≠ V126), L137 (≠ M127), F139 (≠ W129), K163 (= K153), S165 (≠ A155), I166 (≠ P156), S196 (≠ L186), G200 (vs. gap), G216 (= G209), S217 (= S210), T220 (≠ A213), I224 (≠ V217)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
33% identity, 94% coverage: 19:447/457 of query aligns to 20:450/466 of 8hapA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: I136 (≠ V126), L137 (≠ M127), F139 (≠ W129), K163 (= K153), S165 (≠ A155), I166 (≠ P156), S196 (≠ L186), G200 (vs. gap), G216 (= G209), S217 (= S210), T220 (≠ A213), I224 (≠ V217), L239 (= L232), C272 (= C265), E368 (= E362), F370 (= F364)
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
36% identity, 92% coverage: 38:456/457 of query aligns to 78:495/505 of 3u4jA
Sites not aligning to the query:
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
32% identity, 98% coverage: 7:453/457 of query aligns to 43:491/503 of 1bpwA
- active site: N166 (= N130), K189 (= K153), E263 (= E231), C297 (= C265), E400 (= E362), E477 (= E439)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V126), L163 (≠ M127), W165 (= W129), N166 (= N130), K189 (= K153), G221 (≠ D185), G225 (= G194), T240 (= T208), G241 (= G209), S242 (= S210), T245 (≠ A213), E263 (= E231), L264 (= L232), C297 (= C265), E400 (= E362), F402 (= F364), F466 (= F428)
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)
32% identity, 98% coverage: 7:453/457 of query aligns to 43:491/503 of P56533
7radA Crystal structure analysis of aldh1b1
33% identity, 98% coverage: 4:453/457 of query aligns to 32:483/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V126), I159 (≠ M127), P160 (= P128), W161 (= W129), N162 (= N130), M167 (vs. gap), K185 (= K153), E188 (≠ P156), G218 (vs. gap), G222 (vs. gap), A223 (vs. gap), T237 (= T208), G238 (= G209), S239 (= S210), V242 (≠ A213), E261 (= E231), L262 (= L232), C295 (= C265), E392 (= E362), F394 (= F364)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ K85), F163 (= F131), E285 (≠ A255), F289 (≠ L259), N450 (≠ V420), V452 (≠ S422)
Query Sequence
>NP_662456.1 NCBI__GCF_000006985.1:NP_662456.1
MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQ
AEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEFLQPEQSEIDGAKGIVAFEPL
GVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYR
AVHIDLDEVDRLTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIV
LEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAK
STEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYS
EEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMV
KSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYLP
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