SitesBLAST
Comparing WP_011034265.1 NCBI__GCF_000007065.1:WP_011034265.1 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, 99% coverage: 3:450/454 of query aligns to 2:450/453 of 4itbA
- active site: N130 (= N131), K153 (= K154), E227 (= E228), C261 (= C262), E358 (= E358), E435 (= E435)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (≠ I127), M127 (= M128), P128 (= P129), W129 (= W130), N130 (= N131), K153 (= K154), A155 (= A156), S156 (= S157), A186 (≠ S187), V189 (≠ A190), G205 (= G206), S206 (= S207), A209 (= A210), S212 (≠ E213), L228 (= L229), C261 (= C262), E358 (= E358), F360 (= F360)
- binding 4-oxobutanoic acid: E227 (= E228), C261 (= C262), S418 (= S418)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
46% identity, 99% coverage: 3:450/454 of query aligns to 2:450/453 of 3vz3A
- active site: N130 (= N131), K153 (= K154), E227 (= E228), A261 (≠ C262), E358 (= E358), E435 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (≠ I127), M127 (= M128), W129 (= W130), N130 (= N131), Q135 (= Q136), R138 (= R139), K153 (= K154), A155 (= A156), S156 (= S157), A186 (≠ S187), V189 (≠ A190), T204 (= T205), G205 (= G206), S206 (= S207), A209 (= A210), E227 (= E228), L228 (= L229), G229 (= G230), A261 (≠ C262), F360 (= F360)
- binding 4-oxobutanoic acid: F131 (= F132), W134 (= W135), S260 (= S261), A261 (≠ C262), I262 (= I263), S418 (= S418)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
42% identity, 99% coverage: 5:454/454 of query aligns to 8:458/459 of 3efvA
- active site: N134 (= N131), E231 (= E228), C265 (= C262), E439 (= E435)
- binding nicotinamide-adenine-dinucleotide: I130 (= I127), M131 (= M128), P132 (= P129), W133 (= W130), N134 (= N131), Q139 (= Q136), R142 (= R139), K157 (= K154), A159 (= A156), N190 (≠ S187), V193 (≠ A190), T208 (= T205), G209 (= G206), S210 (= S207), A213 (= A210), E231 (= E228), L232 (= L229), G233 (= G230), C265 (= C262), E362 (= E358), F364 (= F360), F428 (= F424)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
39% identity, 99% coverage: 4:452/454 of query aligns to 3:453/455 of 4ywuA
- active site: N131 (= N131), K154 (= K154), E228 (= E228), C262 (= C262), E359 (= E358), E436 (= E435)
- binding 4-oxobutanoic acid: N131 (= N131), Q136 (= Q136), R139 (= R139), E228 (= E228), V261 (≠ S261), C262 (= C262), F425 (= F424)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
39% identity, 99% coverage: 4:452/454 of query aligns to 3:453/455 of 4ohtA
- active site: N131 (= N131), K154 (= K154), E228 (= E228), C262 (= C262), E359 (= E358), E436 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (≠ I127), E128 (≠ M128), P129 (= P129), W130 (= W130), K154 (= K154), H155 (= H155), A156 (= A156), S157 (= S157), Y187 (≠ S187), S207 (= S207), I214 (= I214)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
39% identity, 100% coverage: 1:452/454 of query aligns to 3:463/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I127), L137 (≠ M128), F139 (≠ W130), K163 (= K154), S165 (≠ A156), I166 (≠ S157), S196 (≠ D186), G200 (≠ A190), G216 (= G206), S217 (= S207), T220 (≠ A210), I224 (= I214)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
39% identity, 100% coverage: 1:452/454 of query aligns to 3:463/466 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 (= I127), L137 (≠ M128), F139 (≠ W130), K163 (= K154), S165 (≠ A156), I166 (≠ S157), S196 (≠ D186), G200 (≠ A190), G216 (= G206), S217 (= S207), T220 (≠ A210), I224 (= I214), L239 (= L229), C272 (= C262), E368 (= E358), F370 (= F360)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 93% coverage: 29:452/454 of query aligns to 53:479/481 of 3jz4A
- active site: N156 (= N131), K179 (= K154), E254 (= E228), C288 (= C262), E385 (= E358), E462 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P129), W155 (= W130), K179 (= K154), A181 (= A156), S182 (= S157), A212 (≠ R188), G216 (vs. gap), G232 (= G206), S233 (= S207), I236 (≠ A210), C288 (= C262), K338 (≠ S312), E385 (= E358), F387 (= F360)
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)
35% identity, 93% coverage: 29:452/454 of query aligns to 54:480/482 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)
33% identity, 99% coverage: 2:451/454 of query aligns to 24:483/497 of P17202
- I28 (= I6) binding K(+)
- D96 (≠ E72) binding K(+)
- SPW 156:158 (≠ MPW 128:130) binding NAD(+)
- Y160 (≠ F132) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R139) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAS 154:157) binding NAD(+)
- L186 (≠ N158) binding K(+)
- SSAT 236:239 (≠ SVRA 207:210) binding NAD(+)
- V251 (≠ I222) binding in other chain
- L258 (= L229) binding NAD(+)
- W285 (≠ I256) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E358) binding NAD(+)
- A441 (≠ F409) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S418) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F424) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K428) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
33% identity, 99% coverage: 2:451/454 of query aligns to 22:481/495 of 4v37A
- active site: N157 (= N131), K180 (= K154), E255 (= E228), A289 (≠ C262), E388 (= E358), E465 (= E435)
- binding 3-aminopropan-1-ol: C448 (≠ S418), W454 (≠ F424)
- binding nicotinamide-adenine-dinucleotide: I153 (= I127), S154 (≠ M128), P155 (= P129), W156 (= W130), N157 (= N131), M162 (≠ Q136), K180 (= K154), S182 (≠ A156), E183 (≠ S157), G213 (≠ D186), G217 (≠ A190), A218 (≠ M191), T232 (= T205), G233 (= G206), S234 (= S207), T237 (≠ A210), E255 (= E228), L256 (= L229), A289 (≠ C262), E388 (= E358), F390 (= F360)
Q56R04 Aminoaldehyde dehydrogenase 1; SlAMADH1; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Betaine aldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; 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 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) (see paper)
34% identity, 99% coverage: 2:451/454 of query aligns to 27:487/504 of Q56R04
- I31 (= I6) binding Na(+)
- D99 (≠ E72) binding Na(+)
- TPW 159:161 (≠ MPW 128:130) binding NAD(+)
- KPSE 185:188 (≠ KHAS 154:157) binding NAD(+)
- L189 (≠ N158) binding Na(+)
- GSGPT 238:242 (≠ GSVRA 206:210) binding NAD(+)
- E260 (= E228) active site, Proton acceptor
- L261 (= L229) binding NAD(+)
- C295 (= C262) active site, Nucleophile
- E394 (= E358) binding NAD(+)
- W460 (≠ F424) binding NAD(+)
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
34% identity, 99% coverage: 2:451/454 of query aligns to 22:482/496 of 4i9bA
- active site: N157 (= N131), K180 (= K154), E255 (= E228), C290 (= C262), E389 (= E358), D466 (≠ E435)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C262), W455 (≠ F424)
- binding nicotinamide-adenine-dinucleotide: I153 (= I127), T154 (≠ M128), W156 (= W130), K180 (= K154), S182 (≠ A156), E183 (≠ S157), G213 (≠ D186), G217 (≠ A190), G218 (≠ M191), F231 (≠ L204), S234 (= S207), T237 (≠ A210), I241 (= I214)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
32% identity, 99% coverage: 7:454/454 of query aligns to 49:499/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I127), A171 (≠ M128), P172 (= P129), W173 (= W130), K197 (= K154), A230 (≠ S187), F248 (≠ L204), G250 (= G206), S251 (= S207), V254 (≠ A210), M257 (≠ E213), L273 (= L229), C306 (= C262), K356 (≠ S312), E403 (= E358), F405 (= F360)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
32% identity, 99% coverage: 2:451/454 of query aligns to 19:481/497 of 3iwkH
- active site: N157 (= N131), K180 (= K154), E255 (= E228), C289 (= C262), E388 (= E358), E465 (= E435)
- binding nicotinamide-adenine-dinucleotide: W156 (= W130), G213 (≠ D186), G217 (≠ A190), A218 (≠ M191), G233 (= G206), S234 (= S207), T237 (≠ A210), K240 (≠ E213), C289 (= C262), Q336 (≠ F309), E388 (= E358), F390 (= F360)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
32% identity, 99% coverage: 2:451/454 of query aligns to 24:486/503 of Q8VWZ1
- N27 (≠ S5) binding Na(+)
- I28 (= I6) binding Na(+)
- D99 (≠ E72) binding Na(+)
- L189 (≠ N158) binding Na(+)
- 238:245 (vs. 206:213, 50% identical) binding NAD(+)
- C294 (= C262) binding NAD(+)
- E393 (= E358) binding NAD(+)
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)
30% identity, 99% coverage: 4:452/454 of query aligns to 30:485/494 of P49189
- C116 (= C91) 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)
30% identity, 99% coverage: 4:452/454 of query aligns to 29:484/493 of 6vr6D
- active site: N156 (= N131), E253 (= E228), C287 (= C262), E467 (= E435)
- binding nicotinamide-adenine-dinucleotide: I152 (= I127), G153 (≠ M128), W155 (= W130), K179 (= K154), A212 (≠ S187), G215 (≠ A190), Q216 (≠ M191), F229 (≠ L204), G231 (= G206), S232 (= S207), T235 (≠ A210), I239 (= I214)
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)
34% identity, 92% coverage: 36:451/454 of query aligns to 109:531/535 of P51649
- G176 (≠ E103) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ E108) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ E110) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R139) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (≠ N149) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KHAS 154:157) binding NAD(+)
- T233 (≠ V159) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A163) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ K181) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (vs. gap) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVRAG 206:211) binding NAD(+)
- R334 (≠ I256) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N257) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C262) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A264) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D293) natural variant: N -> S
- P382 (= P303) to L: in SSADHD; 2% of activity
- V406 (≠ P327) to I: in dbSNP:rs143741652
- G409 (≠ Y330) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S418) 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
- 93 C → F: in SSADHD; 3% of activity; dbSNP:rs765561257
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
32% identity, 99% coverage: 2:452/454 of query aligns to 30:487/489 of 7a6qB
- active site: N163 (= N131), E262 (= E228), C296 (= C262), E470 (= E435)
- binding nicotinamide-adenine-dinucleotide: I159 (= I127), W162 (= W130), K186 (= K154), E189 (≠ S157), G219 (≠ D186), G223 (≠ A190), S240 (= S207), V243 (≠ A210), K342 (≠ E308)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ K4), T33 (≠ S5), C34 (≠ I6), P36 (= P8), D103 (≠ E72), E189 (≠ S157), Q190 (≠ N158), F218 (≠ I185), I339 (≠ A305), D340 (≠ K306)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ K86), D141 (≠ T109), N143 (≠ A111), N451 (≠ V416), L453 (≠ S418), A455 (≠ P420)
Query Sequence
>WP_011034265.1 NCBI__GCF_000007065.1:WP_011034265.1
MKIKSIDPYTEEVNWTYDALSFGDCEDQIEKSRAAFLKWGSLSVKERTAYISRVAEILRQ
NRRIYAGIITKEMGKPVRQSLAEIEKCAWLCDYYAENAAGFLEDELVETEAEKSYVTFEP
LGVILGIMPWNFPFWQTFRFAVPTLIAGNVCLLKHASNVPGSALEIEKVFTGAGLPQDVF
KSLLIDSRTAMEIIDEDLVDGISLTGSVRAGSEIGELAGRTIKPFVLELGGSDPFIVLED
ADIDRAAEVGVRARFINTGQSCIAAKRFIVVEDVVVDFIEAFELHMQELKVGDPMDEETD
IGPVAKKEFIDSLERVLKDAKKKGAEPRVYGEEHKKGFFFRPTIVPAASTDMKVLNMEVF
GPIAPVVMVKDEDEAVKIANSTDFGLGAEIWSADLKRAEHLAKRIKSGFVTINGRVKSDP
RLPFGGVKKSGIGRELSHYGLKEFVNIKTVVINK
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