SitesBLAST
Comparing 6937359 FitnessBrowser__SB2B:6937359 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
47% identity, 95% coverage: 22:509/515 of query aligns to 5:491/504 of 1eyyA
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
25% identity, 92% coverage: 17:492/515 of query aligns to 483:945/959 of 5ur2B
Sites not aligning to the query:
- binding N-propargylglycine-modified flavin adenine dinucleotide: 174, 215, 216, 249, 278, 279, 280, 281, 283, 300, 301, 302, 303, 306, 329, 330, 331, 332, 356, 357, 358, 379, 398, 403, 405
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
26% identity, 76% coverage: 21:410/515 of query aligns to 33:413/491 of 5gtlA
- active site: N165 (= N159), K188 (= K184), E263 (= E265), C297 (= C302), E394 (= E391)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ F155), P163 (≠ A157), K188 (= K184), A190 (≠ H186), E191 (≠ P187), Q192 (≠ S188), G221 (≠ E221), G225 (≠ S225), G241 (= G241), S242 (= S242), T245 (≠ V245), L264 (= L266), C297 (= C302), E394 (= E391), F396 (= F393)
Sites not aligning to the query:
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
26% identity, 76% coverage: 21:410/515 of query aligns to 33:413/491 of 5gtkA
- active site: N165 (= N159), K188 (= K184), E263 (= E265), C297 (= C302), E394 (= E391)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ F155), I162 (≠ G156), P163 (≠ A157), W164 (≠ S158), K188 (= K184), E191 (≠ P187), G221 (≠ E221), G225 (≠ S225), A226 (≠ V226), F239 (= F239), G241 (= G241), S242 (= S242), T245 (≠ V245), Y248 (≠ L248), L264 (= L266), C297 (= C302), Q344 (vs. gap), R347 (vs. gap), E394 (= E391), F396 (= F393)
Sites not aligning to the query:
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
29% identity, 64% coverage: 4:333/515 of query aligns to 1:311/488 of 5u0mA
- active site: N148 (= N159), K171 (= K184), E246 (= E265), C280 (= C302)
- binding nicotinamide-adenine-dinucleotide: F144 (= F155), Y147 (≠ S158), N148 (= N159), K171 (= K184), S173 (≠ H186), E174 (≠ P187), G207 (≠ S225), T222 (= T240), G223 (= G241), S224 (= S242), V227 (= V245), E246 (= E265), M247 (≠ L266), G248 (= G267), C280 (= C302)
Sites not aligning to the query:
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
29% identity, 64% coverage: 4:333/515 of query aligns to 1:311/488 of 5u0lA
Sites not aligning to the query:
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
30% identity, 57% coverage: 9:304/515 of query aligns to 29:307/515 of 2d4eC
- active site: N173 (= N159), K196 (= K184), E271 (= E265), C305 (= C302)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F155), T170 (≠ G156), P171 (≠ A157), W172 (≠ S158), K196 (= K184), A198 (≠ H186), G229 (≠ E221), G233 (≠ S225), A234 (≠ V226), T248 (= T240), G249 (= G241), E250 (≠ S242), T253 (≠ V245), E271 (= E265), L272 (= L266), C305 (= C302)
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
29% identity, 54% coverage: 26:303/515 of query aligns to 31:289/481 of 3jz4A
- active site: N156 (= N159), K179 (= K184), E254 (= E265), C288 (= C302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A157), W155 (≠ S158), K179 (= K184), A181 (≠ H186), S182 (≠ P187), A212 (≠ E221), G216 (≠ S225), G232 (= G241), S233 (= S242), I236 (≠ V245), C288 (= C302)
Sites not aligning to the query:
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)
29% identity, 54% coverage: 26:303/515 of query aligns to 32:290/482 of P25526
Sites not aligning to the query:
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
28% identity, 58% coverage: 10:306/515 of query aligns to 21:307/498 of 4go2A
- active site: N170 (= N159), K193 (= K184), E269 (= E265), C303 (= C302)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ F155), I167 (≠ G156), P168 (≠ A157), W169 (≠ S158), K193 (= K184), A195 (≠ H186), Q196 (≠ P187), S225 (= S220), G226 (≠ E221), G230 (≠ S225), Q231 (≠ V226), F244 (= F239), G246 (= G241), S247 (= S242), V250 (= V245), I254 (≠ L249), E269 (= E265), G271 (= G267), C303 (= C302)
Sites not aligning to the query:
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
28% identity, 58% coverage: 10:306/515 of query aligns to 21:307/498 of 2o2rA
- active site: N170 (= N159), K193 (= K184), E269 (= E265), C303 (= C302)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ F155), I167 (≠ G156), W169 (≠ S158), K193 (= K184), A195 (≠ H186), Q196 (≠ P187), S225 (= S220), G226 (≠ E221), G230 (≠ S225), Q231 (≠ V226), F244 (= F239), S247 (= S242), V250 (= V245), I254 (≠ L249)
Sites not aligning to the query:
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
28% identity, 58% coverage: 10:306/515 of query aligns to 106:392/583 of 7rluA
Sites not aligning to the query:
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)
28% identity, 58% coverage: 10:306/515 of query aligns to 425:711/902 of P28037
- IPW 571:573 (≠ GAS 156:158) binding
- KPAQ 597:600 (≠ KGHP 184:187) binding
- GSLVGQ 630:635 (≠ EPALSV 221:226) binding
- GS 650:651 (= GS 241:242) binding
- E673 (= E265) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 265:266) binding
- C707 (= C302) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
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.
- 757 binding
- 804:806 binding
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
25% identity, 81% coverage: 8:423/515 of query aligns to 5:420/485 of 4u3wA
Sites not aligning to the query:
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
28% identity, 63% coverage: 1:326/515 of query aligns to 1:319/484 of Q8NMB0
- N157 (= N159) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K184) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (≠ L206) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E265) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C302) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
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)
26% identity, 57% coverage: 10:304/515 of query aligns to 11:293/497 of P17202
- I28 (≠ F25) binding
- D96 (≠ E92) binding
- SPW 156:158 (≠ GAS 156:158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G169) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- K--PSE 182:185 (≠ KGHPSH 184:189) binding
- L186 (≠ T192) binding
- SSAT 236:239 (≠ SLKV 242:245) binding
- V251 (≠ P257) binding in other chain
- L258 (= L266) binding
- W285 (≠ M296) mutation to A: Decreases binding affinity for betaine aldehyde.
Sites not aligning to the query:
- 390 binding
- 441 A→I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- 450 C→S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- 456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
- 460 binding
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
28% identity, 55% coverage: 21:304/515 of query aligns to 27:294/494 of 4pz2B
- active site: N159 (= N159), K182 (= K184), E258 (= E265), C292 (= C302)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F155), I156 (≠ G156), P157 (≠ A157), W158 (≠ S158), N159 (= N159), M164 (≠ F164), K182 (= K184), A184 (≠ H186), E185 (≠ P187), G215 (≠ E221), G219 (≠ S225), F233 (= F239), T234 (= T240), G235 (= G241), S236 (= S242), V239 (= V245), E258 (= E265), L259 (= L266), C292 (= C302)
Sites not aligning to the query:
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)
28% identity, 59% coverage: 10:313/515 of query aligns to 64:351/535 of P51649
- C93 (≠ G40) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (≠ S123) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ M127) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ K129) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ A167) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C179) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KGHP 184:187) binding
- T233 (≠ H189) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A197) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S215) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S225) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSLKVG 241:246) binding
- R334 (≠ M296) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ G297) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C302) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S304) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 372 natural variant: N -> S
- 382 P → L: in SSADHD; 2% of activity
- 406 V → I: in dbSNP:rs143741652
- 409 G → D: in SSADHD; <1% of activity; dbSNP:rs118203984
- 498 binding ; S→A: Reduces catalytic activity to less than 15% of wild-type.
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
25% identity, 89% coverage: 10:467/515 of query aligns to 8:460/476 of 5x5uA
- active site: N151 (= N159), K174 (= K184), E249 (= E265), C283 (= C302), E380 (= E391), E457 (≠ H464)
- binding glycerol: D15 (≠ Q17), A16 (≠ S18), A17 (≠ E19), G19 (≠ S21)
- binding nicotinamide-adenine-dinucleotide: P149 (≠ A157), P207 (≠ E221), A208 (≠ P222), S211 (= S225), G227 (= G241), S228 (= S242), V231 (= V245), R329 (≠ S349), R330 (≠ I350), E380 (= E391), F382 (= F393)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
25% identity, 89% coverage: 10:467/515 of query aligns to 8:460/476 of 5x5tA
Query Sequence
>6937359 FitnessBrowser__SB2B:6937359
MTTDLCGRHFIAHEWHQSEASFTRFNPSTNSVLPGAFSQGTVVEVEAAAIAADAAFWEFQ
QTSADQKAKLLETMAKEIEQDGDAIVACAMLESGLPEARLKGELGRTAGQLRLFASVLRE
PYSPLLMDKANPDRQPLPKPELKLGQLPLGVVAVFGASNFPLAFSTAGGDTASALAAGCA
VIVKGHPSHPGTSELVARAMARAIDLTGMPKGLFSLIQGSEPALSVALVEHPLVKAVGFT
GSLKVGRLLADRCALRPEPIPFYGELGSVNPQLLLPGKLARDAAVLAEAQVNSMMMGHGQ
FCTSPGLVIAIKGPGLESYLAALSDIASRQNAAAMLSAGICQAFNQDVSILVPRVNVIAQ
GQAAEAAHHSRPLIASIEASALFGQPELLEEIFGPFALVAICDSKEEMFELVKRLPGQLT
GSIHGLETEVADFGDIIDRLAFKVGRIMFNQMPTGVEVARAMNHGGPYPASTDGRSTSVG
AEAMKRFMRPICYQNMPETLLPNELKASSRRLMMF
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