SitesBLAST
Comparing GFF3650 FitnessBrowser__Phaeo:GFF3650 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)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
46% identity, 98% coverage: 7:455/459 of query aligns to 8:454/459 of 3efvA
- active site: N134 (= N134), E231 (= E231), C265 (= C265), E439 (= E440)
- binding nicotinamide-adenine-dinucleotide: I130 (= I130), M131 (≠ Q131), P132 (= P132), W133 (= W133), N134 (= N134), Q139 (= Q139), R142 (= R142), K157 (= K157), A159 (= A159), N190 (≠ H190), V193 (≠ S193), T208 (= T208), G209 (= G209), S210 (= S210), A213 (= A213), E231 (= E231), L232 (= L232), G233 (= G233), C265 (= C265), E362 (= E362), F364 (= F364), F428 (= F429)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
39% identity, 99% coverage: 5:457/459 of query aligns to 2:452/453 of 4itbA
- active site: N130 (= N134), K153 (= K157), E227 (= E231), C261 (= C265), E358 (= E362), E435 (= E440)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (≠ I130), M127 (≠ Q131), P128 (= P132), W129 (= W133), N130 (= N134), K153 (= K157), A155 (= A159), S156 (= S160), A186 (≠ H190), V189 (≠ S193), G205 (= G209), S206 (= S210), A209 (= A213), S212 (≠ K216), L228 (= L232), C261 (= C265), E358 (= E362), F360 (= F364)
- binding 4-oxobutanoic acid: E227 (= E231), C261 (= C265), S418 (≠ A423)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
38% identity, 99% coverage: 5:457/459 of query aligns to 2:452/453 of 3vz3A
- active site: N130 (= N134), K153 (= K157), E227 (= E231), A261 (≠ C265), E358 (= E362), E435 (= E440)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (≠ I130), M127 (≠ Q131), W129 (= W133), N130 (= N134), Q135 (= Q139), R138 (= R142), K153 (= K157), A155 (= A159), S156 (= S160), A186 (≠ H190), V189 (≠ S193), T204 (= T208), G205 (= G209), S206 (= S210), A209 (= A213), E227 (= E231), L228 (= L232), G229 (= G233), A261 (≠ C265), F360 (= F364)
- binding 4-oxobutanoic acid: F131 (= F135), W134 (≠ Y138), S260 (≠ T264), A261 (≠ C265), I262 (= I266), S418 (≠ A423)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
37% identity, 98% coverage: 7:457/459 of query aligns to 4:453/455 of 4ywuA
- active site: N131 (= N134), K154 (= K157), E228 (= E231), C262 (= C265), E359 (= E362), E436 (= E440)
- binding 4-oxobutanoic acid: N131 (= N134), Q136 (= Q139), R139 (= R142), E228 (= E231), V261 (≠ T264), C262 (= C265), F425 (= F429)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
37% identity, 98% coverage: 7:457/459 of query aligns to 4:453/455 of 4ohtA
- active site: N131 (= N134), K154 (= K157), E228 (= E231), C262 (= C265), E359 (= E362), E436 (= E440)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (≠ I130), E128 (≠ Q131), P129 (= P132), W130 (= W133), K154 (= K157), H155 (= H158), A156 (= A159), S157 (= S160), Y187 (≠ H190), S207 (= S210), I214 (≠ V217)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
31% identity, 99% coverage: 3:457/459 of query aligns to 25:479/481 of 3jz4A
- active site: N156 (= N134), K179 (= K157), E254 (= E231), C288 (= C265), E385 (= E362), E462 (= E440)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P132), W155 (= W133), K179 (= K157), A181 (= A159), S182 (= S160), A212 (≠ H190), G216 (≠ S193), G232 (= G209), S233 (= S210), I236 (≠ A213), C288 (= C265), K338 (≠ D315), 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)
31% identity, 99% coverage: 3:457/459 of query aligns to 26:480/482 of P25526
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)
31% identity, 99% coverage: 2:457/459 of query aligns to 26:485/494 of P49189
- C116 (≠ I92) 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)
31% identity, 99% coverage: 2:457/459 of query aligns to 25:484/493 of 6vr6D
- active site: N156 (= N134), E253 (= E231), C287 (= C265), E467 (= E440)
- binding nicotinamide-adenine-dinucleotide: I152 (= I130), G153 (≠ Q131), W155 (= W133), K179 (= K157), A212 (≠ H190), G215 (≠ S193), Q216 (≠ D194), F229 (≠ L207), G231 (= G209), S232 (= S210), T235 (≠ A213), I239 (≠ V217)
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)
30% identity, 99% coverage: 3:455/459 of query aligns to 23:482/497 of P17202
- I28 (≠ V8) binding
- D96 (≠ E74) binding
- SPW 156:158 (≠ QPW 131:133) binding
- Y160 (≠ F135) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R142) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAS 157:160) binding
- L186 (≠ N161) binding
- SSAT 236:239 (≠ SDGA 210:213) binding
- V251 (= V225) binding in other chain
- L258 (= L232) binding
- W285 (≠ Y259) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E362) binding
- A441 (≠ M414) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A423) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F429) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K433) binding
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
32% identity, 99% coverage: 4:459/459 of query aligns to 21:476/476 of 5x5uA
- active site: N151 (= N134), K174 (= K157), E249 (= E231), C283 (= C265), E380 (= E362), E457 (= E440)
- binding nicotinamide-adenine-dinucleotide: P149 (= P132), P207 (≠ S189), A208 (≠ H190), S211 (= S193), G227 (= G209), S228 (= S210), V231 (≠ A213), R329 (≠ D311), R330 (≠ L312), E380 (= E362), F382 (= F364)
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
32% identity, 99% coverage: 4:459/459 of query aligns to 21:476/476 of 5x5tA
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
30% identity, 99% coverage: 3:455/459 of query aligns to 21:480/495 of 4v37A
- active site: N157 (= N134), K180 (= K157), E255 (= E231), A289 (≠ C265), E388 (= E362), E465 (= E440)
- binding 3-aminopropan-1-ol: C448 (≠ A423), W454 (≠ F429)
- binding nicotinamide-adenine-dinucleotide: I153 (= I130), S154 (≠ Q131), P155 (= P132), W156 (= W133), N157 (= N134), M162 (≠ Q139), K180 (= K157), S182 (≠ A159), E183 (≠ S160), G213 (≠ S189), G217 (≠ S193), A218 (≠ D194), T232 (= T208), G233 (= G209), S234 (= S210), T237 (≠ A213), E255 (= E231), L256 (= L232), A289 (≠ C265), E388 (= E362), F390 (= F364)
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)
30% identity, 99% coverage: 1:455/459 of query aligns to 21:485/503 of Q8VWZ1
- N27 (≠ T7) binding
- I28 (≠ V8) binding
- D99 (≠ E74) binding
- L189 (≠ N161) binding
- 238:245 (vs. 209:216, 50% identical) binding
- C294 (= C265) binding
- E393 (= E362) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
30% identity, 99% coverage: 1:455/459 of query aligns to 16:480/497 of 3iwkH
- active site: N157 (= N134), K180 (= K157), E255 (= E231), C289 (= C265), E388 (= E362), E465 (= E440)
- binding nicotinamide-adenine-dinucleotide: W156 (= W133), G213 (≠ S189), G217 (≠ S193), A218 (≠ D194), G233 (= G209), S234 (= S210), T237 (≠ A213), K240 (= K216), C289 (= C265), Q336 (≠ L312), E388 (= E362), F390 (= F364)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
29% identity, 98% coverage: 8:457/459 of query aligns to 12:475/494 of 5izdA
- active site: N149 (= N134), K172 (= K157), E247 (= E231), C281 (= C265), E381 (= E362), E458 (= E440)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I130), T146 (≠ Q131), W148 (= W133), K172 (= K157), P173 (≠ H158), S174 (≠ A159), S175 (= S160), R204 (≠ I188), G205 (≠ S189), G209 (≠ S193), D210 (= D194), G225 (= G209), S226 (= S210), T229 (≠ A213)
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)
32% identity, 99% coverage: 4:457/459 of query aligns to 23:481/490 of Q9HTJ1
- GAWN 150:153 (≠ QPWN 131:134) binding
- K162 (≠ Y143) active site, Charge relay system
- KPSE 176:179 (≠ KHAS 157:160) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ SDGA 210:213) binding
- E252 (= E231) active site, Proton acceptor
- C286 (= C265) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E362) binding
- E464 (= E440) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
32% identity, 99% coverage: 4:457/459 of query aligns to 22:480/489 of 4cazA
- active site: N152 (= N134), K175 (= K157), E251 (= E231), C285 (= C265), E386 (= E362), E463 (= E440)
- 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 (= I130), G149 (≠ Q131), W151 (= W133), N152 (= N134), K175 (= K157), E178 (≠ S160), G208 (vs. gap), G212 (≠ S193), F226 (≠ L207), T227 (= T208), G228 (= G209), G229 (≠ S210), T232 (≠ A213), V236 (= V217), E251 (= E231), L252 (= L232), C285 (= C265), E386 (= E362), F388 (= F364)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
32% identity, 99% coverage: 4:457/459 of query aligns to 22:480/489 of 2woxA
- active site: N152 (= N134), K175 (= K157), E251 (= E231), C285 (= C265), E386 (= E362), E463 (= E440)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I130), G149 (≠ Q131), W151 (= W133), N152 (= N134), K175 (= K157), S177 (≠ A159), E178 (≠ S160), G208 (vs. gap), G212 (≠ S193), F226 (≠ L207), T227 (= T208), G228 (= G209), G229 (≠ S210), T232 (≠ A213), V236 (= V217), E251 (= E231), L252 (= L232), C285 (= C265), E386 (= E362), F388 (= F364)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
32% identity, 99% coverage: 4:457/459 of query aligns to 22:480/489 of 2wmeA
- active site: N152 (= N134), K175 (= K157), E251 (= E231), C285 (= C265), E386 (= E362), E463 (= E440)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ Q131), W151 (= W133), K175 (= K157), S177 (≠ A159), E178 (≠ S160), G208 (vs. gap), G212 (≠ S193), F226 (≠ L207), G228 (= G209), G229 (≠ S210), T232 (≠ A213), V236 (= V217)
Query Sequence
>GFF3650 FitnessBrowser__Phaeo:GFF3650
MSDTVTTVNPTTGKTLDTYNVLSGKALEDAVQRCHNAFLDWRLTSVEDRANTIKAIGAAL
RDRKDELAELMTKEMGKLLKQSHQEIDLCAAICDYSAAEAPAAFAPEERDIEGGEKGHIF
YSPIGVVYGIQPWNFPAYQVVRYSIASLIAGNGVLLKHASNVTGSGQMLQEIYEAAGLPK
GLFQALVISHDQSDTLISHDLVRGVTLTGSDGAGRKVGAKAAEAVKKTVLELGSNDAYIV
LEDADIDAAVQTCVTGRTYNNGETCIAAKRFIVVDAIYNQFRDAYVAAMKRVTLGDPMGE
DADIGPMARKDLRDDLHQQVKDSLEGGAKLLCGGEMPDTDGFFYPATVLENVAPGQPAYD
DELFGPVAALIRAQDADDAMRIANDSRFGLGGGIMTKDTEKALALARDYFDTGMVFINGF
GLAIPNMPFGGVKDSGYGREHGGFGMKEFVNVKSVMVMS
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