SitesBLAST
Comparing Pf6N2E2_859 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_859 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
47% identity, 95% coverage: 21:519/526 of query aligns to 4:501/504 of 1eyyA
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
28% identity, 85% coverage: 8:455/526 of query aligns to 5:437/486 of 3ju8A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301), E377 (= E391)
- binding nicotinamide-adenine-dinucleotide: G144 (= G157), Y146 (≠ S159), N147 (= N160), L152 (≠ F165), K170 (= K185), S172 (≠ H187), F220 (= F238), T221 (= T239), G222 (= G240), S223 (= S241), T226 (≠ G244), E245 (= E264), M246 (= M265), G247 (≠ S266), C279 (= C301), E377 (= E391), F379 (= F393)
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
29% identity, 64% coverage: 9:343/526 of query aligns to 9:330/489 of 4cazA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301)
- 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 (≠ F156), G149 (= G157), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), G212 (= G224), F226 (= F238), T227 (= T239), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248), E251 (= E264), L252 (≠ M265), C285 (= C301)
Sites not aligning to the query:
- active site: 386, 463
- 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: 386, 388
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
29% identity, 64% coverage: 9:343/526 of query aligns to 9:330/489 of 2woxA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F156), G149 (= G157), W151 (≠ S159), N152 (= N160), K175 (= K185), S177 (≠ H187), E178 (≠ S188), G208 (= G222), G212 (= G224), F226 (= F238), T227 (= T239), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248), E251 (= E264), L252 (≠ M265), C285 (= C301)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
29% identity, 64% coverage: 9:343/526 of query aligns to 9:330/489 of 2wmeA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G157), W151 (≠ S159), K175 (= K185), S177 (≠ H187), E178 (≠ S188), G208 (= G222), G212 (= G224), F226 (= F238), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248)
Sites not aligning to the query:
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)
29% identity, 64% coverage: 9:343/526 of query aligns to 10:331/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 157:160) binding
- K162 (≠ D171) active site, Charge relay system
- KPSE 176:179 (≠ KAHS 185:188) binding
- G209 (= G222) binding
- GTST 230:233 (≠ SLKG 241:244) binding
- E252 (= E264) active site, Proton acceptor
- C286 (= C301) binding covalent; modified: Cysteine sulfenic acid (-SOH)
Sites not aligning to the query:
- 387 binding
- 464 active site, Charge relay system
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
30% identity, 61% coverage: 4:324/526 of query aligns to 2:306/488 of 5u0mA
- active site: N148 (= N160), K171 (= K185), E246 (= E264), C280 (= C301)
- binding nicotinamide-adenine-dinucleotide: F144 (= F156), Y147 (≠ S159), N148 (= N160), K171 (= K185), S173 (≠ H187), E174 (≠ S188), G207 (= G224), T222 (= T239), G223 (= G240), S224 (= S241), V227 (≠ G244), E246 (= E264), M247 (= M265), G248 (≠ S266), C280 (= C301)
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)
30% identity, 61% coverage: 4:324/526 of query aligns to 2:306/488 of 5u0lA
Sites not aligning to the query:
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
26% identity, 88% coverage: 8:468/526 of query aligns to 29:490/515 of 2d4eC
- active site: N173 (= N160), K196 (= K185), E271 (= E264), C305 (= C301), E409 (= E391), E486 (≠ H464)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F156), T170 (≠ G157), P171 (≠ A158), W172 (≠ S159), K196 (= K185), A198 (≠ H187), G229 (= G222), G233 (= G224), A234 (≠ E225), T248 (= T239), G249 (= G240), E250 (≠ S241), T253 (≠ G244), E271 (= E264), L272 (≠ M265), C305 (= C301), E409 (= E391), F411 (= F393), F475 (vs. gap)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
28% identity, 77% coverage: 24:426/526 of query aligns to 25:420/489 of 6wsbA
- active site: N152 (= N160), E250 (= E264), C284 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), G149 (= G157), A150 (= A158), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), G211 (= G224), A212 (≠ E225), F225 (= F238), T226 (= T239), G227 (= G240), G228 (≠ S241), T231 (≠ G244), V235 (≠ L248), E250 (= E264), L251 (≠ M265), G252 (≠ S266), C284 (= C301), E385 (= E391), F387 (= F393)
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
27% identity, 71% coverage: 42:413/526 of query aligns to 46:407/481 of 3jz4A
- active site: N156 (= N160), K179 (= K185), E254 (= E264), C288 (= C301), E385 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A158), W155 (≠ S159), K179 (= K185), A181 (≠ H187), S182 (= S188), A212 (≠ G222), G216 (= G224), G232 (= G240), S233 (= S241), I236 (≠ G244), C288 (= C301), K338 (vs. gap), E385 (= E391), F387 (= F393)
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)
27% identity, 71% coverage: 42:413/526 of query aligns to 47:408/482 of P25526
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
25% identity, 73% coverage: 44:429/526 of query aligns to 44:418/454 of 3ty7B
Sites not aligning to the query:
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
25% identity, 80% coverage: 2:423/526 of query aligns to 6:423/487 of Q9H2A2
- R109 (= R106) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N160) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
25% identity, 75% coverage: 7:402/526 of query aligns to 6:388/475 of Q59931
- R103 (= R106) binding
- S151 (≠ G157) binding
- K177 (= K185) binding
- T180 (≠ S188) binding
- D215 (≠ E225) binding
- 230:251 (vs. 240:265, 31% identical) binding
- E377 (= E391) binding
Sites not aligning to the query:
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
30% identity, 47% coverage: 7:253/526 of query aligns to 5:243/485 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)
24% identity, 84% coverage: 7:450/526 of query aligns to 12:441/484 of Q8NMB0
- N157 (= N160) 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 (= K185) 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 (≠ R207) 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 (= E264) 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 (= C301) 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.
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 69% coverage: 41:402/526 of query aligns to 37:387/474 of 2esdA
- active site: N153 (= N160), K176 (= K185), A249 (≠ E264), C283 (= C301), E376 (= E391)
- binding glyceraldehyde-3-phosphate: R102 (= R106), Y154 (≠ F161), R282 (≠ F300), C283 (= C301), T284 (= T302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ S159), K176 (= K185), P178 (≠ H187), T179 (≠ S188), G209 (= G222), G213 (= G224), D214 (≠ E225), F227 (= F238), S230 (= S241), I233 (≠ G244), K328 (≠ T339), S329 (≠ L340), Y332 (= Y343)
Sites not aligning to the query:
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
25% identity, 85% coverage: 7:455/526 of query aligns to 2:438/476 of 4yweA
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)
26% identity, 66% coverage: 56:401/526 of query aligns to 109:448/535 of P51649
- G176 (= G125) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (vs. gap) to Y: 83% of activity; dbSNP:rs2760118
- P182 (vs. gap) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ A168) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C180) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KP-------AE 228:231 (≠ KAHSGHMATAE 185:195) binding
- T233 (≠ V197) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A198) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N216) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G224) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSLKGG 240:245) binding
- R334 (≠ Q295) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ G296) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (vs. gap) modified: Disulfide link with 342, In inhibited form
- C342 (= C301) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ A324) natural variant: N -> S
- P382 (≠ T333) to L: in SSADHD; 2% of activity
- V406 (= V357) to I: in dbSNP:rs143741652
- G409 (≠ A360) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
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
- 498 binding ; S→A: Reduces catalytic activity to less than 15% of wild-type.
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
Query Sequence
>Pf6N2E2_859 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_859
MSLITGQNFIGGQRSAAGTIIVKSVDASTGETLPYAFHQATAQEVENAAHAAHHAFSSYR
TLSASKRAEFLDAIAQELEALDDEFIALVCRETALPVARIQGERARTSGQMRLFANVLRR
GDFYGARIDQALPLRKPLPRPDLRQYRTAIGPVAVFGASNFPLAFSTAGGDTASALAAGC
PVVFKAHSGHMATAEQVANAIIRAAERSGMPAGVFNMIYGSGVGEALVKHPLIKGVGFTG
SLKGGRALCDMAAARPEPIPVFAEMSSINPVVILPHALSRRADSIAHDLAASVVQGCGQF
CTNPGLVVGIRSDAFTAFQDRVAALMNDQPAQTMLNAGTLRSYAAGLQNLHAHPGIVHLA
GSDQQAHQAQPQLFKADVELLLNGDKVLQEEIFGPTSIFIEVADQAQLSAAINALRGQLT
ATLIGEPEDLTQFTELTALLEMKVGRILINGYPTGVEVCDSMVHGGPYPATSDSRGTSVG
TLAIDRFLRPVCFQNYPDALLPDALKNANPLNISRLVDGCLSRDRL
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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