SitesBLAST
Comparing Pf1N1B4_3385 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3385 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)
44% identity, 94% coverage: 26:520/526 of query aligns to 9:502/504 of 1eyyA
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)
27% 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:
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)
27% identity, 70% coverage: 39:407/526 of query aligns to 44:402/484 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 (≠ K207) 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)
27% identity, 75% coverage: 7:402/526 of query aligns to 5:387/474 of 2esdA
- active site: N153 (= N160), K176 (= K185), A249 (≠ P260), 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 (≠ A339), S329 (≠ L340), Y332 (= Y343)
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
26% identity, 76% coverage: 9:406/526 of query aligns to 9:403/489 of 4cazA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E386 (= E391)
- 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), E386 (= E391), F388 (= F393)
Sites not aligning to the query:
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
26% identity, 76% coverage: 9:406/526 of query aligns to 9:403/489 of 2woxA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E386 (= E391)
- 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), E386 (= E391), F388 (= F393)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
26% identity, 76% coverage: 9:406/526 of query aligns to 9:403/489 of 2wmeA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E386 (= E391)
- 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)
26% identity, 76% coverage: 9:406/526 of query aligns to 10:404/490 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)
- E387 (= E391) binding
Sites not aligning to the query:
- 464 active site, Charge relay system
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
27% identity, 75% coverage: 7:402/526 of query aligns to 5:387/474 of 1qi1B
- active site: N153 (= N160), K176 (= K185), E249 (= E264), S283 (≠ C301), E376 (= E391)
- binding sn-glycerol-3-phosphate: Y154 (≠ F161), R282 (≠ F300), S283 (≠ C301), T284 (= T302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (≠ A158), F152 (≠ S159), N153 (= N160), L158 (≠ T167), K176 (= K185), P178 (≠ H187), T179 (≠ S188), G209 (= G222), G213 (= G224), G229 (= G240), S230 (= S241), I233 (≠ G244), E249 (= E264), L250 (≠ M265), S283 (≠ C301)
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)
24% identity, 80% coverage: 4:423/526 of query aligns to 8:423/487 of Q9H2A2
- R109 (≠ K116) 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.
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
24% identity, 81% coverage: 8:432/526 of query aligns to 10:426/490 of 5ekcE
- active site: N154 (= N160), K177 (= K185), E252 (= E264), C286 (= C301), E381 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (≠ F156), T151 (≠ G157), P152 (≠ A158), W153 (≠ S159), K177 (= K185), S180 (= S188), G210 (= G222), G214 (= G224), F228 (= F238), G230 (= G240), E231 (≠ S241), T234 (≠ G244), N331 (vs. gap), R333 (vs. gap), Q334 (vs. gap)
Sites not aligning to the query:
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
24% identity, 81% coverage: 8:432/526 of query aligns to 3:419/482 of 5ek6A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301), E374 (= E391)
- binding 2-methylpropanal: I152 (≠ F165), K155 (≠ A168), T222 (= T239), E245 (= E264)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F156), T144 (≠ G157), W146 (≠ S159), N147 (= N160), I152 (≠ F165), K170 (= K185), A172 (≠ H187), S173 (= S188), P202 (≠ G221), G203 (= G222), G207 (= G224), F221 (= F238), T222 (= T239), G223 (= G240), E224 (≠ S241), T227 (≠ G244), I231 (≠ L248), E245 (= E264), L246 (≠ M265), C279 (= C301), E374 (= E391)
Sites not aligning to the query:
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
24% identity, 81% coverage: 8:432/526 of query aligns to 3:419/482 of 4h73A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301), E374 (= E391)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F156), T144 (≠ G157), P145 (≠ A158), W146 (≠ S159), K170 (= K185), A172 (≠ H187), S173 (= S188), G203 (= G222), G207 (= G224), F221 (= F238), G223 (= G240), E224 (≠ S241), T227 (≠ G244)
Sites not aligning to the query:
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
26% identity, 70% coverage: 35:404/526 of query aligns to 33:391/480 of 3rhhD
- active site: N155 (= N160), K178 (= K185), E251 (= E264), C285 (= C301), E378 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ F156), P153 (≠ A158), F154 (≠ S159), K178 (= K185), P179 (vs. gap), A180 (= A186), T181 (≠ H187), G211 (= G222), G215 (= G224), D216 (≠ E225), F229 (= F238), G231 (= G240), G232 (≠ S241), T235 (≠ G244)
Sites not aligning to the query:
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
25% identity, 76% coverage: 8:408/526 of query aligns to 5:404/483 of 4npiA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), W160 (≠ G170), E251 (= E264), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), K175 (= K185), E178 (≠ S188), G208 (= G222), G213 (= G224), E214 (= E225), F227 (= F238), G229 (= G240), E230 (≠ S241), T233 (≠ G244), G253 (≠ S266), C285 (= C301), K335 (vs. gap), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
25% identity, 76% coverage: 8:408/526 of query aligns to 5:404/483 of 4i2rA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), F227 (= F238), T228 (= T239), G229 (= G240), E230 (≠ S241), T233 (≠ G244), E251 (= E264), L252 (≠ M265), G253 (≠ S266), C285 (= C301), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
25% identity, 76% coverage: 8:408/526 of query aligns to 5:404/483 of 4i25A
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), G213 (= G224), F227 (= F238), T228 (= T239), G229 (= G240), E230 (≠ S241), T233 (≠ G244), E251 (= E264), L252 (≠ M265), C285 (= C301), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
25% identity, 76% coverage: 8:408/526 of query aligns to 5:404/483 of 5kllA
- active site: D152 (≠ N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R106), D152 (≠ N160), L157 (≠ F165), W160 (≠ G170), C285 (= C301)
Sites not aligning to the query:
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
25% identity, 76% coverage: 8:408/526 of query aligns to 6:405/484 of 5kj5B
- active site: D153 (≠ N160), K176 (= K185), E252 (= E264), C286 (= C301), E388 (= E391)
- binding nicotinamide-adenine-dinucleotide: I149 (≠ F156), S150 (≠ G157), P151 (≠ A158), W152 (≠ S159), D153 (≠ N160), L158 (≠ F165), K176 (= K185), G209 (= G222), K210 (vs. gap), G214 (= G224), F228 (= F238), T229 (= T239), G230 (= G240), E231 (≠ S241), T234 (≠ G244), E252 (= E264), L253 (≠ M265), C286 (= C301), E388 (= E391), F390 (= F393)
Sites not aligning to the query:
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
26% identity, 76% coverage: 8:408/526 of query aligns to 5:404/483 of 4ou2A
- active site: N152 (= N160), K175 (= K185), A251 (= A263), C285 (= C301), E387 (= E391)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), N152 (= N160), K175 (= K185), G208 (= G222), G213 (= G224), E214 (= E225), F227 (= F238), T228 (= T239), G229 (= G240), E230 (≠ S241), T233 (≠ G244), A251 (= A263), L252 (≠ E264), G253 (≠ M265), C285 (= C301), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_3385 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3385
MTTLLGHNYIGGGRSANGTLQLQSLDASTGDALPGTFFQATEAEVDAAAKAAAAAYPVYR
NLSAEKRARFLDAIADEIDALGEDFIATVCRETALPAGRIQGERARTSGQMRLFAKVLRR
GDFYGARIDRALPDRQPLPRPDLRQYRIALGPVAVFGASNFPLAFSTAGGDTASALAAGC
PVVFKAHSGHMATAEWVADAIIRAAEKTEMPAGVYNMIYGGGVGEWLVKHPAIQAVGFTG
SLKGGNALSHMAATRPQPIPVFAEMSSINPVFLLPEALAVRCEQIGAQLAGSVTLGCGQF
CTNPGLVIGLRSPQFSTFLEMFCASMNQQPPQTMLNAGALASYSKGLVELHEHPGLTHLA
GKPQQGNQAQPQVFQADVSLLLKGDELLQEEVFGPTTIVIEVEDRAQLTAALHGLRGQLT
ATLIGEADELLEYRWLAELLQEKVGRILLNGYPTGVEVCEAMVHGGPYPATSDSRGTSVG
TLAIDRFLRPVCFQNYPDALLPQALQNANPLGIRRLVDGEVSQLAL
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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