SitesBLAST
Comparing Pf1N1B4_5978 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5978 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)
45% identity, 94% coverage: 26:521/526 of query aligns to 9:503/504 of 1eyyA
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
28% identity, 86% coverage: 4:455/526 of query aligns to 1:437/486 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
28% identity, 80% coverage: 9:430/526 of query aligns to 9:423/489 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)
28% identity, 80% coverage: 9:430/526 of query aligns to 9:423/489 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)
28% identity, 80% coverage: 9:430/526 of query aligns to 9:423/489 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)
28% identity, 80% coverage: 9:430/526 of query aligns to 10:424/490 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
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
26% identity, 76% coverage: 8:406/526 of query aligns to 3:391/482 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 (≠ A221), 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+
26% identity, 76% coverage: 8:406/526 of query aligns to 3:391/482 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:
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
25% identity, 76% coverage: 8:406/526 of query aligns to 10:398/490 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 (= N336), R333 (≠ G338), Q334 (≠ T339)
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
28% identity, 77% coverage: 26:430/526 of query aligns to 20:422/481 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 (vs. gap), G216 (= G224), G232 (= G240), S233 (= S241), I236 (≠ G244), C288 (= C301), K338 (≠ A349), 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)
28% identity, 77% coverage: 26:430/526 of query aligns to 21:423/482 of P25526
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
27% identity, 71% coverage: 63:435/526 of query aligns to 70:441/503 of Q84LK3
- N162 (= N160) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ G170) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
26% identity, 73% coverage: 44:429/526 of query aligns to 44:418/454 of 3ty7B
Sites not aligning to the query:
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)
26% identity, 79% coverage: 7:423/526 of query aligns to 6:409/475 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:
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 79% coverage: 7:423/526 of query aligns to 5:408/474 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:
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, 79% coverage: 7:423/526 of query aligns to 11:423/487 of Q9H2A2
- R109 (≠ Q116) 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.
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 79% coverage: 7:423/526 of query aligns to 5:408/474 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:
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
28% identity, 73% coverage: 39:423/526 of query aligns to 35:420/485 of 4u3wA
Sites not aligning to the query:
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
30% identity, 55% coverage: 12:302/526 of query aligns to 514:787/983 of 3hazA
- active site: N652 (= N160), K675 (= K185), E752 (= E264), C786 (= C301)
- binding nicotinamide-adenine-dinucleotide: I648 (≠ F156), S649 (≠ G157), P650 (≠ A158), W651 (≠ S159), N652 (= N160), I657 (≠ F165), K675 (= K185), P676 (≠ A186), A677 (≠ H187), G708 (= G222), G711 (= G224), A712 (≠ E225), T726 (= T239), G727 (= G240), S728 (= S241), V731 (≠ G244), I735 (≠ L248), E752 (= E264), T753 (≠ M265), C786 (= C301)
Sites not aligning to the query:
- active site: 878, 960
- binding flavin-adenine dinucleotide: 272, 273, 306, 333, 335, 336, 337, 338, 339, 340, 358, 359, 360, 361, 364, 387, 388, 389, 390, 435, 460, 461
- binding nicotinamide-adenine-dinucleotide: 878, 880, 948
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
25% identity, 69% coverage: 44:407/526 of query aligns to 42:399/489 of 4o6rA
- active site: N150 (= N160), K173 (= K185), E248 (= E264), C282 (= C301), E383 (= E391)
- binding adenosine monophosphate: I146 (≠ F156), V147 (≠ G157), K173 (= K185), G206 (= G220), G210 (= G224), Q211 (≠ E225), F224 (= F238), G226 (= G240), S227 (= S241), T230 (≠ G244), R233 (≠ A247)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_5978 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5978
MPEIIGHNYIGGARSAAGNIAMQSHDASTGEALPFSFMQATAEEVDAAAQAAAAAYPAFR
NLPATRRAEFLEAIATQLDALDDEFVALVTRETALPTGRIQGERNRTSGQMRLFAQVLRR
GDFYGARIDRALPERLPLPRVDLRQYRIGVGPVAVFGASNFPLAFSTAGGDTAAALAAGC
PVVFKAHSGHMATAEHVADAIIRAAEQTDMPKGVFNMIYGAGVGEALVKHPAIQAVGFTG
SLKGGRALCDMAAARPQPIPVFAEMSSINPVLVLPEALLARGEKIAGELVASVVQGCGQF
CTNPGLVIGMRSPHFSAFIARLSALMTEQPAQTMLNAGTLGSYEKGVQALLDHPRIIRLA
GQDRHGNQAQPQLFKADVSLLLKGDPLLQEEVFGPTTLVVEVADKAELRQALNSLHGQLT
ATLIGEAQDLKEHADLLVLLEQKVGRVLFNGYPTGVEVCDAMVHGGPYPATSDARGTSVG
SLAIERFLRPVCYQNCPDALLPDALKNANPLGIARLIDGNSHREPV
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