SitesBLAST
Comparing Pf1N1B4_4153 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4153 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)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
39% identity, 94% coverage: 12:250/254 of query aligns to 5:253/255 of 5itvA
- active site: G18 (= G25), S141 (= S143), Y154 (= Y156), K158 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G21), S17 (= S24), G18 (= G25), I19 (= I26), D38 (= D45), I39 (= I46), T61 (≠ A63), I63 (= I65), N89 (= N91), G91 (= G93), T139 (≠ I141), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (≠ V186), G185 (= G187), I186 (≠ V189), I187 (≠ V190)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
38% identity, 95% coverage: 10:250/254 of query aligns to 6:251/258 of 4wecA
- active site: G21 (= G25), S143 (= S143), Q154 (≠ A154), Y157 (= Y156), K161 (= K160)
- binding nicotinamide-adenine-dinucleotide: G17 (= G21), A19 (= A23), S20 (= S24), G21 (= G25), I22 (= I26), D41 (= D45), I42 (= I46), V61 (≠ L61), D62 (= D64), V63 (≠ I65), N89 (= N91), T141 (≠ I141), Y157 (= Y156), K161 (= K160), P187 (≠ V186), P189 (≠ D188), V190 (= V189)
5itvD Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
39% identity, 94% coverage: 12:250/254 of query aligns to 5:225/227 of 5itvD
- active site: G18 (= G25), S141 (= S143), Y154 (= Y156), K158 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G21), S17 (= S24), G18 (= G25), I19 (= I26), D38 (= D45), I39 (= I46), T61 (≠ A63), D62 (= D64), I63 (= I65), N89 (= N91), T139 (≠ I141), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (≠ V186), G185 (= G187), I187 (≠ V189)
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
38% identity, 94% coverage: 12:251/254 of query aligns to 3:239/240 of 4dmmB
- active site: G16 (= G25), S142 (= S143), Q152 (≠ I153), Y155 (= Y156), K159 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G21), S14 (≠ A23), R15 (≠ S24), G16 (= G25), I17 (= I26), A37 (≠ I46), S38 (≠ N47), S39 (≠ P48), A62 (= A63), D63 (= D64), V64 (≠ I65), N90 (= N91), A91 (= A92), L113 (≠ V114), I140 (= I141), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (≠ V186), G186 (= G187), I188 (≠ V189), T190 (= T191), M192 (≠ I193)
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
35% identity, 94% coverage: 11:250/254 of query aligns to 10:257/267 of 3ay6B
- active site: G24 (= G25), S151 (= S143), Y164 (= Y156), K168 (= K160)
- binding beta-D-glucopyranose: E102 (≠ I95), S151 (= S143), H153 (≠ A145), W158 (≠ F150), Y164 (= Y156), N202 (≠ L194), K205 (≠ V197)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G21), T23 (≠ S24), G24 (= G25), L25 (≠ I26), Y45 (≠ I46), D71 (= D64), V72 (≠ I65), N98 (= N91), A99 (= A92), G100 (= G93), V101 (≠ I94), M149 (≠ I141), S151 (= S143), Y164 (= Y156), K168 (= K160), P194 (≠ V186), G195 (= G187), M197 (≠ V189), T199 (= T191), P200 (≠ N192), I201 (= I193), N202 (≠ L194)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
38% identity, 93% coverage: 14:250/254 of query aligns to 5:246/248 of 6ixmC
- active site: G16 (= G25), S142 (= S143), Y155 (= Y156), K159 (= K160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G21), S15 (= S24), G16 (= G25), I17 (= I26), D36 (= D45), I37 (= I46), A61 (= A63), D62 (= D64), T63 (≠ I65), N89 (= N91), A90 (= A92), M140 (≠ I141), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (≠ V186), A186 (≠ G187), Y187 (≠ D188), I188 (≠ V189), L192 (≠ I193)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
35% identity, 93% coverage: 15:250/254 of query aligns to 8:251/261 of 1g6kA
- active site: G18 (= G25), S145 (= S143), Y158 (= Y156), K162 (= K160)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S24), G18 (= G25), L19 (≠ I26), R39 (vs. gap), D65 (= D64), V66 (≠ I65), N92 (= N91), A93 (= A92), G94 (= G93), M143 (≠ I141), S145 (= S143), Y158 (= Y156), P188 (≠ V186), G189 (= G187), I191 (≠ V189), T193 (= T191)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
35% identity, 93% coverage: 15:250/254 of query aligns to 8:251/261 of P40288
- 11:35 (vs. 18:42, 32% identical) binding
- E96 (≠ I95) mutation E->A,G,K: Heat stable.
- D108 (= D107) mutation to N: Heat stable.
- V112 (≠ I111) mutation to A: Heat stable.
- E133 (≠ P132) mutation to K: Heat stable.
- V183 (= V181) mutation to I: Heat stable.
- P194 (≠ N192) mutation to Q: Heat stable.
- E210 (≠ G209) mutation to K: Heat stable.
- Y217 (≠ R216) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
37% identity, 93% coverage: 15:249/254 of query aligns to 6:237/239 of 4nbtA
- active site: G16 (= G25), S132 (= S143), Y145 (= Y156), K149 (= K160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G21), K15 (≠ S24), G16 (= G25), L17 (≠ I26), D36 (= D45), L37 (≠ I46), L52 (≠ A63), N53 (≠ D64), V54 (≠ I65), N80 (= N91), A81 (= A92), G82 (= G93), I130 (= I141), S132 (= S143), Y145 (= Y156), K149 (= K160), P177 (≠ V186), G178 (= G187), I180 (≠ V189), T182 (= T191)
P0A2C9 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 93% coverage: 15:249/254 of query aligns to 6:241/244 of P0A2C9
- M125 (= M130) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A231) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S232) mutation to F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226.
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
42% identity, 74% coverage: 63:250/254 of query aligns to 61:251/253 of 4ituA
- active site: N113 (= N115), S141 (= S143), Y154 (= Y156), K158 (= K160)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S143), Y154 (= Y156), T186 (≠ D188), R209 (≠ H208), Y213 (≠ A212)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D62 (= D64), V63 (≠ I65), N89 (= N91), V112 (= V114), F139 (≠ I141), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (≠ V186), T186 (≠ D188), V187 (= V189), T190 (≠ N192), M192 (≠ L194)
Sites not aligning to the query:
A7IQH5 2-(S)-hydroxypropyl-CoM dehydrogenase 3; S-HPCDH 3; 2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3; Aliphatic epoxide carboxylation component IV; Epoxide carboxylase component IV; SHPCDH3; EC 1.1.1.269 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 2 papers)
42% identity, 74% coverage: 63:250/254 of query aligns to 63:253/255 of A7IQH5
- DV 64:65 (≠ DI 64:65) binding
- N91 (= N91) binding
- S143 (= S143) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y156) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K160) binding ; mutation to A: Loss of activity.
- T188 (≠ D188) binding
- VTSTG 189:193 (≠ VVTNI 189:193) binding
- R211 (≠ H208) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- K214 (≠ A211) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- Y215 (≠ A212) binding
Sites not aligning to the query:
P50162 Tropinone reductase 1; Tropine dehydrogenase; Tropinone reductase I; TR-I; EC 1.1.1.206 from Datura stramonium (Jimsonweed) (Common thornapple) (see paper)
31% identity, 100% coverage: 1:254/254 of query aligns to 8:272/273 of P50162
- 25:49 (vs. 18:42, 52% identical) binding
- S158 (= S143) binding
- Y171 (= Y156) active site, Proton acceptor
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
38% identity, 93% coverage: 15:249/254 of query aligns to 6:241/244 of 6t77A
- active site: G16 (= G25), S138 (= S143), Y151 (= Y156)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G21), S14 (≠ A23), R15 (≠ S24), T37 (vs. gap), L58 (≠ A63), N59 (≠ D64), V60 (≠ I65), A87 (= A92), G88 (= G93), I89 (= I94)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
38% identity, 93% coverage: 15:249/254 of query aligns to 5:240/243 of 1q7bA
- active site: G15 (= G25), E101 (≠ D107), S137 (= S143), Q147 (≠ I153), Y150 (= Y156), K154 (= K160)
- binding calcium ion: E232 (≠ S241), T233 (≠ V242)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G21), S13 (≠ A23), R14 (≠ S24), T36 (vs. gap), N58 (≠ D64), V59 (≠ I65), N85 (= N91), A86 (= A92), G87 (= G93), I88 (= I94), S137 (= S143), Y150 (= Y156), K154 (= K160), P180 (≠ V186), G181 (= G187), I183 (≠ V189)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
40% identity, 93% coverage: 15:250/254 of query aligns to 3:248/250 of 2cfcA
- active site: G13 (= G25), S142 (= S143), Y155 (= Y156), K159 (= K160)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (= F150), R152 (≠ I153), Y155 (= Y156), W195 (≠ H196), R196 (≠ V197)
- binding nicotinamide-adenine-dinucleotide: G9 (= G21), S12 (= S24), G13 (= G25), N14 (≠ I26), D33 (= D45), L34 (≠ I46), A59 (= A63), D60 (= D64), V61 (≠ I65), N87 (= N91), A88 (= A92), G89 (= G93), I140 (= I141), P185 (≠ V186), G186 (= G187), M187 (≠ D188), I188 (≠ V189), T190 (= T191), P191 (≠ N192), M192 (≠ I193), T193 (≠ L194)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
40% identity, 93% coverage: 15:250/254 of query aligns to 3:248/250 of Q56840
- SGN 12:14 (≠ SGI 24:26) binding
- D33 (= D45) binding
- DV 60:61 (≠ DI 64:65) binding
- N87 (= N91) binding
- S142 (= S143) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ I153) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y156) mutation Y->E,F: Loss of activity.
- K159 (= K160) mutation to A: Loss of activity.
- R179 (= R180) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VVTNI 189:193) binding
- WR 195:196 (≠ HV 196:197) binding
- R196 (≠ V197) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ L205) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ A211) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 93% coverage: 15:249/254 of query aligns to 6:241/244 of P0AEK2
- GASR 12:15 (≠ GAAS 21:24) binding
- T37 (vs. gap) binding
- NV 59:60 (≠ DI 64:65) binding
- N86 (= N91) binding
- Y151 (= Y156) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YTASK 156:160) binding
- A154 (≠ S159) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K160) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V189) binding
- E233 (≠ S241) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
37% identity, 93% coverage: 15:249/254 of query aligns to 9:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G21), S17 (≠ A23), R18 (≠ S24), I20 (= I26), T40 (≠ I46), N62 (≠ D64), V63 (≠ I65), N89 (= N91), A90 (= A92), I92 (= I94), V139 (≠ I141), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (≠ V186), G185 (= G187), I187 (≠ V189), T189 (= T191), M191 (≠ I193)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 95% coverage: 14:254/254 of query aligns to 5:246/251 of 6vspA
- active site: G16 (= G25), S138 (= S143), Y151 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G21), N15 (≠ S24), G16 (= G25), M17 (≠ I26), D36 (= D45), W37 (≠ I46), W37 (≠ I46), A38 (≠ N47), I59 (≠ A63), D60 (= D64), V61 (≠ I65), N87 (= N91), A88 (= A92), G89 (= G93), V90 (≠ I94), V110 (= V114), T136 (≠ I141), S138 (= S143), Y151 (= Y156), K155 (= K160), P181 (≠ V186), S182 (≠ G187), L183 (≠ D188), V184 (= V189), T186 (= T191), N187 (= N192), M188 (≠ I193), T189 (≠ L194)
Query Sequence
>Pf1N1B4_4153 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4153
MTDIKNSTPNEVADKVALVTGAASGIGQAIALLLHARGAKVIAEDINPEVQALARPGLVP
LVADITQDGAAERAVALAVEQFGRLDILVNNAGIIINKLVIDMTREDWERIQAVNATAAF
LHSREAVKAMMPNKSGSIVNIASYASYFAFPTIAAYTASKGALAQLTRTLALEVIGHGIR
VNAVGVGDVVTNILNHVVDDGPAFLAQHGEAAPIGRAAQPEEIAEVVAFIASDRASFMVG
SVVMADGGMTVTAG
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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