SitesBLAST
Comparing 7025614 FitnessBrowser__ANA3:7025614 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)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
46% identity, 99% coverage: 3:252/252 of query aligns to 5:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N121), S139 (= S150), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding acetoacetyl-coenzyme a: D93 (= D94), K98 (= K99), S139 (= S150), N146 (= N156), V147 (= V157), Q149 (= Q159), Y152 (= Y162), F184 (≠ V194), M189 (= M199), K200 (≠ R210)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ G15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ V37), V59 (≠ L60), D60 (= D61), V61 (≠ I62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (= I91), T137 (≠ I148), S139 (= S150), Y152 (= Y162), K156 (= K166), P182 (= P192), F184 (≠ V194), T185 (≠ I195), T187 (= T197), M189 (= M199)
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
43% identity, 97% coverage: 6:250/252 of query aligns to 2:249/253 of 4nbwA
- active site: G12 (= G16), S146 (= S150), Y159 (= Y162), K163 (= K166)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), N11 (≠ G15), G12 (= G16), I13 (≠ L17), D32 (= D36), L33 (≠ V37), V57 (≠ L60), D58 (= D61), V59 (≠ I62), N85 (= N88), A86 (= A89), G87 (= G90), S146 (= S150), Y159 (= Y162), K163 (= K166), I192 (= I195), T194 (= T197)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
40% identity, 99% coverage: 3:252/252 of query aligns to 3:239/239 of 4nbtA
- active site: G16 (= G16), S132 (= S150), Y145 (= Y162), K149 (= K166)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ G15), G16 (= G16), L17 (= L17), D36 (= D48), L37 (= L49), L52 (= L60), N53 (≠ D61), V54 (≠ I62), N80 (= N88), A81 (= A89), G82 (= G90), I130 (= I148), S132 (= S150), Y145 (= Y162), K149 (= K166), P177 (= P192), G178 (= G193), I180 (= I195), T182 (= T197)
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
39% identity, 98% coverage: 5:252/252 of query aligns to 6:239/241 of 4cqmF
- active site: G17 (= G16), S139 (= S150), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), R16 (≠ G15), G17 (= G16), I18 (≠ L17), A37 (≠ D36), R38 (≠ V37), N39 (≠ D38), D60 (= D61), V61 (≠ I62), A87 (≠ N88), A88 (= A89), G89 (= G90), V137 (≠ I148), S139 (= S150), Y152 (= Y162), K156 (= K166), V185 (≠ I195), T187 (= T197), M189 (= M199)
Q8N4T8 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-[acyl-carrier-protein] reductase beta subunit; KAR beta subunit; Carbonyl reductase family member 4; CBR4; Quinone reductase CBR4; Short chain dehydrogenase/reductase family 45C member 1; EC 1.1.1.100; EC 1.6.5.10 from Homo sapiens (Human) (see 4 papers)
39% identity, 98% coverage: 5:252/252 of query aligns to 2:235/237 of Q8N4T8
- G9 (= G12) mutation to S: Unable to restore growth of an OAR1-deficient yeast mutant.
- SRGI 11:14 (≠ AGGL 14:17) binding
- R12 (≠ G15) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
- R34 (≠ V37) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- RN 34:35 (≠ VD 37:38) binding
- D56 (= D61) binding
- L70 (≠ I75) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ NAG 88:90) binding
- S135 (= S150) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y162) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K166) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- R168 (= R182) mutation to E: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- K169 (≠ Y183) mutation to E: Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- VHT 181:183 (≠ IAT 195:197) binding
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
39% identity, 99% coverage: 1:250/252 of query aligns to 1:237/240 of 4dmmB
- active site: G16 (= G16), S142 (= S150), Q152 (= Q159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ A14), R15 (≠ G15), G16 (= G16), I17 (≠ L17), A37 (≠ V37), S38 (≠ D38), S39 (≠ Q39), A62 (vs. gap), D63 (= D61), V64 (≠ I62), N90 (= N88), A91 (= A89), L113 (≠ V120), I140 (= I148), S142 (= S150), Y155 (= Y162), K159 (= K166), P185 (= P192), G186 (= G193), I188 (= I195), T190 (= T197), M192 (= M199)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
38% identity, 99% coverage: 1:250/252 of query aligns to 1:245/247 of 4jroC
- active site: G16 (= G16), S142 (= S150), Q152 (= Q159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ A14), R15 (≠ G15), G16 (= G16), I17 (≠ L17), N35 (≠ D36), Y36 (≠ V37), N37 (≠ D38), G38 (vs. gap), S39 (vs. gap), N63 (≠ D61), V64 (≠ I62), N90 (= N88), A91 (= A89), I93 (= I91), I113 (≠ V120), S142 (= S150), Y155 (= Y162), K159 (= K166), P185 (= P192), I188 (= I195), T190 (= T197)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
37% identity, 100% coverage: 1:252/252 of query aligns to 4:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (≠ G15), G19 (= G16), I20 (≠ L17), D39 (= D36), R40 (≠ V37), C63 (≠ L60), I65 (= I62), N91 (= N88), G93 (= G90), I94 (= I91), V114 (= V120), Y155 (= Y162), K159 (= K166), I188 (= I195), T190 (= T197), T193 (= T200)
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
37% identity, 98% coverage: 7:252/252 of query aligns to 3:244/244 of 1edoA
- active site: G12 (= G16), S138 (= S150), Y151 (= Y162), K155 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (≠ A14), R11 (≠ G15), I13 (≠ L17), N31 (≠ D38), Y32 (≠ Q39), A33 (≠ E40), R34 (≠ K41), S35 (≠ L42), D59 (= D61), V60 (≠ I62), N86 (= N88), A87 (= A89), S138 (= S150), Y151 (= Y162), K155 (= K166), P181 (= P192), G182 (= G193), I184 (= I195), S186 (≠ T197), M188 (= M199)
4o5oB X-ray crystal structure of a 3-hydroxyacyl-coa dehydrogenase from brucella suis
39% identity, 100% coverage: 1:252/252 of query aligns to 7:258/261 of 4o5oB
Sites not aligning to the query:
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
38% identity, 98% coverage: 1:248/252 of query aligns to 4:236/240 of P73826
- S134 (= S150) mutation to A: 12% enzymatic activity.
- Y147 (= Y162) mutation to A: No enzymatic activity.
- K151 (= K166) mutation to A: 5% enzymatic activity.
O70351 3-hydroxyacyl-CoA dehydrogenase type-2; 17-beta-estradiol 17-dehydrogenase; 2-methyl-3-hydroxybutyryl-CoA dehydrogenase; MHBD; 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)); 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase type II; 3alpha(or 20beta)-hydroxysteroid dehydrogenase; 7-alpha-hydroxysteroid dehydrogenase; Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Short chain dehydrogenase/reductase family 5C member 1; Short-chain type dehydrogenase/reductase XH98G2; Type II HADH; EC 1.1.1.35; EC 1.1.1.62; EC 1.1.1.239; EC 1.1.1.178; EC 1.1.1.53; EC 1.1.1.159 from Rattus norvegicus (Rat) (see paper)
38% identity, 100% coverage: 2:252/252 of query aligns to 7:259/261 of O70351
- S155 (= S150) binding
- Y168 (= Y162) active site, Proton acceptor
1e3wD Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and 3-keto butyrate (see paper)
38% identity, 100% coverage: 2:252/252 of query aligns to 1:253/255 of 1e3wD
- active site: G15 (= G16), N115 (= N121), T147 (≠ I148), S149 (= S150), Y162 (= Y162), K166 (= K166), F195 (≠ I195)
- binding acetoacetic acid: Y162 (= Y162), T202 (≠ A202)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (≠ G15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (= V37), N58 (≠ D61), V59 (≠ I62), C85 (≠ N88), A86 (= A89), G87 (= G90), V114 (= V120), T147 (≠ I148), Y162 (= Y162), K166 (= K166), P192 (= P192), L194 (≠ V194), F195 (≠ I195), T197 (= T197), L199 (≠ M199)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
38% identity, 100% coverage: 1:252/252 of query aligns to 1:245/248 of Q9KJF1
- M1 (= M1) modified: Initiator methionine, Removed
- S15 (≠ G15) binding
- D36 (= D36) binding
- D62 (= D61) binding
- I63 (= I62) binding
- N89 (= N88) binding
- Y153 (= Y162) binding
- K157 (= K166) binding
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
35% identity, 98% coverage: 3:250/252 of query aligns to 4:246/248 of 4cqmA
- active site: G17 (= G16), S143 (= S150), Y156 (= Y162), K160 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), S16 (≠ G15), G17 (= G16), I18 (≠ L17), D37 (= D36), L38 (≠ V37), A61 (≠ L60), V63 (≠ I62), C90 (≠ N88), A91 (= A89), G92 (= G90), I93 (= I91), V113 (= V120), I141 (= I148), S143 (= S150), Y156 (= Y162), K160 (= K166), P186 (= P192), G187 (= G193), I189 (= I195), T191 (= T197), P192 (≠ E198), M193 (= M199), T194 (= T200)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
38% identity, 99% coverage: 3:252/252 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), M16 (≠ L17), D35 (= D36), I36 (≠ V37), I62 (= I62), N88 (= N88), G90 (= G90), I138 (= I148), S140 (= S150), Y152 (= Y162), K156 (= K166), I185 (= I195)
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
35% identity, 98% coverage: 3:250/252 of query aligns to 6:249/251 of 4cqlI
- active site: G19 (= G16), S146 (= S150), Y159 (= Y162), K163 (= K166)
- binding nicotinamide-adenine-dinucleotide: S18 (≠ G15), G19 (= G16), I20 (≠ L17), D39 (= D36), L40 (≠ V37), A64 (≠ L60), D65 (= D61), V66 (≠ I62), C93 (≠ N88), A94 (= A89), G95 (= G90), I96 (= I91), V116 (= V120), I144 (= I148), S146 (= S150), Y159 (= Y162), K163 (= K166), P189 (= P192), G190 (= G193), I192 (= I195), T194 (= T197), M196 (= M199)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
37% identity, 98% coverage: 3:250/252 of query aligns to 4:244/247 of P73574
- A14 (≠ G13) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ V157) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K166) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ V194) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ K204) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
Q92506 (3R)-3-hydroxyacyl-CoA dehydrogenase; 17-beta-hydroxysteroid dehydrogenase 8; 17-beta-HSD 8; HSD17B8; 3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit; KAR alpha subunit; 3-oxoacyl-[acyl-carrier-protein] reductase; Estradiol 17-beta-dehydrogenase 8; Protein Ke6; Ke6; Short chain dehydrogenase/reductase family 30C member 1; Testosterone 17-beta-dehydrogenase 8; EC 1.1.1.n12; EC 1.1.1.62; EC 1.1.1.239 from Homo sapiens (Human) (see 2 papers)
35% identity, 98% coverage: 3:250/252 of query aligns to 9:259/261 of Q92506
- 15:23 (vs. 9:17, 33% identical) binding
- D42 (= D36) mutation to A: Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- DL 42:43 (≠ DV 36:37) binding
- ADV 74:76 (≠ LDI 60:62) binding
- R148 (≠ A142) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- V158 (vs. gap) to L: in a breast cancer sample; somatic mutation
- Y169 (= Y162) mutation to A: Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- YAASK 169:173 (= YAASK 162:166) binding
- K173 (= K166) mutation to A: Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- R189 (= R182) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- IAT 202:204 (= IAT 195:197) binding
1e6wC Rat brain 3-hydroxyacyl-coa dehydrogenase binary complex with nadh and estradiol (see paper)
38% identity, 100% coverage: 2:252/252 of query aligns to 1:246/248 of 1e6wC
- active site: G15 (= G16), N115 (= N121), T147 (≠ I148), S149 (= S150), Y162 (= Y162), K166 (= K166), F195 (≠ I195)
- binding estradiol: Q159 (= Q159), Y162 (= Y162), L200 (≠ A207)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (≠ G15), G15 (= G16), L16 (= L17), D35 (= D36), V36 (= V37), N58 (≠ D61), V59 (≠ I62), C85 (≠ N88), A86 (= A89), T147 (≠ I148), Y162 (= Y162), K166 (= K166), P192 (= P192), L194 (≠ V194), F195 (≠ I195), T197 (= T197), L199 (≠ E206)
Query Sequence
>7025614 FitnessBrowser__ANA3:7025614
MDLKDKVVVITGGAGGLGLAMAHNFAQAGAKLALIDVDQEKLERACADLGSATEVQGYAL
DITDEEDVVAGFAYILEDFGKINVLVNNAGILRDGMLVKAKDGKVTDRMSFDQFQSVINV
NLTGTFLCGREAAAAMIESGQAGVIVNISSLAKAGNVGQSNYAASKAGVAAMSVGWAKEL
ARYNIRSAAVAPGVIATEMTAAMKPEALERLEKLVPVGRLGQAEEIASTVRFIIENDYVN
GRVFEVDGGIRL
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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