SitesBLAST
Comparing WP_005457037.1 NCBI__GCF_000244975.1:WP_005457037.1 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)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
47% identity, 98% coverage: 7:248/248 of query aligns to 5:246/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
46% identity, 98% coverage: 7:248/248 of query aligns to 2:239/239 of 3sj7A
- active site: G12 (= G17), S138 (= S143), Q148 (= Q153), Y151 (= Y156), K155 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), S10 (≠ A15), R11 (= R16), I13 (= I18), N31 (≠ C36), Y32 (≠ F37), A33 (≠ R38), G34 (≠ Q39), S35 (≠ R40), A58 (≠ C63), N59 (≠ D64), V60 (= V65), N86 (= N91), A87 (= A92), T109 (= T114), S138 (= S143), Y151 (= Y156), K155 (= K160), P181 (= P186), G182 (= G187)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
45% identity, 98% coverage: 7:248/248 of query aligns to 6:247/247 of 4jroC
- active site: G16 (= G17), S142 (= S143), Q152 (= Q153), Y155 (= Y156), K159 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (≠ A15), R15 (= R16), G16 (= G17), I17 (= I18), N35 (≠ C36), Y36 (≠ F37), N37 (≠ R38), G38 (≠ Q39), S39 (≠ R40), N63 (≠ D64), V64 (= V65), N90 (= N91), A91 (= A92), I93 (≠ V94), I113 (≠ T114), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (= P186), I188 (= I189), T190 (= T191)
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)
45% identity, 100% coverage: 1:248/248 of query aligns to 1:246/247 of P73574
- A14 (= A14) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ A151) 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 (= K160) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ Y188) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ P198) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
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)
43% identity, 97% coverage: 8:248/248 of query aligns to 10:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G13), S17 (≠ A15), R18 (= R16), I20 (= I18), T40 (≠ R38), N62 (≠ Q61), V63 (≠ P62), N89 (= N91), A90 (= A92), I92 (≠ V94), V139 (≠ I141), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (= P186), G185 (= G187), I187 (= I189), T189 (= T191), M191 (= M193)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
42% identity, 98% coverage: 7:248/248 of query aligns to 6:243/244 of 6t77A
- active site: G16 (= G17), S138 (= S143), Y151 (= Y156)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (≠ A15), R15 (= R16), T37 (≠ R40), L58 (≠ C63), N59 (≠ D64), V60 (= V65), A87 (= A92), G88 (= G93), I89 (≠ V94)
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
42% identity, 98% coverage: 7:248/248 of query aligns to 2:244/244 of 1edoA
- active site: G12 (= G17), S138 (= S143), Y151 (= Y156), K155 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), S10 (≠ A15), R11 (= R16), I13 (= I18), N31 (≠ C36), Y32 (≠ F37), A33 (≠ R38), R34 (≠ Q39), S35 (≠ R40), D59 (= D64), V60 (= V65), N86 (= N91), A87 (= A92), S138 (= S143), Y151 (= Y156), K155 (= K160), P181 (= P186), G182 (= G187), I184 (= I189), S186 (≠ T191), M188 (= M193)
P9WGT3 3-oxoacyl-[acyl-carrier-protein] reductase MabA; 3-ketoacyl reductase; 3-ketoacyl-acyl carrier protein reductase; Acetoacetyl-CoA reductase; Beta-ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; Mycolic acid biosynthesis A; EC 1.1.1.100; EC 1.1.1.36 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 7 papers)
45% identity, 96% coverage: 10:246/248 of query aligns to 19:243/247 of P9WGT3
- T21 (= T12) modified: Phosphothreonine; mutation to A: Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-114 and A-191.
- RGI 25:27 (= RGI 16:18) binding NADP(+)
- R47 (= R38) binding NADP(+)
- C60 (= C63) mutation to V: Displays a lower activity than the wild-type and a slightly decreased affinity for the cofactor. Retains 84% of activity; when associated with L-144. Totally inactive; when associated with A-139 and L-144.
- DV 61:62 (= DV 64:65) binding NADP(+)
- G90 (= G93) binding NADP(+)
- T114 (= T117) modified: Phosphothreonine; mutation to A: Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-191.
- G139 (≠ S142) mutation to A: Complete protein inactivation and freezes the catalytic site into its closed form. Totally inactive; when associated with V-60 and L-144.
- S140 (= S143) mutation to A: Loss of activity. Can still bind NADPH.; mutation to T: Loss of activity. Impaired NADPH binding.
- S144 (≠ V147) mutation to L: Stabilizes the catalytic loop in its open active form. Retains 84% of activity; when associated with V-60. Totally inactive; when associated with V-60 and A-139.
- Y185 (= Y188) mutation to L: 70% decrease in activity with acetoacetyl-CoA as substrate. Does not affect NADP binding.
- T191 (= T194) modified: Phosphothreonine; mutation to A: Retains 22% of wild-type reductase activity. Strong decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-114.; mutation to D: Phosphomimetic mutant that retains less than 10% of wild-type reductase activity. Impaired NADPH binding. Overproduction of the mutant leads to a significant inhibition of de novo biosynthesis of mycolic acids.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4nbuB Crystal structure of fabg from bacillus sp (see paper)
40% identity, 100% coverage: 1:248/248 of query aligns to 2:244/244 of 4nbuB
- active site: G18 (= G17), N111 (= N115), S139 (= S143), Q149 (= Q153), Y152 (= Y156), K156 (= K160)
- binding acetoacetyl-coenzyme a: D93 (= D97), K98 (≠ M102), S139 (= S143), N146 (= N150), V147 (≠ A151), Q149 (= Q153), Y152 (= Y156), F184 (≠ Y188), M189 (= M193), K200 (= K204)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ R16), G18 (= G17), I19 (= I18), D38 (≠ Q39), F39 (≠ R40), V59 (≠ C63), D60 (= D64), V61 (= V65), N87 (= N91), A88 (= A92), G89 (= G93), I90 (≠ V94), T137 (≠ I141), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), F184 (≠ Y188), T185 (≠ I189), T187 (= T191), M189 (= M193)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
44% identity, 97% coverage: 9:248/248 of query aligns to 11:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G13), R18 (= R16), G19 (= G17), I20 (= I18), D39 (≠ F37), R40 (= R38), C63 (= C63), I65 (≠ V65), N91 (= N91), G93 (= G93), I94 (≠ V94), V114 (≠ T114), Y155 (= Y156), K159 (= K160), I188 (= I189), T190 (= T191), T193 (= T194)
5ovlA Crystal structure of maba bound to NADP+ from m. Smegmatis (see paper)
45% identity, 96% coverage: 10:246/248 of query aligns to 13:237/241 of 5ovlA
- active site: G20 (= G17), S134 (= S143), Y147 (= Y156), L154 (≠ I163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G13), N18 (≠ A15), R19 (= R16), G20 (= G17), I21 (= I18), R41 (= R38), D55 (= D64), V56 (= V65), N82 (= N91), A83 (= A92), I85 (≠ V94), T105 (= T114), I132 (= I141), S134 (= S143), Y147 (= Y156), K151 (= K160), P177 (= P186), G178 (= G187), I180 (= I189)
5ovkA Crystal structure maba bound to NADPH from m. Smegmatis (see paper)
45% identity, 96% coverage: 10:246/248 of query aligns to 14:238/242 of 5ovkA
P71534 3-oxoacyl-[acyl-carrier-protein] reductase MabA; 3-ketoacyl-acyl carrier protein reductase; Acetoacetyl-CoA reductase; Beta-ketoacyl-ACP reductase; Beta-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100; EC 1.1.1.36 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
45% identity, 96% coverage: 10:246/248 of query aligns to 27:251/255 of P71534
- NRGI 32:35 (≠ ARGI 15:18) binding NADP(+)
- R55 (= R38) binding NADP(+)
- DV 69:70 (= DV 64:65) binding NADP(+)
- Y161 (= Y156) binding NADP(+)
- K165 (= K160) binding NADP(+)
- I194 (= I189) binding NADP(+)
- R205 (≠ K200) binding NADP(+)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
43% identity, 96% coverage: 10:248/248 of query aligns to 8:242/243 of 7emgB
1uznA Maba from mycobacterium tuberculosis (see paper)
45% identity, 96% coverage: 10:246/248 of query aligns to 11:235/239 of 1uznA
- active site: G18 (= G17), S132 (= S143), Y145 (= Y156), K149 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G13), N16 (≠ A15), R17 (= R16), I19 (= I18), R39 (= R38), D53 (= D64), V54 (= V65), A81 (= A92), G82 (= G93)
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)
41% identity, 98% coverage: 7:248/248 of query aligns to 6:243/244 of P0AEK2
- GASR 12:15 (≠ GAAR 13:16) binding NADP(+)
- T37 (≠ R40) binding NADP(+)
- NV 59:60 (≠ DV 64:65) binding NADP(+)
- N86 (= N91) binding NADP(+)
- Y151 (= Y156) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAASK 156:160) binding NADP(+)
- 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 (= I189) binding NADP(+)
- E233 (≠ Q238) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
41% identity, 98% coverage: 7:248/248 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G17), E101 (= E107), S137 (= S143), Q147 (= Q153), Y150 (= Y156), K154 (= K160)
- binding calcium ion: E232 (≠ Q238), T233 (≠ V239)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G13), S13 (≠ A15), R14 (= R16), T36 (≠ R40), N58 (≠ D64), V59 (= V65), N85 (= N91), A86 (= A92), G87 (= G93), I88 (≠ V94), S137 (= S143), Y150 (= Y156), K154 (= K160), P180 (= P186), G181 (= G187), I183 (= I189)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
42% identity, 97% coverage: 8:248/248 of query aligns to 10:242/243 of 4i08A
- active site: G19 (= G17), N113 (= N115), S141 (= S143), Q151 (= Q153), Y154 (= Y156), K158 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G13), S17 (≠ A15), R18 (= R16), I20 (= I18), T40 (≠ R38), N62 (≠ Q61), V63 (≠ P62), N89 (= N91), A90 (= A92), G140 (≠ S142), S141 (= S143), Y154 (= Y156), K158 (= K160), P184 (= P186), G185 (= G187), T189 (= 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)
41% identity, 98% coverage: 7:248/248 of query aligns to 6:243/244 of P0A2C9
- M125 (= M130) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ L228) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S229) 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.
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
41% identity, 98% coverage: 7:248/248 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G17), S137 (= S143), Q147 (= Q153), F150 (≠ Y156), K154 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G13), S13 (≠ A15), R14 (= R16), A35 (≠ Q39), T36 (≠ R40), L57 (≠ C63), N58 (≠ D64), V59 (= V65), G87 (= G93), I88 (≠ V94)
Query Sequence
>WP_005457037.1 NCBI__GCF_000244975.1:WP_005457037.1
MTGAGEPCALVTGAARGIGREVALRLARDGYRIAGCFRQRGEDAARVERELAEAGARTFF
QPCDVRDADAVSRFVTEAEDALGPITALVNNAGVTRDANTVMMSPEEWSTVLDTNLTGTW
NVCRAVVFRMLKRRAGAVVNISSIAGVHGNAGQSNYAASKAGIIGLTKSLAKETARAGVR
ANVVAPGYIDTEMTSALPAKGQDKALAAIPLRRFGRPDDVAPLVAFLLSDESSYITGQVF
AVDGGMVL
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