SitesBLAST
Comparing 353245 FitnessBrowser__Btheta:353245 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 12 hits to proteins with known functional sites (download)
2j5tD Glutamate 5-kinase from escherichia coli complexed with glutamate (see paper)
31% identity, 97% coverage: 8:356/360 of query aligns to 5:352/365 of 2j5tD
P0A7B5 Glutamate 5-kinase; Gamma-glutamyl kinase; GK; EC 2.7.2.11 from Escherichia coli (strain K12) (see paper)
31% identity, 97% coverage: 8:356/360 of query aligns to 7:354/367 of P0A7B5
- S50 (= S51) binding substrate
- D137 (= D138) binding substrate
- N149 (= N150) binding substrate
2j5vB Glutamate 5-kinase from escherichia coli complexed with glutamyl-5- phosphate and pyroglutamic acid (see paper)
29% identity, 97% coverage: 8:356/360 of query aligns to 5:312/325 of 2j5vB
- binding pyroglutamic acid: T11 (≠ S14), G49 (= G52), A50 (= A53), I51 (≠ V54), A52 (= A55), D135 (= D138)
- binding gamma-glutamyl phosphate: K8 (= K11), S48 (= S51), D135 (= D138), G145 (≠ T148), D146 (= D149), N147 (= N150)
2j5vA Glutamate 5-kinase from escherichia coli complexed with glutamyl-5- phosphate and pyroglutamic acid (see paper)
28% identity, 97% coverage: 8:356/360 of query aligns to 5:310/323 of 2j5vA
- binding magnesium ion: K8 (= K11), G10 (= G13), L166 (= L169)
- binding pyroglutamic acid: T11 (≠ S14), S48 (= S51), G49 (= G52), A50 (= A53), I51 (≠ V54)
- binding gamma-glutamyl phosphate: K8 (= K11), G10 (= G13), S48 (= S51), D135 (= D138), D146 (= D149), N147 (= N150)
2akoA Crystal structure of glutamate 5-kinase from campylobacter jejuni
34% identity, 64% coverage: 7:235/360 of query aligns to 2:219/241 of 2akoA
- binding adenosine-5'-diphosphate: H10 (≠ N15), S161 (= S170), D162 (≠ N171), I163 (= I172), F166 (≠ I175), Y167 (= Y176), N170 (≠ S179), P171 (= P180), T194 (≠ R210), G196 (= G212), K200 (= K216)
8j0gB Gk monomer complexes with glutamate and atp
35% identity, 65% coverage: 3:235/360 of query aligns to 5:248/274 of 8j0gB
- binding adenosine-5'-triphosphate: K13 (= K11), G15 (= G13), T16 (≠ S14), A17 (≠ N15), V185 (≠ I172), G191 (= G178), P193 (= P180), F215 (≠ Q202), R223 (= R210), G225 (= G212), M226 (= M213), K229 (= K216)
- binding gamma-l-glutamic acid: A55 (= A53), N147 (= N135), D150 (= D138), N163 (= N150), R223 (= R210)
- binding magnesium ion: R223 (= R210), G224 (= G211), G225 (= G212)
- binding : Y65 (vs. gap), L68 (vs. gap), V69 (vs. gap), F73 (vs. gap)
7wx3B Gk domain of drosophila p5cs filament with glutamate, atp, and NADPH (see paper)
33% identity, 64% coverage: 7:238/360 of query aligns to 14:240/258 of 7wx3B
- binding gamma-glutamyl phosphate: S59 (= S51), A61 (= A53), N149 (= N135), T150 (≠ E136), D152 (= D138), M158 (= M146), N165 (= N150)
- binding : E72 (≠ K65), M75 (≠ D68), L77 (≠ V70), S78 (≠ D71), M79 (≠ Q72), R80 (= R73)
8j0eB Gk monomer complexes with catalytic intermediate
35% identity, 65% coverage: 3:235/360 of query aligns to 8:243/269 of 8j0eB
- binding magnesium ion: D163 (= D151), G219 (= G211)
- binding (2~{R})-5-[[[[(2~{R},3~{S},4~{S},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-2-azanyl-5-oxidanylidene-pentanoic acid: K16 (= K11), G18 (= G13), T19 (≠ S14), A20 (≠ N15), S56 (= S51), G57 (= G52), V59 (= V54), D153 (= D138), N162 (= N150), V184 (≠ I172), P192 (= P180), K217 (vs. gap), R218 (= R210), G219 (= G211), G220 (= G212), M221 (= M213)
- binding : Y68 (vs. gap), L71 (vs. gap), V72 (vs. gap), V72 (vs. gap), S74 (vs. gap), F76 (vs. gap), F76 (vs. gap), Q80 (vs. gap)
8j0fA Gk tetramer with adjacent hooks at reaction state (see paper)
35% identity, 65% coverage: 3:235/360 of query aligns to 9:242/270 of 8j0fA
- binding adenosine-5'-diphosphate: A21 (≠ N15), D183 (≠ N171), V184 (≠ I172), Y188 (= Y176), G190 (= G178), F214 (= F208), G219 (= G212), M220 (= M213)
- binding magnesium ion: R217 (= R210), G218 (= G211), G219 (= G212)
- binding gamma-glutamyl phosphate: K17 (= K11), T20 (≠ S14), S57 (= S51), D154 (= D138), N162 (= N150), R217 (= R210)
- binding : L72 (vs. gap), V73 (vs. gap), N74 (vs. gap), S75 (vs. gap), S76 (vs. gap), F77 (vs. gap), F77 (vs. gap), A78 (vs. gap), L80 (vs. gap)
7f5xA Gk domain of drosophila p5cs filament with glutamate (see paper)
31% identity, 64% coverage: 7:238/360 of query aligns to 14:218/236 of 7f5xA
3wwmA Crystal structure of lysz from thermus thermophilus with adp (see paper)
25% identity, 35% coverage: 65:191/360 of query aligns to 84:210/269 of 3wwmA
Sites not aligning to the query:
O50147 [LysW]-aminoadipate kinase; EC 2.7.2.17 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
25% identity, 35% coverage: 65:191/360 of query aligns to 84:210/269 of O50147
- R111 (≠ F92) mutation to E: Shows reduced activity.
- R112 (= R93) mutation to E: Shows reduced activity.
- K113 (≠ E94) mutation to E: Loss of activity.
- K117 (≠ A98) mutation to E: Does not bind LysW.
- K123 (≠ Q101) mutation to E: Does not bind LysW.
- K125 (≠ L103) mutation to E: Does not bind LysW.
- R128 (≠ K106) mutation to E: Does not bind LysW.
Sites not aligning to the query:
- 57 H→A: Shows reduced activity.
- 227 R→E: Still binds LysW, but shows reduced activity.
- 230 R→E: Still binds LysW, but shows reduced activity.
- 231 K→E: Still binds LysW, but shows reduced activity.
Query Sequence
>353245 FitnessBrowser__Btheta:353245
MKQEFTRIAVKVGSNVLARRDGTLDVTRMSALVDQIAELNKSGVEIILISSGAVASGRSE
IHPQKKLDSVDQRQLFSAVGQAKLINRYYELFREHGIAVGQVLTTKENFSTRRHYLNQKN
CMTVMLENGVIPIVNENDTISVSELMFTDNDELSGLIASMMDAQALIILSNIDGIYNGSP
SDPASAVIREIEHGKDLSNYIQATKSSFGRGGMLTKTNIARKVADEGITVIIANGKRDNI
LVDLLQQPDDTVCTRFIPSTEAVSSVKKWIAHSEGFAKGEIHINECATDILSSEKAASIL
PVGITHIEGEFEKDDIVRIMDFLGNQVGVGKANCDSAQAREAMGKHGKKPVVHYDYLYIE
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