SitesBLAST
Comparing WP_007695331.1 NCBI__GCF_000336675.1:WP_007695331.1 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)
6mdeA Mevalonate kinase from methanosarcina mazei with mevalonate bound (see paper)
42% identity, 91% coverage: 1:300/329 of query aligns to 2:274/302 of 6mdeA
6mdfA Mevalonate kinase from methanosarcina mazei with 5-phosphomevalonate bound (see paper)
42% identity, 91% coverage: 1:300/329 of query aligns to 3:275/303 of 6mdfA
4hacA Crystal structure of the mevalonate kinase from an archaeon methanosarcina mazei (see paper)
42% identity, 91% coverage: 1:300/329 of query aligns to 12:284/312 of 4hacA
8tebA Structure of mkbur (see paper)
38% identity, 91% coverage: 1:301/329 of query aligns to 1:274/306 of 8tebA
Q58487 Mevalonate kinase; MK; MVK; EC 2.7.1.36 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
31% identity, 89% coverage: 3:295/329 of query aligns to 2:285/312 of Q58487
- R196 (≠ G198) mutation to K: 13.5-fold decrease in affinity for mevalonate, whereas only little effect on affinity for ATP and on reaction rate.; mutation to Q: 1900-fold decrease in catalytic efficiency.; mutation to V: 63-fold decrease in catalytic efficiency.
- K272 (= K282) mutation K->R,A: 13- to 26-fold decrease in catalytic efficiency. Still thermostable.
2hfuA Crystal structure of l. Major mevalonate kinase in complex with r- mevalonate (see paper)
29% identity, 93% coverage: 8:314/329 of query aligns to 17:313/326 of 2hfuA
2dejA Crystal structure of galaktokinase from pyrococcus horikoshii with amp-pn and galactose
28% identity, 92% coverage: 1:303/329 of query aligns to 1:316/346 of 2dejA
- binding {5'-o-[(r)-{[(s)-amino(hydroxy-kappao)phosphoryl]oxy}(hydroxy-kappao)phosphoryl]adenosinato(2-)}magnesium: S47 (≠ L54), F50 (= F57), W67 (≠ V77), Y70 (= Y84), V92 (= V107), L98 (= L113), G99 (= G114), G101 (= G116), S103 (≠ G118), S104 (= S119), S105 (= S120), F108 (≠ V123)
- binding alpha-D-galactopyranose: E15 (= E15), H16 (= H16), D18 (vs. gap), G146 (≠ S161), D149 (= D164), Y194 (vs. gap)
2deiA Crystal structure of galaktokinase from pyrococcus horikoshii with amp-pnp and galactose
28% identity, 92% coverage: 1:303/329 of query aligns to 1:320/350 of 2deiA
- binding alpha-D-galactopyranose: E15 (= E15), H16 (= H16), D18 (vs. gap), G146 (≠ S161), D149 (= D164), Y198 (≠ R210)
- binding magnesium-5'-adenyly-imido-triphosphate: S47 (≠ L54), F50 (= F57), W67 (≠ V77), Y70 (= Y84), L98 (= L113), G99 (= G114), G101 (= G116), S103 (≠ G118), S104 (= S119), S105 (= S120), F108 (≠ V123)
P0A6T3 Galactokinase; Galactose kinase; EC 2.7.1.6 from Escherichia coli (strain K12) (see 2 papers)
27% identity, 91% coverage: 5:302/329 of query aligns to 24:350/382 of P0A6T3
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 371 Y→H: Displays relaxed substrate specificity since it gains kinase activity toward sugars as diverse as D-galacturonic acid, D-talose, L-altrose, and L-glucose. Also shows enhanced turnover of the small pool of sugars converted by the wild-type enzyme.
2r42A The biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism (see paper)
31% identity, 81% coverage: 5:269/329 of query aligns to 9:306/383 of 2r42A
- binding s-[(2e,6e)-3,7,11-trimethyldodeca-2,6,10-trienyl] trihydrogen thiodiphosphate: N55 (≠ D51), G128 (= G114), G130 (= G116), G132 (= G118), S133 (= S119), S134 (= S120), Y137 (vs. gap)
- binding magnesium ion: G132 (= G118), A135 (= A121), D192 (= D164)
Q03426 Mevalonate kinase; MK; EC 2.7.1.36 from Homo sapiens (Human) (see 12 papers)
29% identity, 85% coverage: 5:284/329 of query aligns to 9:332/396 of Q03426
- E19 (= E15) mutation to D: No change in protein stability. Weak decrease in kinase activity. Approximately 2-fold decrease in Vmax. Approximately 2-fold decrease affinity for ATP and mevalonate.
- H20 (= H16) to P: in HIDS and MEVA; dbSNP:rs104895295
- S52 (vs. gap) to N: in dbSNP:rs7957619
- I56 (vs. gap) mutation to A: No effect on kinase activity. Approximately 4- and 5-fold decrease affinities for ATP and mevalonate, respectively.
- T104 (≠ D74) mutation to A: No effect on kinase activity. Approximately 4-fold increase affinity for ATP. Normal affinity for mevalonate.
- S145 (= S119) mutation to A: Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax.
- S146 (= S120) mutation to A: Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. 4000-fold decrease in Vmax.
- Y149 (≠ V123) mutation to A: No effect on kinase activity. Approximately 4- and 8-fold decrease affinities for ATP and mevalonate, respectively.
- E193 (vs. gap) mutation to Q: No change in protein stability. Decreased kinase activity. Approximately 50-fold decrease in Vmax. Approximately 20- and 40-fold decrease affinities for ATP and mevalonate, respectively.
- I196 (vs. gap) mutation to A: No effect on kinase activity. Approximately 2- and 3-fold decrease affinities for ATP and mevalonate, respectively.
- S201 (= S161) mutation to A: Modest changes in KM for ATP. 100-fold increase in KM for mevalonate. Approximately 2-fold increase in Vmax.
- G202 (≠ R162) to R: in HIDS and POROK3; dbSNP:rs104895301
- D204 (= D164) mutation to A: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate.; mutation to N: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate.
- T243 (= T202) mutation to A: Modest changes in KM for ATP. 40-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax.
- I268 (= I226) to T: in HIDS and MEVA; dbSNP:rs104895304
- E296 (≠ R247) mutation to Q: No change in protein stability. No effect on kinase activity.
- N301 (= N252) to T: in MEVA; diminished activity; dbSNP:rs121917789
- V310 (= V261) to M: in MEVA and HIDS; dbSNP:rs104895319
Sites not aligning to the query:
- 356 T → M: in dbSNP:rs104895342
- 377 V → I: in HIDS; most frequent mutation; dbSNP:rs28934897
1kvkA The structure of binary complex between a mammalian mevalonate kinase and atp: insights into the reaction mechanism and human inherited disease (see paper)
30% identity, 81% coverage: 5:269/329 of query aligns to 9:302/378 of 1kvkA
- binding adenosine-5'-triphosphate: N88 (≠ T73), E89 (≠ D74), S92 (≠ V77), G124 (= G114), G126 (= G116), G128 (= G118), S129 (= S119), S130 (= S120), I180 (≠ Q156)
- binding magnesium ion: G128 (= G118), S130 (= S120), A131 (= A121), E177 (= E152), H181 (≠ N157), D188 (= D164)
8tfoA Structure of mkvar (see paper)
29% identity, 89% coverage: 5:296/329 of query aligns to 10:349/390 of 8tfoA
P17256 Mevalonate kinase; MK; EC 2.7.1.36 from Rattus norvegicus (Rat) (see 2 papers)
29% identity, 81% coverage: 5:269/329 of query aligns to 9:318/395 of P17256
- K13 (= K9) binding ATP
- H20 (= H16) mutation to K: Induce significant secondary structural change.; mutation H->L,Y: Approximately 5-fold decrease in Vmax for (R,S)-mevalonate. Approximately 3-fold increase in KM for (R,S)-mevalonate.
- N55 (≠ D51) binding ATP
- N104 (≠ G87) binding ATP
- S108 (vs. gap) binding ATP
- S135 (= S109) binding ATP
- 140:146 (vs. 114:120, 100% identical) binding ATP
- S146 (= S120) binding Mg(2+)
- E193 (= E152) binding Mg(2+)
Q9HHB6 Galactokinase; Galactose kinase; EC 2.7.1.6 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see paper)
26% identity, 91% coverage: 5:303/329 of query aligns to 7:322/352 of Q9HHB6
- EHTD 17:20 (≠ EHA- 15:17) binding substrate
- S107 (= S120) binding Mg(2+)
- E139 (= E152) binding Mg(2+)
- Y200 (≠ R210) binding substrate
1s4eF Pyrococcus furiosus galactokinase in complex with galactose, adp and magnesium (see paper)
26% identity, 91% coverage: 5:303/329 of query aligns to 6:321/351 of 1s4eF
- binding adenosine-5'-diphosphate: S48 (≠ L54), F51 (= F57), W68 (≠ V77), Y71 (= Y84), I93 (≠ V107), L99 (= L113), G100 (= G114), S104 (≠ G118), S105 (= S119), S106 (= S120), F109 (≠ V123)
- binding alpha-D-galactopyranose: E16 (= E15), H17 (= H16), D19 (vs. gap), Y199 (≠ R210), A304 (≠ S286)
6gr2A Structure of human galactokinase in complex with galactose and adp
27% identity, 93% coverage: 5:310/329 of query aligns to 30:361/383 of 6gr2A
- binding adenosine-5'-diphosphate: T74 (≠ Y61), S76 (≠ G63), Y106 (= Y84), L132 (= L113), G133 (= G114), G135 (= G116), S137 (≠ G118), S138 (= S119), S139 (= S120)
- binding beta-D-galactopyranose: E40 (= E15), H41 (= H16), D43 (≠ V18), G180 (≠ S161), D183 (= D164), Y227 (= Y195)
1wuuA Crystal structure of human galactokinase complexed with mgamppnp and galactose (see paper)
27% identity, 93% coverage: 5:310/329 of query aligns to 34:369/391 of 1wuuA
- binding phosphoaminophosphonic acid-adenylate ester: T78 (≠ Y61), S80 (≠ G63), W107 (vs. gap), Y110 (= Y84), L136 (= L113), G137 (= G114), G139 (= G116), S141 (≠ G118), S142 (= S119), S143 (= S120), L146 (≠ V123)
- binding alpha-D-galactopyranose: E44 (= E15), H45 (= H16), D47 (≠ V18), Y48 (≠ V19), G184 (≠ S161), M186 (≠ A163), D187 (= D164), Y235 (≠ L205)
6zfhA Structure of human galactokinase in complex with galactose and 2'- (benzo[d]oxazol-2-ylamino)-7',8'-dihydro-1'h-spiro[cyclopentane-1,4'- quinazolin]-5'(6'h)-one (see paper)
27% identity, 93% coverage: 5:310/329 of query aligns to 31:364/386 of 6zfhA
- binding beta-D-galactopyranose: E41 (= E15), H42 (= H16), D44 (≠ V18), G181 (≠ S161), M183 (≠ A163), D184 (= D164), Y230 (≠ L205), G340 (≠ S286)
- binding 2-(1,3-benzoxazol-2-ylamino)spiro[1,6,7,8-tetrahydroquinazoline-4,1'-cyclopentane]-5-one: W104 (vs. gap), Y107 (= Y84), L133 (= L113), S139 (= S119), S140 (= S120), L143 (≠ V123)
6tepA Crystal structure of a galactokinase from bifidobacterium infantis in complex with adp (see paper)
27% identity, 89% coverage: 3:295/329 of query aligns to 34:373/414 of 6tepA
- binding adenosine-5'-diphosphate: S80 (≠ N55), V82 (≠ F57), W103 (≠ G81), Y106 (= Y84), L135 (= L113), G136 (= G114), G138 (= G116), S140 (≠ G118), S141 (= S119), S142 (= S120), M145 (≠ V123)
Query Sequence
>WP_007695331.1 NCBI__GCF_000336675.1:WP_007695331.1
MAVSSAPGKVYLFGEHAVVYGEPAVPCAIERRARVEATQRSDSRVRVHAQDLYLNGFSVE
YAGPADDRPTVATDQSVLDLGMRYIDGAIDRARDLADQPEVGLDVTVESDLPLGAGLGSS
AAVVVAGIDATARELGLELDSEEVANHAYKVEHEVQNGEASRADTFCSATGGAAKVEGDS
CETIDAPNLPFVVGYDGGTGNTGELVAGVRALREEYDFAASTVESIGDLVRRGEHALDAG
DVDELGRLMDVNHGLLSALGVSARSLDAMVWAAREAGARGAKLTGSGGGGCIVALDETED
TPTALGYTPECERAFRAELDTEGVRREDG
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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