SitesBLAST
Comparing WP_011320144.1 NCBI__GCF_000204075.1:WP_011320144.1 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)
P74285 UTP--glucose-1-phosphate uridylyltransferase; Cyanobacterial UDP-glucose pyrophosphorylase; UDP-glucose pyrophosphorylase; UDP-Glc PPase; EC 2.7.7.9 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
80% identity, 99% coverage: 1:384/389 of query aligns to 1:385/388 of P74285
- A8 (= A8) mutation to G: Two-fold decrease in affinity for UTP. No effect on affinity for Glc-1P and on catalytic activity rate.
7d73E Cryo-em structure of gmppa/gmppb complex bound to gtp (state i) (see paper)
30% identity, 87% coverage: 1:340/389 of query aligns to 1:327/360 of 7d73E
- binding guanosine-5'-triphosphate: L6 (= L6), V7 (≠ A7), G8 (≠ A8), G9 (= G9), G11 (= G11), T12 (= T12), R13 (= R13), A52 (≠ N52), S54 (= S54), E80 (= E79), P83 (≠ A92), G85 (= G94), N108 (≠ C117)
7d72K Cryo-em structures of human gmppa/gmppb complex bound to gdp-mannose (see paper)
30% identity, 87% coverage: 1:340/389 of query aligns to 1:327/360 of 7d72K
- binding guanosine-5'-diphosphate-alpha-d-mannose: L6 (= L6), V7 (≠ A7), G8 (≠ A8), G85 (= G94), T86 (≠ S95), N108 (≠ C117), S109 (≠ G118), D110 (= D119), N172 (= N184), E194 (= E203), D218 (= D232)
7d72E Cryo-em structures of human gmppa/gmppb complex bound to gdp-mannose (see paper)
30% identity, 87% coverage: 1:340/389 of query aligns to 1:327/360 of 7d72E
7whsA Cryo-em structure of leishmanial gdp-mannose pyrophosphorylase in complex with gtp (see paper)
29% identity, 88% coverage: 1:343/389 of query aligns to 1:324/366 of 7whsA
- binding guanosine-5'-triphosphate: L6 (= L6), V7 (≠ A7), G8 (≠ A8), G9 (= G9), G11 (= G11), R13 (= R13), A52 (≠ N52), G85 (= G94), N108 (≠ C117), D110 (= D119)
- binding magnesium ion: D110 (= D119), D218 (= D232)
7whtA Cryo-em structure of leishmanial gdp-mannose pyrophosphorylase in complex with gdp-mannose (see paper)
29% identity, 88% coverage: 1:343/389 of query aligns to 1:318/360 of 7whtA
- binding guanosine-5'-diphosphate-alpha-d-mannose: L6 (= L6), V7 (≠ A7), G9 (= G9), G11 (= G11), K23 (= K23), P83 (≠ A92), L84 (≠ I93), N108 (≠ C117), S109 (≠ G118), D110 (= D119), E159 (= E171), N170 (= N184), E192 (≠ G207), W209 (= W230), D211 (= D232)
- binding magnesium ion: D110 (= D119), D211 (= D232)
7x8kB Arabidopsis gdp-d-mannose pyrophosphorylase (vtc1) structure (product- bound) (see paper)
29% identity, 86% coverage: 1:333/389 of query aligns to 1:298/367 of 7x8kB
O22287 Mannose-1-phosphate guanylyltransferase 1; GDP-mannose pyrophosphorylase 1; Protein CYTOKINESIS DEFECTIVE 1; Protein EMBRYO DEFECTIVE 101; Protein HYPERSENSITIVE TO AMMONIUM ION 1; Protein SENSITIVE TO OZONE 1; Protein VITAMIN C DEFECTIVE 1; EC 2.7.7.13 from Arabidopsis thaliana (Mouse-ear cress) (see 5 papers)
29% identity, 86% coverage: 1:333/389 of query aligns to 1:298/361 of O22287
- L6 (= L6) binding GDP-alpha-D-mannose
- V7 (≠ A7) binding GDP-alpha-D-mannose
- G9 (= G9) binding diphosphate
- G11 (= G11) binding diphosphate; mutation to S: In hsn1; reduced enzyme activity, ascorbate concentrations and N-glycosylation, and increased sensitivity to ammonium.
- T12 (= T12) binding diphosphate
- R13 (= R13) binding diphosphate
- P22 (= P22) mutation to S: In vtc1-1 and vtc1-2; reduced enzyme activity and ascorbate concentrations, and ozone-sensitive.
- K23 (= K23) binding diphosphate
- D27 (≠ P27) mutation to E: Abolishes interaction with CSN5B and subsequent degradation in the dark by the 26S proteasome, and increases ascorbate accumulation in seedlings.
- G85 (= G94) binding GDP-alpha-D-mannose
- P89 (≠ G98) mutation to L: In cyt1-1; deficient in N-glycosylation and cellulose, and embryo lethal.
- N109 (≠ C117) binding GDP-alpha-D-mannose
- D111 (= D119) binding GDP-alpha-D-mannose
- G146 (= G156) binding GDP-alpha-D-mannose
- N173 (= N184) binding GDP-alpha-D-mannose
Sites not aligning to the query:
- 223:361 mutation Missing: Reduces catalytic activity 3-fold.
7x8kA Arabidopsis gdp-d-mannose pyrophosphorylase (vtc1) structure (product- bound) (see paper)
29% identity, 86% coverage: 1:333/389 of query aligns to 1:297/365 of 7x8kA
- binding guanosine-5'-diphosphate-alpha-d-mannose: V7 (≠ A7), G8 (≠ A8), E80 (= E79), G85 (= G94), P89 (≠ G98), N109 (≠ C117), D111 (= D119), G146 (= G156), E162 (= E171), N172 (= N184), G174 (= G186), E194 (= E203)
5z09A St0452(y97n)-utp binding form (see paper)
28% identity, 87% coverage: 1:338/389 of query aligns to 1:317/401 of 5z09A
- binding uridine 5'-triphosphate: L6 (= L6), A7 (= A7), A8 (= A8), G9 (= G9), S10 (≠ K10), G11 (= G11), E12 (≠ T12), R13 (= R13), Q73 (≠ E79), G79 (≠ L88), G98 (= G118), D99 (= D119)
2ggqA Complex of hypothetical glucose-1-phosphate thymidylyltransferase from sulfolobus tokodaii
28% identity, 87% coverage: 1:338/389 of query aligns to 1:317/401 of 2ggqA
- active site: R13 (= R13)
- binding thymidine-5'-triphosphate: L6 (= L6), A8 (= A8), G9 (= G9), S10 (≠ K10), G11 (= G11), E12 (≠ T12), R13 (= R13), K23 (= K23), Q73 (≠ E79), G79 (≠ L88), A83 (= A92), R179 (≠ I206), E181 (≠ G208)
Sites not aligning to the query:
Q975F9 Bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferase; EC 2.7.7.24; EC 2.7.7.9; EC 2.7.7.83; EC 2.7.7.23; EC 2.3.1.276; EC 2.3.1.157 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 3 papers)
28% identity, 87% coverage: 1:338/389 of query aligns to 1:317/401 of Q975F9
- AGSGER 8:13 (≠ AGKGTR 8:13) binding a ribonucleoside 5'-triphosphate
- Q73 (≠ E79) binding a ribonucleoside 5'-triphosphate
- G79 (≠ L88) binding a ribonucleoside 5'-triphosphate
- T80 (≠ V89) mutation T->A,G,Q: Increases both GlcNAc-1-P UTase and Glc-1-P UTase activities.; mutation T->D,H: Decrease in GlcNAc-1-P UTase activity but increase in Glc-1-P UTase activity.; mutation T->E,K,L,M,R,W,Y: Strong decrease in GlcNAc-1-P UTase activity and loss of Glc-1-P UTase activity.; mutation T->F,I: Loss of both GlcNAc-1-P UTase and Glc-1-P UTase activities.; mutation T->N,S: Strong increase in GlcNAc-1-P UTase activity and decrease in Glc-1-P UTase activity.; mutation to N: Loss of GlcNAc-1-P UTase activity; when associated with V-97.
- Y97 (≠ C117) mutation Y->A,D,F,G,I,K,T,V: Increases GlcNAc-1-P UTase activity. Decreases Glc-1-P UTase activity.; mutation Y->C,E,P,R,W: Decreases GlcNAc-1-P UTase and Glc-1-P UTase activities.; mutation Y->H,L,M,N,Q,S: Increases GlcNAc-1-P UTase and Glc-1-P UTase activities.; mutation to V: Loss of GlcNAc-1-P UTase activity; when associated with N-80.
- E146 (= E171) mutation E->A,C,F,G,I,K,L,M,P,Q,R,V,W,Y: Loss of both GlcNAc-1-P UTase and Glc-1-P UTase activities.; mutation E->D,N: Decrease in GlcNAc-1-P UTase and Glc-1-P UTase activities.; mutation E->H,S,T: Decrease in GlcNAc-1-P UTase activity and loss of Glc-1-P UTase activity.
- H308 (= H329) mutation to A: Strong decrease in GalN-1-P AcTase activity and almost loss of GlcN-1-P AcTase activity.
- Y311 (≠ R332) mutation to A: Strong decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity.
Sites not aligning to the query:
- 331 N→A: Strong decrease in GalN-1-P AcTase activity and decrease in GlcN-1-P AcTase activity.
- 337 K→A: Slight decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity.
- 340 K→A: Decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity.
- 391:401 mutation Missing: No change in GlcNAc-1-P UTase activity. Shows 38% less GalN-1-P AcTase activity than the wild-type, but increases GlcN-1-P AcTase activity 16.8 times. Significantly affects the thermostability of the entire protein.
- 397:401 mutation Missing: No change in GlcNAc-1-P UTase activity. Shows 20% less GalN-1-P AcTase activity than the wild-type, but increases GlcN-1-P AcTase activity 4.8 times. Does not affect thermostability.
4y7vA Structural analysis of muru (see paper)
29% identity, 52% coverage: 1:201/389 of query aligns to 1:187/216 of 4y7vA
Sites not aligning to the query:
Q88QT2 N-acetylmuramate alpha-1-phosphate uridylyltransferase; MurNAc-1P uridylyltransferase; MurNAc-alpha-1P uridylyltransferase; EC 2.7.7.99 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
37% identity, 33% coverage: 1:127/389 of query aligns to 1:115/223 of Q88QT2
- GER 11:13 (≠ GTR 11:13) binding UTP
- K23 (= K23) binding UTP
- N105 (≠ C117) binding substrate
- D107 (= D119) binding Mg(2+)
Sites not aligning to the query:
- 140 binding substrate
- 205 binding Mg(2+); binding substrate
4y7uA Structural analysis of muru (see paper)
37% identity, 33% coverage: 1:127/389 of query aligns to 1:115/224 of 4y7uA
Sites not aligning to the query:
Q8Z5I4 Glucose-1-phosphate cytidylyltransferase; CDP-glucose pyrophosphorylase; EC 2.7.7.33 from Salmonella typhi (see 2 papers)
28% identity, 51% coverage: 1:198/389 of query aligns to 1:200/257 of Q8Z5I4
- K23 (= K23) binding substrate
- S104 (≠ I93) binding substrate
- R109 (≠ G98) binding substrate
- G128 (= G118) binding substrate
- D129 (= D119) binding Mg(2+)
Sites not aligning to the query:
6r8uA Escherichia coli agpase in complex with amp.
25% identity, 62% coverage: 3:242/389 of query aligns to 16:280/425 of 6r8uA
Sites not aligning to the query:
5l6sC Crystal structure of e. Coli adp-glucose pyrophosphorylase (agpase) in complex with a positive allosteric regulator beta-fructose-1,6- diphosphate (fbp) - agpase Fbp (see paper)
25% identity, 62% coverage: 3:242/389 of query aligns to 9:273/418 of 5l6sC
Sites not aligning to the query:
5l6vA Crystal structure of e. Coli adp-glucose pyrophosphorylase (agpase) in complex with a negative allosteric regulator adenosine monophosphate (amp) - agpase Amp (see paper)
25% identity, 62% coverage: 3:242/389 of query aligns to 14:278/422 of 5l6vA
Sites not aligning to the query:
P0A6V1 Glucose-1-phosphate adenylyltransferase; ADP-glucose pyrophosphorylase; ADPGlc PPase; ADP-glucose synthase; EC 2.7.7.27 from Escherichia coli (strain K12) (see 11 papers)
25% identity, 62% coverage: 3:242/389 of query aligns to 22:286/431 of P0A6V1
- K39 (≠ T20) binding beta-D-fructose 1,6-bisphosphate; mutation to E: The level of activation by pyridoxal phosphate and fructose-1,6-phosphate is only approximately 2-fold compared to activation of 15- to 28-fold respectively, for the wild-type. NADPH is unable to activate the mutant enzyme.
- R40 (≠ I21) binding AMP
- A44 (≠ M25) to T: in SG14 mutant; lower apparent affinities for substrates, fructose-1,6-bisphosphate and AMP
- H46 (≠ P27) binding AMP
- R52 (≠ P32) binding AMP
- R67 (≠ D47) to C: in CL1136 mutant; less dependent on the allosteric activator, fructose-1,6-bisphosphate, for activity and less sensitive to inhibition by AMP
- Q74 (≠ S54) mutation to A: Insensitive to activation by fructose-1,6-bisphosphate, but still binds fructose-1,6-bisphosphate with similar affinity as the wild-type. AMP causes similar inhibition on the wild-type and mutant.; mutation to E: Insensitive to activation by fructose-1,6-bisphosphate.; mutation to N: The enzyme is activated 35-fold by fructose-1,6-bisphosphate.
- W113 (vs. gap) mutation to A: Insensitive to activation by fructose-1,6-bisphosphate, but still binds fructose-1,6-bisphosphate, with similar affinity as the wild-type. AMP causes similar inhibition on the wild-type and mutant.; mutation to L: The enzyme is activated only 3-fold by fructose-1,6-bisphosphate.; mutation to Y: The enzyme is activated 15-fold by fructose-1,6-bisphosphate.
- Y114 (vs. gap) mutation to F: Shows a decrease of affinity for the substrates and less than 2-fold activation by fructose 1,6-bisphosphate in the ADP-glucose synthesis direction. In contrast, in the pyrophosphorolysis direction, the mutant shoqws about a 30-fold activation by fructose 1,6-bisphosphate.
- R130 (≠ F108) binding AMP
- K195 (= K172) mutation K->E,I,H,R: Decrease of the affinity for alpha-D-glucose 1-phosphate, but no loss in adenylyltransferase activity.; mutation to Q: 600-fold decrease of the affinity for alpha-D-glucose 1-phosphate compared to the wild-type. In contrast, kinetic constants for ATP, magnesium and fructose-1,6-bisphosphate are similar in mutant and wild-type cases. The catalytic efficiency is 2-fold lower in the mutant.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 295 P → S: in SG5 mutant
- 336 G → D: in 618 mutant; causes lowered affinity for AMP
- 370 binding AMP
- 386 binding AMP
- 419:423 binding beta-D-fructose 1,6-bisphosphate
- 429:431 binding beta-D-fructose 1,6-bisphosphate
Query Sequence
>WP_011320144.1 NCBI__GCF_000204075.1:WP_011320144.1
MKAMILAAGKGTRVRPITYTIPKPMIPILQKPVMEFLLELLRQHGFDQIMVNVSHLAEEI
ENYFRDGQRFGVQIAYSFEGKIDDEGKLVGEAIGSAGGMRRIQDFSPFFDDTFVVLCGDA
LIDLDLTAAVKWHKSKGSIATIITKTVPEEEVSSYGVVVTDENSRVKAFQEKPSIEEALS
TNINTGIYIFEPEVFNYIPSGVEYDIGGQLFPKLVEIGAPFYAIAMDFEWVDIGKVPDYW
RAIRGVLQGEIKNVQIPGHEVAPGIYTGLNVAVNWDKVDITGPVYIGGMTRIEDGAKIVG
PAMIGPNCWICGEATVDNSVIFEWSRLGHGARLVDKLVFGRYCVDKTGAAIDVQAAALDW
LITDARQTPPEHTPVERQAIAELLGTNAI
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