SitesBLAST
Comparing WP_002719715.1 NCBI__GCF_000015985.1:WP_002719715.1 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)
2ux8G Crystal structure of sphingomonas elodea atcc 31461 glucose-1- phosphate uridylyltransferase in complex with glucose-1-phosphate. (see paper)
56% identity, 89% coverage: 9:287/312 of query aligns to 8:282/288 of 2ux8G
5i1fA Crystal structure of utp-glucose-1-phosphate uridylyltransferase from burkholderia vietnamiensis in complex with uridine-5'-diphosphate- glucose
51% identity, 92% coverage: 5:290/312 of query aligns to 4:287/290 of 5i1fA
- binding uridine-5'-diphosphate-glucose: P11 (= P12), A13 (= A14), G14 (= G15), K28 (= K29), E29 (= E30), Q106 (= Q107), A109 (= A110), L110 (= L111), G111 (= G112), L112 (= L113), A115 (= A116), D135 (= D136), Y172 (= Y173), G173 (= G174), E192 (= E193), K193 (= K194), V205 (= V206)
5ve7A Crystal structure of utp-glucose-1-phosphate uridylyltransferase from burkholderia ambifaria in complex with utp
49% identity, 91% coverage: 5:289/312 of query aligns to 2:280/282 of 5ve7A
- binding uridine 5'-triphosphate: P9 (= P12), V10 (≠ I13), A11 (= A14), G12 (= G15), G14 (= G17), T15 (= T18), R16 (= R19), K26 (= K29), E27 (= E30), Q104 (= Q107), A107 (= A110), G109 (= G112), A113 (= A116)
2ux8A Crystal structure of sphingomonas elodea atcc 31461 glucose-1- phosphate uridylyltransferase in complex with glucose-1-phosphate. (see paper)
48% identity, 89% coverage: 9:287/312 of query aligns to 8:249/255 of 2ux8A
6knlA Uridine and triphosphate-bound ugpase from acinetobacter baumannii
46% identity, 91% coverage: 6:288/312 of query aligns to 2:286/290 of 6knlA
- binding triphosphate: G13 (= G17), T14 (= T18), R15 (= R19), K79 (≠ A83), K81 (= K85)
- binding uridine: P8 (= P12), G11 (= G15), K25 (= K29), Q103 (= Q107), P106 (≠ A110), G108 (= G112), P130 (= P134), D131 (= D135)
6k8dA Udp-glucose pyrophosphorylase with upg from acinetobacter baumanii
46% identity, 91% coverage: 6:288/312 of query aligns to 2:286/290 of 6k8dA
- binding uridine-5'-diphosphate-glucose: P8 (= P12), A10 (= A14), G11 (= G15), Q103 (= Q107), P106 (≠ A110), G108 (= G112), L109 (= L113), A112 (= A116), L129 (= L133), D131 (= D135), E193 (= E193), V206 (= V206)
8f73E Crystal structure of pseudomonas aeruginosa udp-glucose phosphorylase in complex with udp-glucose (see paper)
46% identity, 85% coverage: 6:270/312 of query aligns to 8:271/281 of 8f73E
- binding uridine-5'-diphosphate-glucose: P14 (= P12), A16 (= A14), G17 (= G15), K31 (= K29), E32 (= E30), Q108 (= Q107), G113 (= G112), L114 (= L113), A117 (= A116), L134 (= L133), D137 (= D136), E196 (= E193), K197 (= K194), I209 (≠ V206)
6ikzB Udp-glucose pyrophosphorylase from acinetobacter baumanii
45% identity, 91% coverage: 6:288/312 of query aligns to 2:281/285 of 6ikzB
- binding uridine 5'-triphosphate: P8 (= P12), V9 (≠ I13), A10 (= A14), G11 (= G15), L12 (≠ M16), G13 (= G17), T14 (= T18), R15 (= R19), K25 (= K29), Q103 (= Q107), P106 (≠ A110), G108 (= G112), D131 (= D135)
3jukA The crystal structure of udp-glucose pyrophosphorylase complexed with udp-glucose (see paper)
44% identity, 87% coverage: 6:277/312 of query aligns to 2:264/265 of 3jukA
- binding uridine-5'-diphosphate-glucose: A10 (= A14), G11 (= G15), E26 (= E30), Q94 (= Q107), M97 (≠ A110), G99 (= G112), L100 (= L113), A103 (= A116), D123 (= D136), Y162 (= Y173), G163 (= G174), E182 (= E193), K183 (= K194), V195 (= V206)
3jukD The crystal structure of udp-glucose pyrophosphorylase complexed with udp-glucose (see paper)
44% identity, 87% coverage: 6:277/312 of query aligns to 2:264/264 of 3jukD
- binding magnesium ion: T14 (= T18), R15 (= R19)
- binding uridine-5'-diphosphate-glucose: P8 (= P12), A10 (= A14), G11 (= G15), E26 (= E30), Q94 (= Q107), M97 (≠ A110), G99 (= G112), L100 (= L113), A103 (= A116), L120 (= L133), D123 (= D136), Y162 (= Y173), G163 (= G174), E182 (= E193), K183 (= K194), V195 (= V206)
8b6dA Crystal structure of udp-glucose pyrophosphorylase from thermocrispum agreste dsm 44070 in complex with udp
44% identity, 90% coverage: 7:288/312 of query aligns to 3:284/291 of 8b6dA
- binding uridine-5'-diphosphate: P8 (= P12), A10 (= A14), G11 (= G15), L12 (≠ M16), G13 (= G17), T14 (= T18), R15 (= R19), K25 (= K29), Q102 (= Q107), A105 (= A110), G107 (= G112), A111 (= A116)
8b68A Crystal structure of udp-glucose pyrophosphorylase from thermocrispum agreste dsm 44070 in complex with udp-glucose
42% identity, 90% coverage: 7:288/312 of query aligns to 3:279/286 of 8b68A
- binding uridine-5'-diphosphate-glucose: P8 (= P12), A10 (= A14), G11 (= G15), Q102 (= Q107), A105 (= A110), G107 (= G112), A111 (= A116), L130 (= L133), P131 (= P134), D133 (= D136), A203 (≠ V206), G205 (= G208)
2pa4B Crystal structure of udp-glucose pyrophosphorylase from corynebacteria glutamicum in complex with magnesium and udp-glucose (see paper)
37% identity, 93% coverage: 6:295/312 of query aligns to 3:293/299 of 2pa4B
- binding uridine-5'-diphosphate-glucose: P9 (= P12), A10 (≠ I13), A11 (= A14), G12 (= G15), E27 (= E30), Q103 (= Q107), P106 (≠ A110), G108 (= G112), L109 (= L113), L131 (= L133), P132 (= P134), D134 (= D136), Y170 (= Y173), G171 (= G174), E192 (= E193), K193 (= K194), A205 (≠ V206)
5z09A St0452(y97n)-utp binding form (see paper)
26% identity, 82% coverage: 14:270/312 of query aligns to 8:219/401 of 5z09A
Sites not aligning to the query:
2ggqA Complex of hypothetical glucose-1-phosphate thymidylyltransferase from sulfolobus tokodaii
26% identity, 82% coverage: 14:270/312 of query aligns to 8:219/401 of 2ggqA
- active site: R13 (= R19)
- binding thymidine-5'-triphosphate: A8 (= A14), G9 (= G15), S10 (≠ M16), G11 (= G17), E12 (≠ T18), R13 (= R19), K23 (= K29), Q73 (= Q107), G79 (= G112), A83 (= A116), R179 (≠ G228), E181 (= E230)
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)
26% identity, 82% coverage: 14:270/312 of query aligns to 8:219/401 of Q975F9
- AGSGER 8:13 (≠ AGMGTR 14:19) binding a ribonucleoside 5'-triphosphate
- Q73 (= Q107) binding a ribonucleoside 5'-triphosphate
- G79 (= G112) binding a ribonucleoside 5'-triphosphate
- T80 (≠ L113) 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 (≠ P134) 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 (= E193) 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.
Sites not aligning to the query:
- 308 H→A: Strong decrease in GalN-1-P AcTase activity and almost loss of GlcN-1-P AcTase activity.
- 311 Y→A: Strong decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity.
- 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.
7d73E Cryo-em structure of gmppa/gmppb complex bound to gtp (state i) (see paper)
28% identity, 83% coverage: 9:267/312 of query aligns to 3:226/360 of 7d73E
- binding guanosine-5'-triphosphate: L6 (≠ P12), V7 (≠ I13), G8 (≠ A14), G9 (= G15), G11 (= G17), T12 (= T18), R13 (= R19), A52 (≠ V58), S54 (= S60), E80 (≠ Q107), P83 (≠ A110), G85 (= G112), N108 (≠ L133)
7d72K Cryo-em structures of human gmppa/gmppb complex bound to gdp-mannose (see paper)
28% identity, 83% coverage: 9:267/312 of query aligns to 3:226/360 of 7d72K
- binding guanosine-5'-diphosphate-alpha-d-mannose: L6 (≠ P12), V7 (≠ I13), G8 (≠ A14), G85 (= G112), T86 (≠ L113), N108 (≠ L133), S109 (≠ P134), D110 (= D135), N172 (≠ V206), E194 (≠ G228), D218 (= D259)
7d72E Cryo-em structures of human gmppa/gmppb complex bound to gdp-mannose (see paper)
28% identity, 83% coverage: 9:267/312 of query aligns to 3:226/360 of 7d72E
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)
28% identity, 69% coverage: 9:223/312 of query aligns to 3:190/361 of O22287
- L6 (≠ P12) binding GDP-alpha-D-mannose
- V7 (≠ I13) binding GDP-alpha-D-mannose
- G9 (= G15) binding diphosphate
- G11 (= G17) binding diphosphate; mutation to S: In hsn1; reduced enzyme activity, ascorbate concentrations and N-glycosylation, and increased sensitivity to ammonium.
- T12 (= T18) binding diphosphate
- R13 (= R19) binding diphosphate
- P22 (= P28) mutation to S: In vtc1-1 and vtc1-2; reduced enzyme activity and ascorbate concentrations, and ozone-sensitive.
- K23 (= K29) binding diphosphate
- D27 (≠ T33) mutation to E: Abolishes interaction with CSN5B and subsequent degradation in the dark by the 26S proteasome, and increases ascorbate accumulation in seedlings.
- G85 (≠ A90) binding GDP-alpha-D-mannose
- P89 (≠ H101) mutation to L: In cyt1-1; deficient in N-glycosylation and cellulose, and embryo lethal.
- N109 (≠ L133) binding GDP-alpha-D-mannose
- D111 (= D135) binding GDP-alpha-D-mannose
- G146 (= G174) binding GDP-alpha-D-mannose
- N173 (≠ V206) binding GDP-alpha-D-mannose
Sites not aligning to the query:
- 223:361 mutation Missing: Reduces catalytic activity 3-fold.
Query Sequence
>WP_002719715.1 NCBI__GCF_000015985.1:WP_002719715.1
MSSQKVTTAIFPIAGMGTRFLPATKSIPKEILTLVDKPLIQYAVEEAREAGIEDFIFVTS
RGKGALEDFFDVNQTLERALRAAGKTELLATLEATNIDSGHVTYVRQHEALGLGHAVWCA
RRLVGDEPFAVILPDDMVVADKPCLAQMIAAHEEVGGSIIATMEVPAEKASSYGVLDIEE
RQGALIRPRGIVEKPKAGTAPSNMAVIGRYILGPRVMQHLDRRTVGAGGEIQLTDAIAHE
LATHPGSVHGFRFQGERFDCGSKAGFLQATVALALEREDLRGEFSTFLRAIAEQHGLGAP
SAAPLRSVAAAS
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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