SitesBLAST
Comparing 6938102 FitnessBrowser__SB2B:6938102 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)
6knlA Uridine and triphosphate-bound ugpase from acinetobacter baumannii
57% identity, 97% coverage: 6:297/302 of query aligns to 2:289/290 of 6knlA
- binding triphosphate: G13 (= G17), T14 (= T18), R15 (= R19), K79 (≠ R83), 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
57% identity, 97% coverage: 6:297/302 of query aligns to 2:289/290 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 (= E201), V206 (= V214)
6ikzB Udp-glucose pyrophosphorylase from acinetobacter baumanii
56% identity, 97% coverage: 6:297/302 of query aligns to 2:284/285 of 6ikzB
- binding uridine 5'-triphosphate: P8 (= P12), V9 (= V13), A10 (= A14), G11 (= G15), L12 (= L16), G13 (= G17), T14 (= T18), R15 (= R19), K25 (= K29), Q103 (= Q107), P106 (≠ A110), G108 (= G112), D131 (= D135)
5i1fA Crystal structure of utp-glucose-1-phosphate uridylyltransferase from burkholderia vietnamiensis in complex with uridine-5'-diphosphate- glucose
52% identity, 96% coverage: 5:294/302 of query aligns to 4:285/290 of 5i1fA
- binding uridine-5'-diphosphate-glucose: P11 (= P12), A13 (= A14), G14 (= G15), K28 (= K29), E29 (= E30), Q106 (= Q107), A109 (= A110), L110 (≠ K111), G111 (= G112), L112 (= L113), A115 (= A116), D135 (≠ V136), Y172 (= Y178), G173 (= G179), E192 (= E201), K193 (= K202), V205 (= V214)
5ve7A Crystal structure of utp-glucose-1-phosphate uridylyltransferase from burkholderia ambifaria in complex with utp
53% identity, 96% coverage: 5:295/302 of query aligns to 2:280/282 of 5ve7A
- binding uridine 5'-triphosphate: P9 (= P12), V10 (= V13), A11 (= A14), G12 (= G15), G14 (= G17), T15 (= T18), R16 (= R19), K26 (= K29), E27 (= E30), Q104 (= Q107), A107 (= A110), G109 (= G112), A113 (= A116)
2ux8G Crystal structure of sphingomonas elodea atcc 31461 glucose-1- phosphate uridylyltransferase in complex with glucose-1-phosphate. (see paper)
47% identity, 93% coverage: 6:286/302 of query aligns to 5:275/288 of 2ux8G
8f73E Crystal structure of pseudomonas aeruginosa udp-glucose phosphorylase in complex with udp-glucose
45% identity, 90% coverage: 6:276/302 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 (≠ V136), E196 (= E201), K197 (= K202), I209 (≠ V214)
3jukD The crystal structure of udp-glucose pyrophosphorylase complexed with udp-glucose (see paper)
42% identity, 91% coverage: 6:279/302 of query aligns to 2:260/264 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 (= D139), Y162 (= Y178), G163 (= G179), E182 (= E201), K183 (= K202), V195 (= V214)
3jukA The crystal structure of udp-glucose pyrophosphorylase complexed with udp-glucose (see paper)
42% identity, 91% coverage: 6:279/302 of query aligns to 2:260/265 of 3jukA
- binding uridine-5'-diphosphate-glucose: A10 (= A14), G11 (= G15), E26 (= E30), Q94 (= Q107), M97 (≠ A110), G99 (= G112), L100 (= L113), A103 (= A116), D123 (= D139), Y162 (= Y178), G163 (= G179), E182 (= E201), K183 (= K202), V195 (= V214)
2ux8A Crystal structure of sphingomonas elodea atcc 31461 glucose-1- phosphate uridylyltransferase in complex with glucose-1-phosphate. (see paper)
41% identity, 93% coverage: 6:286/302 of query aligns to 5:242/255 of 2ux8A
8b6dA Crystal structure of udp-glucose pyrophosphorylase from thermocrispum agreste dsm 44070 in complex with udp
39% identity, 96% coverage: 9:298/302 of query aligns to 5:288/291 of 8b6dA
- binding uridine-5'-diphosphate: P8 (= P12), A10 (= A14), G11 (= G15), L12 (= L16), 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
38% identity, 96% coverage: 9:298/302 of query aligns to 5:283/286 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 (≠ V136), A203 (≠ V214), G205 (= G216)
2pa4B Crystal structure of udp-glucose pyrophosphorylase from corynebacteria glutamicum in complex with magnesium and udp-glucose (see paper)
37% identity, 97% coverage: 6:298/302 of query aligns to 3:290/299 of 2pa4B
- binding uridine-5'-diphosphate-glucose: P9 (= P12), A10 (≠ V13), A11 (= A14), G12 (= G15), E27 (= E30), Q103 (= Q107), P106 (≠ A110), G108 (= G112), L109 (= L113), L131 (= L133), P132 (= P134), D134 (≠ V136), Y170 (= Y178), G171 (= G179), E192 (= E201), K193 (= K202), A205 (≠ V214)
5z09A St0452(y97n)-utp binding form (see paper)
28% identity, 91% coverage: 8:281/302 of query aligns to 2:223/401 of 5z09A
- binding uridine 5'-triphosphate: L6 (≠ P12), A7 (≠ V13), A8 (= A14), G9 (= G15), S10 (≠ L16), G11 (= G17), E12 (≠ T18), R13 (= R19), Q73 (≠ P97), G79 (= G112), G98 (= G140), D99 (= D144)
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)
28% identity, 72% coverage: 8:224/302 of query aligns to 2:193/388 of P74285
- A8 (= A14) mutation to G: Two-fold decrease in affinity for UTP. No effect on affinity for Glc-1P and on catalytic activity rate.
2ggqA Complex of hypothetical glucose-1-phosphate thymidylyltransferase from sulfolobus tokodaii
27% identity, 91% coverage: 8:281/302 of query aligns to 2:223/401 of 2ggqA
- active site: R13 (= R19)
- binding thymidine-5'-triphosphate: L6 (≠ P12), A8 (= A14), G9 (= G15), S10 (≠ L16), G11 (= G17), E12 (≠ T18), R13 (= R19), K23 (= K29), Q73 (≠ P97), G79 (= G112), A83 (= A116), R179 (≠ G236), E181 (= E238)
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)
27% identity, 91% coverage: 8:281/302 of query aligns to 2:223/401 of Q975F9
- AGSGER 8:13 (≠ AGLGTR 14:19) binding
- Q73 (≠ P97) binding
- G79 (= G112) binding
- 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 (≠ L132) 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 (= E201) 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.
5fuhA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor
29% identity, 82% coverage: 7:255/302 of query aligns to 8:218/298 of 5fuhA
Sites not aligning to the query:
4b4bA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
29% identity, 82% coverage: 7:255/302 of query aligns to 8:218/298 of 4b4bA
Sites not aligning to the query:
5fu8A Pseudomonas aeruginosa rmla in complex with allosteric inhibitor
29% identity, 82% coverage: 7:255/302 of query aligns to 7:217/297 of 5fu8A
Sites not aligning to the query:
Query Sequence
>6938102 FitnessBrowser__SB2B:6938102
MRQTKIRKAVIPVAGLGTRMLPATKAIPKEMLPVVDKPLIQYVVSEAVAAGIKEIVLVTH
ASKNSIENHFDTSFELEAQLERRVKRQLLDEVQAICPKDVTVISVRQAQAKGLGHAILCA
RPVVGDEPFAVLLPDVIIDGAKSDLTSENLAAMVRLFDETSTGQIMVEAVPHEMVNQYGI
ADVKGHQMVNGDSVPLEALVEKPAVDEAPSNLAVVGRYVLPADIWPLLARTPAGAGDEIQ
LTDAIAMLMESAQVNAYGMVGKSHDCGNKQGYMQANVEYALRHPELGKEFAKYLKQLVKG
LN
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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