SitesBLAST
Comparing CCNA_03752 FitnessBrowser__Caulo:CCNA_03752 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 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, 97% coverage: 7:296/298 of query aligns to 1:287/288 of 2ux8G
5i1fA Crystal structure of utp-glucose-1-phosphate uridylyltransferase from burkholderia vietnamiensis in complex with uridine-5'-diphosphate- glucose
47% identity, 94% coverage: 8:286/298 of query aligns to 2:279/290 of 5i1fA
- binding uridine-5'-diphosphate-glucose: P11 (= P17), A13 (= A19), G14 (= G20), K28 (= K34), E29 (= E35), Q106 (= Q112), A109 (≠ P115), L110 (= L116), G111 (= G117), L112 (= L118), A115 (= A121), D135 (≠ V141), Y172 (= Y179), G173 (= G180), E192 (= E199), K193 (= K200), V205 (≠ I212)
2ux8A Crystal structure of sphingomonas elodea atcc 31461 glucose-1- phosphate uridylyltransferase in complex with glucose-1-phosphate. (see paper)
48% identity, 97% coverage: 7:296/298 of query aligns to 1:254/255 of 2ux8A
5ve7A Crystal structure of utp-glucose-1-phosphate uridylyltransferase from burkholderia ambifaria in complex with utp
48% identity, 93% coverage: 11:286/298 of query aligns to 3:273/282 of 5ve7A
- binding uridine 5'-triphosphate: P9 (= P17), V10 (= V18), A11 (= A19), G12 (= G20), G14 (= G22), T15 (= T23), R16 (= R24), K26 (= K34), E27 (= E35), Q104 (= Q112), A107 (≠ P115), G109 (= G117), A113 (= A121)
6knlA Uridine and triphosphate-bound ugpase from acinetobacter baumannii
46% identity, 92% coverage: 11:285/298 of query aligns to 2:279/290 of 6knlA
- binding triphosphate: G13 (= G22), T14 (= T23), R15 (= R24), K79 (= K88), K81 (= K90)
- binding uridine: P8 (= P17), G11 (= G20), K25 (= K34), Q103 (= Q112), P106 (= P115), G108 (= G117), P130 (= P139), D131 (= D140)
6k8dA Udp-glucose pyrophosphorylase with upg from acinetobacter baumanii
46% identity, 92% coverage: 11:285/298 of query aligns to 2:279/290 of 6k8dA
- binding uridine-5'-diphosphate-glucose: P8 (= P17), A10 (= A19), G11 (= G20), Q103 (= Q112), P106 (= P115), G108 (= G117), L109 (= L118), A112 (= A121), L129 (= L138), D131 (= D140), E193 (= E199), V206 (≠ I212)
6ikzB Udp-glucose pyrophosphorylase from acinetobacter baumanii
44% identity, 92% coverage: 11:285/298 of query aligns to 2:274/285 of 6ikzB
- binding uridine 5'-triphosphate: P8 (= P17), V9 (= V18), A10 (= A19), G11 (= G20), L12 (= L21), G13 (= G22), T14 (= T23), R15 (= R24), K25 (= K34), Q103 (= Q112), P106 (= P115), G108 (= G117), D131 (= D140)
8f73E Crystal structure of pseudomonas aeruginosa udp-glucose phosphorylase in complex with udp-glucose
43% identity, 89% coverage: 11:274/298 of query aligns to 8:271/281 of 8f73E
- binding uridine-5'-diphosphate-glucose: P14 (= P17), A16 (= A19), G17 (= G20), K31 (= K34), E32 (= E35), Q108 (= Q112), G113 (= G117), L114 (= L118), A117 (= A121), L134 (= L138), D137 (vs. gap), E196 (= E199), K197 (= K200), I209 (= I212)
3jukA The crystal structure of udp-glucose pyrophosphorylase complexed with udp-glucose (see paper)
40% identity, 91% coverage: 11:281/298 of query aligns to 2:264/265 of 3jukA
- binding uridine-5'-diphosphate-glucose: A10 (= A19), G11 (= G20), E26 (= E35), Q94 (= Q112), M97 (≠ P115), G99 (= G117), L100 (= L118), A103 (= A121), D123 (vs. gap), Y162 (= Y179), G163 (= G180), E182 (= E199), K183 (= K200), V195 (≠ I212)
3jukD The crystal structure of udp-glucose pyrophosphorylase complexed with udp-glucose (see paper)
40% identity, 91% coverage: 11:281/298 of query aligns to 2:264/264 of 3jukD
- binding magnesium ion: T14 (= T23), R15 (= R24)
- binding uridine-5'-diphosphate-glucose: P8 (= P17), A10 (= A19), G11 (= G20), E26 (= E35), Q94 (= Q112), M97 (≠ P115), G99 (= G117), L100 (= L118), A103 (= A121), L120 (= L138), D123 (vs. gap), Y162 (= Y179), G163 (= G180), E182 (= E199), K183 (= K200), V195 (≠ I212)
8b6dA Crystal structure of udp-glucose pyrophosphorylase from thermocrispum agreste dsm 44070 in complex with udp
43% identity, 93% coverage: 14:290/298 of query aligns to 5:282/291 of 8b6dA
- binding uridine-5'-diphosphate: P8 (= P17), A10 (= A19), G11 (= G20), L12 (= L21), G13 (= G22), T14 (= T23), R15 (= R24), K25 (= K34), Q102 (= Q112), A105 (≠ P115), G107 (= G117), A111 (= A121)
8b68A Crystal structure of udp-glucose pyrophosphorylase from thermocrispum agreste dsm 44070 in complex with udp-glucose
41% identity, 93% coverage: 14:290/298 of query aligns to 5:277/286 of 8b68A
- binding uridine-5'-diphosphate-glucose: P8 (= P17), A10 (= A19), G11 (= G20), Q102 (= Q112), A105 (≠ P115), G107 (= G117), A111 (= A121), L130 (= L138), P131 (= P139), D133 (≠ V141), A203 (≠ I212), G205 (= G214)
2pa4B Crystal structure of udp-glucose pyrophosphorylase from corynebacteria glutamicum in complex with magnesium and udp-glucose (see paper)
37% identity, 96% coverage: 11:296/298 of query aligns to 3:290/299 of 2pa4B
- binding uridine-5'-diphosphate-glucose: P9 (= P17), A10 (≠ V18), A11 (= A19), G12 (= G20), E27 (= E35), Q103 (= Q112), P106 (= P115), G108 (= G117), L109 (= L118), L131 (= L138), P132 (= P139), D134 (≠ V141), Y170 (= Y179), G171 (= G180), E192 (= E199), K193 (= K200), A205 (≠ I212)
7d73E Cryo-em structure of gmppa/gmppb complex bound to gtp (state i) (see paper)
30% identity, 76% coverage: 13:237/298 of query aligns to 2:197/360 of 7d73E
- binding guanosine-5'-triphosphate: L6 (≠ P17), V7 (= V18), G8 (≠ A19), G9 (= G20), G11 (= G22), T12 (= T23), R13 (= R24), A52 (≠ V63), S54 (≠ G65), E80 (≠ Q112), P83 (= P115), G85 (= G117), N108 (≠ L138)
7d72K Cryo-em structures of human gmppa/gmppb complex bound to gdp-mannose (see paper)
30% identity, 76% coverage: 13:237/298 of query aligns to 2:197/360 of 7d72K
Sites not aligning to the query:
7d72E Cryo-em structures of human gmppa/gmppb complex bound to gdp-mannose (see paper)
30% identity, 76% coverage: 13:237/298 of query aligns to 2:197/360 of 7d72E
Sites not aligning to the query:
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)
26% identity, 77% coverage: 13:242/298 of query aligns to 2:216/388 of P74285
- A8 (= A19) 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
25% identity, 88% coverage: 13:274/298 of query aligns to 2:219/401 of 2ggqA
- active site: R13 (= R24)
- binding thymidine-5'-triphosphate: L6 (≠ P17), A8 (= A19), G9 (= G20), S10 (≠ L21), G11 (= G22), E12 (≠ T23), R13 (= R24), K23 (= K34), Q73 (= Q112), G79 (= G117), A83 (= A121), R179 (≠ G234), E181 (= E236)
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)
25% identity, 88% coverage: 13:274/298 of query aligns to 2:219/401 of Q975F9
- AGSGER 8:13 (≠ AGLGTR 19:24) binding
- Q73 (= Q112) binding
- G79 (= G117) binding
- T80 (≠ L118) 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 (≠ L138) 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 (= E199) 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.
7x8kB Arabidopsis gdp-d-mannose pyrophosphorylase (vtc1) structure (product- bound) (see paper)
26% identity, 85% coverage: 13:265/298 of query aligns to 2:221/367 of 7x8kB
Query Sequence
>CCNA_03752 FitnessBrowser__Caulo:CCNA_03752
MSADEMSMKPVRKAVLPVAGLGTRVLPGTKTTPKELLNVVDRPILSYIVEEGRKAGIEHF
VFVTGRSKGAIEDYFDHQIELEAQLEAKGKIEILEQLRAELPKPGEMSFVRQMAPLGLGH
AVWCARDIIGDEPFAVMLPDVIVDAERACLGQLIDLYNKVGGGNVIGVEEVPESETHKYG
VVAPGKVDGRMATMTGMVEKPAKGTAPSNWAIAGRYILQPEIFALLAAQEKGAGNEIQLT
DSMAKLMQDQAFHAYVYEGVTHDCGDKIGLLRANVALALKRADLGAAARAAVEAALKA
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