SitesBLAST
Comparing CCNA_02389 FitnessBrowser__Caulo:CCNA_02389 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)
P43889 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see 3 papers)
41% identity, 95% coverage: 13:451/462 of query aligns to 7:455/456 of P43889
- LAAG 11:14 (= LAAG 17:20) binding
- K25 (= K31) mutation to A: No pyrophosphorylase activity.
- Q76 (= Q84) binding ; mutation to A: No pyrophosphorylase activity.
- GT 81:82 (= GT 89:90) binding
- Y103 (= Y112) mutation to A: Reduces the pyrophosphorylase activity.
- YGD 103:105 (≠ YAD 112:114) binding
- D105 (= D114) mutation to A: No pyrophosphorylase activity.
- G140 (= G150) binding
- E154 (= E165) binding
- N169 (= N180) binding
- V223 (= V233) mutation to A: Reduces slightly the pyrophosphorylase activity.
- E224 (≠ Q234) mutation to A: Reduces the pyrophosphorylase activity.
2v0jA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/449 of 2v0jA
4kqlA Hin glmu bound to wg578 (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 4kqlA
- active site: R15 (= R24)
- binding N-(4-{[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-methoxybenzoyl]amino}phenyl)pyridine-2-carboxamide: A9 (= A18), A10 (= A19), Q73 (= Q84), Q76 (≠ P87), G78 (= G89), T79 (= T90), Y100 (= Y112), D102 (= D114), Y136 (= Y149), T167 (≠ S181), V220 (= V233), G222 (= G235)
4kpzA Hin glmu bound to a small molecule fragment (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 4kpzA
- active site: R15 (= R24)
- binding 1-(3-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione: L8 (= L17), A9 (= A18), A10 (= A19), G11 (= G20), V23 (= V32), Q73 (= Q84), Q76 (≠ P87), G78 (= G89), D102 (= D114)
4kpxA Hin glmu bound to wg766 (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 4kpxA
4knxA Hin glmu bound to wg176 (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 4knxA
- active site: R15 (= R24)
- binding [(4-{[4-(benzoylamino)phenyl]amino}-6-methoxyquinazolin-7-yl)oxy]acetic acid: L8 (= L17), A10 (= A19), G11 (= G20), Q73 (= Q84), Q76 (≠ P87), T79 (= T90), Y100 (= Y112), D102 (= D114), Y136 (= Y149), T167 (≠ S181), V220 (= V233), G222 (= G235)
4knrA Hin glmu bound to wg188 (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 4knrA
4e1kA Glmu in complex with a quinazoline compound (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 4e1kA
2w0wA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 2
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 2w0wA
- active site: R15 (= R24)
- binding n-{6-(cyclopropylmethoxy)-7-methoxy-2-[6-(2-methylpropyl)-5-oxo-3,4,5,6-tetrahydro-2,6-naphthyridin-2(1h)-yl]quinazolin-4-yl}-2,2,2-trifluoroethanesulfonamide: L8 (= L17), G11 (= G20), Q73 (= Q84), T79 (= T90), Y100 (= Y112), D102 (= D114), Y136 (= Y149), N166 (= N180), T167 (≠ S181), G168 (= G182), V220 (= V233), G222 (= G235)
Sites not aligning to the query:
2w0vA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 1
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 2w0vA
- active site: R15 (= R24)
- binding 6-(cycloprop-2-en-1-ylmethoxy)-2-[6-(cyclopropylmethyl)-5-oxo-3,4,5,6-tetrahydro-2,6-naphthyridin-2(1h)-yl]-7-methoxyquinazolin-4(3h)-one: L8 (= L17), G11 (= G20), Y100 (= Y112), D102 (= D114), V128 (≠ F141), T167 (≠ S181), V220 (= V233), G222 (= G235)
Sites not aligning to the query:
2vd4A Structure of small-molecule inhibitor of glmu from haemophilus influenzae reveals an allosteric binding site (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 2vd4A
2v0lA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 2v0lA
Sites not aligning to the query:
2v0kA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1- phosphate uridyltransferase (glmu) (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 2v0kA
2v0iA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 93% coverage: 13:442/462 of query aligns to 4:446/450 of 2v0iA
- active site: R15 (= R24)
- binding uridine-diphosphate-n-acetylglucosamine: A10 (= A19), Q73 (= Q84), Q76 (≠ P87), G78 (= G89), T79 (= T90), D102 (= D114), Y136 (= Y149), G137 (= G150), E151 (= E165), N166 (= N180), T167 (≠ S181), Y194 (= Y208), T196 (= T210)
Sites not aligning to the query:
Q97R46 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) (see 2 papers)
39% identity, 94% coverage: 14:446/462 of query aligns to 5:452/459 of Q97R46
P0ACC7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Escherichia coli (strain K12) (see 6 papers)
40% identity, 93% coverage: 13:442/462 of query aligns to 7:449/456 of P0ACC7
- LAAG 11:14 (= LAAG 17:20) binding
- G14 (= G20) mutation to A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP.
- R18 (= R24) mutation to A: Dramatically impairs the uridyltransferase activity.
- K25 (= K31) mutation to A: 8-fold decrease in uridyltransferase activity.
- Q76 (= Q84) binding
- GT 81:82 (= GT 89:90) binding
- YGD 103:105 (≠ YAD 112:114) binding
- D105 (= D114) binding ; binding
- G140 (= G150) binding
- E154 (= E165) binding
- N169 (= N180) binding
- N227 (= N237) binding ; binding
- 230:250 (vs. 240:260, 24% identical) Linker
- C296 (≠ A300) mutation to A: No effect.
- C307 (vs. gap) mutation to A: 1350-fold decrease in acetyltransferase activity.
- C324 (≠ A317) mutation to A: 8-fold decrease in acetyltransferase activity.
- R333 (= R326) binding
- K351 (= K344) binding
- Y366 (= Y359) binding
- N377 (= N370) binding
- A380 (= A373) binding
- C385 (= C378) mutation to A: No effect.
- S405 (= S398) binding
- A423 (≠ S416) binding
- R440 (= R433) binding
Sites not aligning to the query:
- 1:229 Pyrophosphorylase
- 251:456 N-acetyltransferase
2oi6B E. Coli glmu- complex with udp-glcnac, coa and glcn-1-po4 (see paper)
40% identity, 93% coverage: 13:442/462 of query aligns to 5:447/452 of 2oi6B
- active site: R16 (= R24)
- binding coenzyme a: G402 (= G397), S403 (= S398), A420 (≠ G415), A421 (≠ S416), R438 (= R433)
- binding 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: H361 (= H356), N375 (= N370)
- binding magnesium ion: D103 (= D114), N225 (= N237)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L17), A10 (= A18), A11 (= A19), G12 (= G20), Q74 (= Q84), Q77 (≠ P87), G79 (= G89), T80 (= T90), Y101 (= Y112), D103 (= D114), Y137 (= Y149), G138 (= G150), E152 (= E165), N167 (= N180), T168 (≠ S181), T197 (= T210), N225 (= N237)
1hv9B Structure of e. Coli glmu: analysis of pyrophosphorylase and acetyltransferase active sites (see paper)
40% identity, 93% coverage: 13:442/462 of query aligns to 5:447/450 of 1hv9B
- active site: R16 (= R24)
- binding cobalt (ii) ion: D103 (= D114), N225 (= N237)
- binding coenzyme a: G402 (= G397), S403 (= S398), A420 (≠ G415), A421 (≠ S416), R438 (= R433)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L17), A10 (= A18), A11 (= A19), G12 (= G20), Q74 (= Q84), Q77 (≠ P87), G79 (= G89), T80 (= T90), Y101 (= Y112), D103 (= D114), Y137 (= Y149), G138 (= G150), E152 (= E165), N167 (= N180), T197 (= T210), N225 (= N237)
2oi7A E. Coli glmu- complex with udp-glcnac, desulpho-coa and glcnac-1-po4 (see paper)
40% identity, 93% coverage: 13:442/462 of query aligns to 4:446/449 of 2oi7A
- active site: R15 (= R24)
- binding desulfo-coenzyme a: G401 (= G397), S402 (= S398), A419 (≠ G415), A420 (≠ S416), R437 (= R433)
- binding 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: K357 (= K353), H360 (= H356), N374 (= N370), A377 (= A373)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L17), A10 (= A19), G11 (= G20), Q73 (= Q84), Q76 (≠ P87), G78 (= G89), T79 (= T90), Y100 (= Y112), D102 (= D114), Y136 (= Y149), G137 (= G150), E151 (= E165), N166 (= N180), T196 (= T210)
2oi5A E. Coli glmu- complex with udp-glcnac and acetyl-coa (see paper)
40% identity, 93% coverage: 13:442/462 of query aligns to 4:446/449 of 2oi5A
- active site: R15 (= R24)
- binding acetyl coenzyme *a: G376 (= G372), F399 (= F395), G401 (= G397), S402 (= S398), A419 (≠ G415), A420 (≠ S416), R437 (= R433)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L17), A10 (= A19), G11 (= G20), Q73 (= Q84), Q76 (≠ P87), G78 (= G89), T79 (= T90), Y100 (= Y112), D102 (= D114), Y136 (= Y149), G137 (= G150), E151 (= E165), N166 (= N180), Y194 (= Y208), T196 (= T210)
Query Sequence
>CCNA_02389 FitnessBrowser__Caulo:CCNA_02389
MTESVSKPVRPRAAVILAAGQGTRMKSPTPKVLHRLAGRTLLDHAIDAAEGLGCERIIVV
VGAHSPQVGESARKRLGPDATVIQDPPLGTGHAVLAAKDALADFHGDVVVTYADCPLTTA
PVIAPLFDLITHVAHVAVLGFEAQNPTGYGRLILAPGHVLLRIVEEKEADLATKQVKHCN
SGVLAADRAVLFDLLANVRNDNAKGEYYLTDVVGLAHERHLSTRTAFAPEASVQGVNAQA
ELAAAEAVWQQNRRKALMVDGVTMPAPDTVHLAWDTQIAGGAVVEQFVVFGPGVSVASGA
VIKAFSHLEGAVVGEGALIGPYARLRPGAEIGPDAHIGNFVEVKKVKVGAGAKANHLSYL
GDGSVGEKANIGAGTIFCNYDGFEKFETHVGKGAFIGSNSALVAPVRVGDGAMTGSGSVI
TKDVEDGALALSRADQTSKAGWATKFRAIKQAQKDKKKDKKA
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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