SitesBLAST
Comparing Ga0059261_3663 Ga0059261_3663 UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase 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)
Q8Z9S7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Yersinia pestis
42% identity, 97% coverage: 1:438/451 of query aligns to 1:451/456 of Q8Z9S7
- R333 (= R320) binding
- K351 (= K338) binding
- Y366 (= Y353) binding
- N377 (= N364) binding
P0ACC7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Escherichia coli (strain K12) (see 6 papers)
42% identity, 97% coverage: 1:438/451 of query aligns to 1:451/456 of P0ACC7
- 1:229 (vs. 1:233, 41% identical) Pyrophosphorylase
- LAAG 11:14 (= LAAG 11:14) binding
- G14 (= G14) mutation to A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP.
- R18 (= R18) mutation to A: Dramatically impairs the uridyltransferase activity.
- K25 (= K25) mutation to A: 8-fold decrease in uridyltransferase activity.
- Q76 (= Q76) binding
- GT 81:82 (= GT 81:82) binding
- YGD 103:105 (= YGD 104:106) binding
- D105 (= D106) binding ; binding
- G140 (= G144) binding
- E154 (= E159) binding
- N169 (= N174) binding
- N227 (= N231) binding ; binding
- 230:250 (vs. 234:254, 14% identical) Linker
- C296 (vs. gap) mutation to A: No effect.
- C307 (≠ V294) mutation to A: 1350-fold decrease in acetyltransferase activity.
- C324 (≠ A311) mutation to A: 8-fold decrease in acetyltransferase activity.
- R333 (= R320) binding
- K351 (= K338) binding
- Y366 (= Y353) binding
- N377 (= N364) binding
- A380 (= A367) binding
- C385 (= C372) mutation to A: No effect.
- S405 (= S392) binding
- A423 (= A410) binding
- R440 (= R427) binding
Sites not aligning to the query:
- 251:456 N-acetyltransferase
2oi6B E. Coli glmu- complex with udp-glcnac, coa and glcn-1-po4 (see paper)
42% identity, 97% coverage: 3:438/451 of query aligns to 1:449/452 of 2oi6B
- active site: R16 (= R18)
- binding coenzyme a: G402 (= G391), S403 (= S392), A420 (= A409), A421 (= A410), R438 (= R427)
- binding 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: H361 (= H350), N375 (= N364)
- binding magnesium ion: D103 (= D106), N225 (= N231)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L11), A10 (= A12), A11 (= A13), G12 (= G14), Q74 (= Q76), Q77 (= Q79), G79 (= G81), T80 (= T82), Y101 (= Y104), D103 (= D106), Y137 (= Y143), G138 (= G144), E152 (= E159), N167 (= N174), T168 (≠ S175), T197 (= T204), N225 (= N231)
1hv9B Structure of e. Coli glmu: analysis of pyrophosphorylase and acetyltransferase active sites (see paper)
42% identity, 97% coverage: 3:438/451 of query aligns to 1:449/450 of 1hv9B
- active site: R16 (= R18)
- binding cobalt (ii) ion: D103 (= D106), N225 (= N231)
- binding coenzyme a: G402 (= G391), S403 (= S392), A420 (= A409), A421 (= A410), R438 (= R427)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L11), A10 (= A12), A11 (= A13), G12 (= G14), Q74 (= Q76), Q77 (= Q79), G79 (= G81), T80 (= T82), Y101 (= Y104), D103 (= D106), Y137 (= Y143), G138 (= G144), E152 (= E159), N167 (= N174), T197 (= T204), N225 (= N231)
2oi7A E. Coli glmu- complex with udp-glcnac, desulpho-coa and glcnac-1-po4 (see paper)
42% identity, 96% coverage: 4:438/451 of query aligns to 1:448/449 of 2oi7A
- active site: R15 (= R18)
- binding desulfo-coenzyme a: G401 (= G391), S402 (= S392), A419 (= A409), A420 (= A410), R437 (= R427)
- binding 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: K357 (= K347), H360 (= H350), N374 (= N364), A377 (= A367)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L11), A10 (= A13), G11 (= G14), Q73 (= Q76), Q76 (= Q79), G78 (= G81), T79 (= T82), Y100 (= Y104), D102 (= D106), Y136 (= Y143), G137 (= G144), E151 (= E159), N166 (= N174), T196 (= T204)
2oi5A E. Coli glmu- complex with udp-glcnac and acetyl-coa (see paper)
42% identity, 96% coverage: 4:438/451 of query aligns to 1:448/449 of 2oi5A
- active site: R15 (= R18)
- binding acetyl coenzyme *a: G376 (= G366), F399 (= F389), G401 (= G391), S402 (= S392), A419 (= A409), A420 (= A410), R437 (= R427)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L11), A10 (= A13), G11 (= G14), Q73 (= Q76), Q76 (= Q79), G78 (= G81), T79 (= T82), Y100 (= Y104), D102 (= D106), Y136 (= Y143), G137 (= G144), E151 (= E159), N166 (= N174), Y194 (= Y202), T196 (= T204)
4fceA Crystal structure of yersinia pestis glmu in complex with alpha-d- glucosamine 1-phosphate (gp1)
42% identity, 96% coverage: 4:436/451 of query aligns to 1:441/441 of 4fceA
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)
40% identity, 98% coverage: 1:441/451 of query aligns to 1:454/456 of P43889
- LAAG 11:14 (= LAAG 11:14) binding
- K25 (= K25) mutation to A: No pyrophosphorylase activity.
- Q76 (= Q76) binding ; mutation to A: No pyrophosphorylase activity.
- GT 81:82 (= GT 81:82) binding
- Y103 (= Y104) mutation to A: Reduces the pyrophosphorylase activity.
- YGD 103:105 (= YGD 104:106) binding
- D105 (= D106) mutation to A: No pyrophosphorylase activity.
- G140 (= G144) binding
- E154 (= E159) binding
- N169 (= N174) binding
- V223 (= V227) mutation to A: Reduces slightly the pyrophosphorylase activity.
- E224 (≠ A228) mutation to A: Reduces the pyrophosphorylase activity.
4kqlA Hin glmu bound to wg578 (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 4kqlA
- active site: R15 (= R18)
- binding N-(4-{[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-methoxybenzoyl]amino}phenyl)pyridine-2-carboxamide: A9 (= A12), A10 (= A13), Q73 (= Q76), Q76 (= Q79), G78 (= G81), T79 (= T82), Y100 (= Y104), D102 (= D106), Y136 (= Y143), T167 (≠ S175), V220 (= V227), G222 (= G229)
4kpzA Hin glmu bound to a small molecule fragment (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 4kpzA
- active site: R15 (= R18)
- binding 1-(3-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione: L8 (= L11), A9 (= A12), A10 (= A13), G11 (= G14), V23 (= V26), Q73 (= Q76), Q76 (= Q79), G78 (= G81), D102 (= D106)
4kpxA Hin glmu bound to wg766 (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 4kpxA
4knxA Hin glmu bound to wg176 (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 4knxA
- active site: R15 (= R18)
- binding [(4-{[4-(benzoylamino)phenyl]amino}-6-methoxyquinazolin-7-yl)oxy]acetic acid: L8 (= L11), A10 (= A13), G11 (= G14), Q73 (= Q76), Q76 (= Q79), T79 (= T82), Y100 (= Y104), D102 (= D106), Y136 (= Y143), T167 (≠ S175), V220 (= V227), G222 (= G229)
4knrA Hin glmu bound to wg188 (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 4knrA
4e1kA Glmu in complex with a quinazoline compound (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 4e1kA
2w0wA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 2
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 2w0wA
- active site: R15 (= R18)
- 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 (= L11), G11 (= G14), Q73 (= Q76), T79 (= T82), Y100 (= Y104), D102 (= D106), Y136 (= Y143), N166 (= N174), T167 (≠ S175), G168 (= G176), V220 (= V227), G222 (= G229)
Sites not aligning to the query:
2w0vA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 1
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 2w0vA
- active site: R15 (= R18)
- 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 (= L11), G11 (= G14), Y100 (= Y104), D102 (= D106), V128 (≠ F135), T167 (≠ S175), V220 (= V227), G222 (= G229)
Sites not aligning to the query:
2vd4A Structure of small-molecule inhibitor of glmu from haemophilus influenzae reveals an allosteric binding site (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 2vd4A
2v0lA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 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)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 2v0kA
2v0iA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
40% identity, 96% coverage: 6:438/451 of query aligns to 3:448/450 of 2v0iA
- active site: R15 (= R18)
- binding uridine-diphosphate-n-acetylglucosamine: A10 (= A13), Q73 (= Q76), Q76 (= Q79), G78 (= G81), T79 (= T82), D102 (= D106), Y136 (= Y143), G137 (= G144), E151 (= E159), N166 (= N174), T167 (≠ S175), Y194 (= Y202), T196 (= T204)
Sites not aligning to the query:
Query Sequence
>Ga0059261_3663 Ga0059261_3663 UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase
MTTSPIAAVILAAGSGTRMKSDLHKVLHPIAGRPMLLHLIDTVASLSPERAVVVVGARRE
QVEAAVAPHGVASAHQAEQLGTGHAVMQAREALAGFDGDVLVLYGDVPLVTEETMRRMVG
RLHESDAPSVVVLGFRPADAAAYGRVIVDGGGRIEKIVEYKDASPEERAVTLCNSGLMAV
RSADLFALLDRLGNDNAASEYYLTDIVELANAHVRGAAVIETDAAEVAGVNSRSDLAAVE
AAWQQVRRARAMAEGVTLTAPETVWFAYDTVLGRDVTVEPNVVFGPGVTVADDVNIRAFS
HIEGASIATGAEIGPYARLRPGTVVGEKAKIGNFVETKKTVLGKGAKANHLTYLGDAEVG
AGANIGAGTITCNYDGFFKYGTRIGAGAFIGSNSALVAPVAIGEGAIVAAGAVVTKDVEA
DALALVRPEQVAKPGWAKRFRAMMQARKATK
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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