SitesBLAST
Comparing SMc00232 FitnessBrowser__Smeli:SMc00232 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)
40% identity, 95% coverage: 7:440/456 of query aligns to 8:456/456 of P43889
- LAAG 11:14 (= LAAG 10:13) binding
- K25 (= K24) mutation to A: No pyrophosphorylase activity.
- Q76 (= Q77) binding ; mutation to A: No pyrophosphorylase activity.
- GT 81:82 (= GT 82:83) binding
- Y103 (≠ F105) mutation to A: Reduces the pyrophosphorylase activity.
- YGD 103:105 (≠ FGD 105:107) binding
- D105 (= D107) mutation to A: No pyrophosphorylase activity.
- G140 (= G143) binding
- E154 (= E157) binding
- N169 (= N172) binding
- V223 (≠ L225) mutation to A: Reduces slightly the pyrophosphorylase activity.
- E224 (≠ T226) mutation to A: Reduces the pyrophosphorylase activity.
4kqlA Hin glmu bound to wg578 (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 4kqlA
- active site: R15 (= R17)
- binding N-(4-{[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-methoxybenzoyl]amino}phenyl)pyridine-2-carboxamide: A9 (= A11), A10 (= A12), Q73 (= Q77), Q76 (≠ R80), G78 (= G82), T79 (= T83), Y100 (≠ F105), D102 (= D107), Y136 (= Y142), T167 (≠ G173), V220 (≠ L225), G222 (= G227)
4kpzA Hin glmu bound to a small molecule fragment (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 4kpzA
- active site: R15 (= R17)
- binding 1-(3-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione: L8 (= L10), A9 (= A11), A10 (= A12), G11 (= G13), V23 (= V25), Q73 (= Q77), Q76 (≠ R80), G78 (= G82), D102 (= D107)
4kpxA Hin glmu bound to wg766 (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 4kpxA
4knxA Hin glmu bound to wg176 (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 4knxA
- active site: R15 (= R17)
- binding [(4-{[4-(benzoylamino)phenyl]amino}-6-methoxyquinazolin-7-yl)oxy]acetic acid: L8 (= L10), A10 (= A12), G11 (= G13), Q73 (= Q77), Q76 (≠ R80), T79 (= T83), Y100 (≠ F105), D102 (= D107), Y136 (= Y142), T167 (≠ G173), V220 (≠ L225), G222 (= G227)
4knrA Hin glmu bound to wg188 (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 4knrA
4e1kA Glmu in complex with a quinazoline compound (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 4e1kA
2w0wA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 2
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 2w0wA
- active site: R15 (= R17)
- 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 (= L10), G11 (= G13), Q73 (= Q77), T79 (= T83), Y100 (≠ F105), D102 (= D107), Y136 (= Y142), N166 (= N172), T167 (≠ G173), G168 (= G174), V220 (≠ L225), G222 (= G227), P449 (= P436), I450 (= I437)
2w0vA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 1
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 2w0vA
- active site: R15 (= R17)
- 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 (= L10), G11 (= G13), Y100 (≠ F105), D102 (= D107), V128 (≠ F134), T167 (≠ G173), V220 (≠ L225), G222 (= G227), I450 (= I437)
2vd4A Structure of small-molecule inhibitor of glmu from haemophilus influenzae reveals an allosteric binding site (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 2vd4A
2v0lA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 2v0lA
2v0kA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1- phosphate uridyltransferase (glmu) (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 2v0kA
2v0iA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
40% identity, 95% coverage: 7:437/456 of query aligns to 5:450/450 of 2v0iA
- active site: R15 (= R17)
- binding uridine-diphosphate-n-acetylglucosamine: A10 (= A12), Q73 (= Q77), Q76 (≠ R80), G78 (= G82), T79 (= T83), D102 (= D107), Y136 (= Y142), G137 (= G143), E151 (= E157), N166 (= N172), T167 (≠ G173), Y194 (= Y200), T196 (= T202), I450 (= I437)
2v0jA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 93% coverage: 7:428/456 of query aligns to 5:440/449 of 2v0jA
P0ACC7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Escherichia coli (strain K12) (see 6 papers)
40% identity, 95% coverage: 8:440/456 of query aligns to 9:456/456 of P0ACC7
- LAAG 11:14 (= LAAG 10:13) binding
- G14 (= G13) mutation to A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP.
- R18 (= R17) mutation to A: Dramatically impairs the uridyltransferase activity.
- K25 (= K24) mutation to A: 8-fold decrease in uridyltransferase activity.
- Q76 (= Q77) binding
- GT 81:82 (= GT 82:83) binding
- YGD 103:105 (≠ FGD 105:107) binding
- D105 (= D107) binding ; binding
- G140 (= G143) binding
- E154 (= E157) binding
- N169 (= N172) binding
- N227 (= N229) binding ; binding
- 230:250 (vs. 232:252, 33% identical) Linker
- 251:456 (vs. 253:440, 43% identical) N-acetyltransferase
- C296 (≠ A292) mutation to A: No effect.
- C307 (vs. gap) mutation to A: 1350-fold decrease in acetyltransferase activity.
- C324 (≠ A309) mutation to A: 8-fold decrease in acetyltransferase activity.
- R333 (= R318) binding
- K351 (= K336) binding
- Y366 (= Y351) binding
- N377 (= N362) binding
- A380 (= A365) binding
- C385 (= C370) mutation to A: No effect.
- S405 (= S390) binding
- A423 (≠ S408) binding
- R440 (= R425) binding
Sites not aligning to the query:
2oi6B E. Coli glmu- complex with udp-glcnac, coa and glcn-1-po4 (see paper)
41% identity, 94% coverage: 8:437/456 of query aligns to 7:451/452 of 2oi6B
- active site: R16 (= R17)
- binding coenzyme a: G402 (= G389), S403 (= S390), A420 (= A407), A421 (≠ S408), R438 (= R425)
- binding 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: H361 (= H348), N375 (= N362)
- binding magnesium ion: D103 (= D107), N225 (= N229)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L10), A10 (= A11), A11 (= A12), G12 (= G13), Q74 (= Q77), Q77 (≠ R80), G79 (= G82), T80 (= T83), Y101 (≠ F105), D103 (= D107), Y137 (= Y142), G138 (= G143), E152 (= E157), N167 (= N172), T168 (≠ G173), T197 (= T202), N225 (= N229)
Q8Z9S7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Yersinia pestis
40% identity, 92% coverage: 8:428/456 of query aligns to 9:443/456 of Q8Z9S7
- R333 (= R318) binding
- K351 (= K336) binding
- Y366 (= Y351) binding
- N377 (= N362) binding
1hv9B Structure of e. Coli glmu: analysis of pyrophosphorylase and acetyltransferase active sites (see paper)
41% identity, 94% coverage: 8:436/456 of query aligns to 7:450/450 of 1hv9B
- active site: R16 (= R17)
- binding cobalt (ii) ion: D103 (= D107), N225 (= N229)
- binding coenzyme a: G402 (= G389), S403 (= S390), A420 (= A407), A421 (≠ S408), R438 (= R425)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L10), A10 (= A11), A11 (= A12), G12 (= G13), Q74 (= Q77), Q77 (≠ R80), G79 (= G82), T80 (= T83), Y101 (≠ F105), D103 (= D107), Y137 (= Y142), G138 (= G143), E152 (= E157), N167 (= N172), T197 (= T202), N225 (= N229)
2oi7A E. Coli glmu- complex with udp-glcnac, desulpho-coa and glcnac-1-po4 (see paper)
41% identity, 94% coverage: 8:436/456 of query aligns to 6:449/449 of 2oi7A
- active site: R15 (= R17)
- binding desulfo-coenzyme a: G401 (= G389), S402 (= S390), A419 (= A407), A420 (≠ S408), R437 (= R425)
- binding 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: K357 (= K345), H360 (= H348), N374 (= N362), A377 (= A365)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L10), A10 (= A12), G11 (= G13), Q73 (= Q77), Q76 (≠ R80), G78 (= G82), T79 (= T83), Y100 (≠ F105), D102 (= D107), Y136 (= Y142), G137 (= G143), E151 (= E157), N166 (= N172), T196 (= T202)
2oi5A E. Coli glmu- complex with udp-glcnac and acetyl-coa (see paper)
41% identity, 94% coverage: 8:436/456 of query aligns to 6:449/449 of 2oi5A
- active site: R15 (= R17)
- binding acetyl coenzyme *a: G376 (= G364), F399 (= F387), G401 (= G389), S402 (= S390), A419 (= A407), A420 (≠ S408), R437 (= R425)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L10), A10 (= A12), G11 (= G13), Q73 (= Q77), Q76 (≠ R80), G78 (= G82), T79 (= T83), Y100 (≠ F105), D102 (= D107), Y136 (= Y142), G137 (= G143), E151 (= E157), N166 (= N172), Y194 (= Y200), T196 (= T202)
Query Sequence
>SMc00232 FitnessBrowser__Smeli:SMc00232
MERTCLAIILAAGESTRMKSAMSKVLHPVAGRPMIAHVVDALASASISDVALVVGRDADA
VSAAAATDEVAVTSFLQKERLGTAHAVLAAREAIAKGYDDVLVVFGDTPLITAAPLKAAR
DGLAAGNDVVVIGFQATDPTGYGRLIVKDGALVAIREHRDASDEERRITYCNGGLMAIDG
RKALDLLNRIGNANAKGEYYLTDLVEIARSLDGRAIAVEAPEEELTGCNTRAELAYIERL
WQQRRRHELMLAGVSMIAPETVFLSWDTALAQDVLLEPNVVFGPGVRVESGAVIHAFSHL
EGAHVRAGATVGPFARLRPGADLGAKSKVGNFCEVKNAEIGAGAKVNHLTYIGDAFVGAG
SNIGAGTITCNYDGVNKHVTRIGANAFVGSNSSLVAPVSIGDGALVASGSVITEDVPADA
VAFGRARQDVKPGRAPILRERYEAEKAARKRAKAAE
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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