SitesBLAST
Comparing WP_020565030.1 NCBI__GCF_000372865.1:WP_020565030.1 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)
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)
53% identity, 99% coverage: 3:455/456 of query aligns to 6:456/456 of P43889
- LAAG 11:14 (= LAAG 8:11) binding UDP-N-acetyl-alpha-D-glucosamine
- K25 (= K22) mutation to A: No pyrophosphorylase activity.
- Q76 (= Q73) binding UDP-N-acetyl-alpha-D-glucosamine; mutation to A: No pyrophosphorylase activity.
- GT 81:82 (= GT 78:79) binding UDP-N-acetyl-alpha-D-glucosamine
- Y103 (= Y100) mutation to A: Reduces the pyrophosphorylase activity.
- YGD 103:105 (= YGD 100:102) binding UDP-N-acetyl-alpha-D-glucosamine
- D105 (= D102) mutation to A: No pyrophosphorylase activity.
- G140 (= G137) binding UDP-N-acetyl-alpha-D-glucosamine
- E154 (= E152) binding UDP-N-acetyl-alpha-D-glucosamine
- N169 (= N167) binding UDP-N-acetyl-alpha-D-glucosamine
- V223 (= V221) mutation to A: Reduces slightly the pyrophosphorylase activity.
- E224 (≠ L222) mutation to A: Reduces the pyrophosphorylase activity.
Q8Z9S7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Yersinia pestis
53% identity, 99% coverage: 3:455/456 of query aligns to 6:456/456 of Q8Z9S7
- R333 (= R332) binding UDP-N-acetyl-alpha-D-glucosamine
- K351 (= K350) binding UDP-N-acetyl-alpha-D-glucosamine
- Y366 (= Y365) binding UDP-N-acetyl-alpha-D-glucosamine
- N377 (= N376) binding UDP-N-acetyl-alpha-D-glucosamine
4kqlA Hin glmu bound to wg578 (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 4kqlA
- active site: R15 (= R15)
- binding N-(4-{[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-methoxybenzoyl]amino}phenyl)pyridine-2-carboxamide: A9 (= A9), A10 (= A10), Q73 (= Q73), Q76 (= Q76), G78 (= G78), T79 (= T79), Y100 (= Y100), D102 (= D102), Y136 (= Y136), T167 (= T168), V220 (= V221), G222 (= G223)
4kpzA Hin glmu bound to a small molecule fragment (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 4kpzA
- active site: R15 (= R15)
- binding 1-(3-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione: L8 (= L8), A9 (= A9), A10 (= A10), G11 (= G11), V23 (= V23), Q73 (= Q73), Q76 (= Q76), G78 (= G78), D102 (= D102)
4kpxA Hin glmu bound to wg766 (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 4kpxA
4knxA Hin glmu bound to wg176 (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 4knxA
- active site: R15 (= R15)
- binding [(4-{[4-(benzoylamino)phenyl]amino}-6-methoxyquinazolin-7-yl)oxy]acetic acid: L8 (= L8), A10 (= A10), G11 (= G11), Q73 (= Q73), Q76 (= Q76), T79 (= T79), Y100 (= Y100), D102 (= D102), Y136 (= Y136), T167 (= T168), V220 (= V221), G222 (= G223)
4knrA Hin glmu bound to wg188 (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 4knrA
4e1kA Glmu in complex with a quinazoline compound (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 4e1kA
2w0wA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 2
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 2w0wA
- active site: R15 (= R15)
- 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 (= L8), G11 (= G11), Q73 (= Q73), T79 (= T79), Y100 (= Y100), D102 (= D102), Y136 (= Y136), N166 (= N167), T167 (= T168), G168 (= G169), V220 (= V221), G222 (= G223), P449 (= P451)
Sites not aligning to the query:
2w0vA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 1
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 2w0vA
- active site: R15 (= R15)
- 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 (= L8), G11 (= G11), Y100 (= Y100), D102 (= D102), V128 (= V128), T167 (= T168), V220 (= V221), G222 (= G223)
Sites not aligning to the query:
2vd4A Structure of small-molecule inhibitor of glmu from haemophilus influenzae reveals an allosteric binding site (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 2vd4A
2v0lA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 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)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 2v0kA
2v0iA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/450 of 2v0iA
- active site: R15 (= R15)
- binding uridine-diphosphate-n-acetylglucosamine: A10 (= A10), Q73 (= Q73), Q76 (= Q76), G78 (= G78), T79 (= T79), D102 (= D102), Y136 (= Y136), G137 (= G137), E151 (= E152), N166 (= N167), T167 (= T168), Y194 (= Y195), T196 (= T197)
Sites not aligning to the query:
2v0jA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
53% identity, 98% coverage: 3:451/456 of query aligns to 3:449/449 of 2v0jA
4fceA Crystal structure of yersinia pestis glmu in complex with alpha-d- glucosamine 1-phosphate (gp1)
53% identity, 98% coverage: 2:448/456 of query aligns to 2:441/441 of 4fceA
P0ACC7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Escherichia coli (strain K12) (see 6 papers)
51% identity, 99% coverage: 3:455/456 of query aligns to 6:456/456 of P0ACC7
- LAAG 11:14 (= LAAG 8:11) binding UDP-N-acetyl-alpha-D-glucosamine
- G14 (= G11) mutation to A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP.
- R18 (= R15) mutation to A: Dramatically impairs the uridyltransferase activity.
- K25 (= K22) mutation to A: 8-fold decrease in uridyltransferase activity.
- Q76 (= Q73) binding UDP-N-acetyl-alpha-D-glucosamine
- GT 81:82 (= GT 78:79) binding UDP-N-acetyl-alpha-D-glucosamine
- YGD 103:105 (= YGD 100:102) binding UDP-N-acetyl-alpha-D-glucosamine
- D105 (= D102) binding Co(2+); binding Mg(2+)
- G140 (= G137) binding UDP-N-acetyl-alpha-D-glucosamine
- E154 (= E152) binding UDP-N-acetyl-alpha-D-glucosamine
- N169 (= N167) binding UDP-N-acetyl-alpha-D-glucosamine
- N227 (= N225) binding Co(2+); binding Mg(2+)
- 230:250 (vs. 228:248, 52% identical) Linker
- 251:456 (vs. 249:455, 55% identical) N-acetyltransferase
- C296 (= C295) mutation to A: No effect.
- C307 (≠ A306) mutation to A: 1350-fold decrease in acetyltransferase activity.
- C324 (≠ S323) mutation to A: 8-fold decrease in acetyltransferase activity.
- R333 (= R332) binding UDP-N-acetyl-alpha-D-glucosamine
- K351 (= K350) binding UDP-N-acetyl-alpha-D-glucosamine
- Y366 (= Y365) binding UDP-N-acetyl-alpha-D-glucosamine
- N377 (= N376) binding UDP-N-acetyl-alpha-D-glucosamine
- A380 (= A379) binding acetyl-CoA
- C385 (= C384) mutation to A: No effect.
- S405 (= S404) binding acetyl-CoA
- A423 (= A422) binding acetyl-CoA
- R440 (= R439) binding acetyl-CoA
Sites not aligning to the query:
2oi6B E. Coli glmu- complex with udp-glcnac, coa and glcn-1-po4 (see paper)
51% identity, 99% coverage: 3:453/456 of query aligns to 4:452/452 of 2oi6B
- active site: R16 (= R15)
- binding coenzyme a: G402 (= G403), S403 (= S404), A420 (≠ G421), A421 (= A422), R438 (= R439)
- binding 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: H361 (= H362), N375 (= N376)
- binding magnesium ion: D103 (= D102), N225 (= N225)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L8), A10 (= A9), A11 (= A10), G12 (= G11), Q74 (= Q73), Q77 (= Q76), G79 (= G78), T80 (= T79), Y101 (= Y100), D103 (= D102), Y137 (= Y136), G138 (= G137), E152 (= E152), N167 (= N167), T168 (= T168), T197 (= T197), N225 (= N225)
2oi7A E. Coli glmu- complex with udp-glcnac, desulpho-coa and glcnac-1-po4 (see paper)
51% identity, 98% coverage: 3:451/456 of query aligns to 3:449/449 of 2oi7A
- active site: R15 (= R15)
- binding desulfo-coenzyme a: G401 (= G403), S402 (= S404), A419 (≠ G421), A420 (= A422), R437 (= R439)
- binding 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: K357 (= K359), H360 (= H362), N374 (= N376), A377 (= A379)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L8), A10 (= A10), G11 (= G11), Q73 (= Q73), Q76 (= Q76), G78 (= G78), T79 (= T79), Y100 (= Y100), D102 (= D102), Y136 (= Y136), G137 (= G137), E151 (= E152), N166 (= N167), T196 (= T197)
2oi5A E. Coli glmu- complex with udp-glcnac and acetyl-coa (see paper)
51% identity, 98% coverage: 3:451/456 of query aligns to 3:449/449 of 2oi5A
- active site: R15 (= R15)
- binding acetyl coenzyme *a: G376 (= G378), F399 (= F401), G401 (= G403), S402 (= S404), A419 (≠ G421), A420 (= A422), R437 (= R439)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L8), A10 (= A10), G11 (= G11), Q73 (= Q73), Q76 (= Q76), G78 (= G78), T79 (= T79), Y100 (= Y100), D102 (= D102), Y136 (= Y136), G137 (= G137), E151 (= E152), N166 (= N167), Y194 (= Y195), T196 (= T197)
Query Sequence
>WP_020565030.1 NCBI__GCF_000372865.1:WP_020565030.1
MKITTIILAAGKGTRMRSELPKVLHKIAGKPLLKHVYDMCSELQNNRIKIIYGHGAEQVL
EVLKDLDADWIEQKQQLGTGHAVQQVKDQINPADIVLILYGDVPLLKLGTVKHLIAEVSD
KSLALLTVNLENPRGYGRIVRNDHGAVTRIVEEKDASESEVLIREVNTGIMAVQGGHLIK
WLDRLNNHNAQGEYYLTDIIEMAVADHVHIATSQPKTIDEVLGVNNRSQLGHLERVHQLE
QAQQLMERGVTLYDPVRFDLRGTIEHLGLDIEIDVNVILEGQISIGNNVRIGANCRIVDS
VIEDNAEILDHSLIEKAVVGQGSRIGPFARLRPETVIARNVHIGNFVEIKKSSVADGSKI
NHLSYIGDCTVGSRVNVGAGTITCNYDGVNKFHTVIGDGAFIGSDTQLIAPVTIGQNATI
GAGSTITKDSPENQLTLSRAKQVSINGWQRPSKREK
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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