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.
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)
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: F400 (= F389), G402 (= G391), S403 (= S392), A420 (= A409), A421 (= A410), I436 (≠ L425), R438 (= R427)
- binding 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: K358 (= K347), H361 (= H350), N375 (= N364)
- binding magnesium ion: D103 (= D106), N225 (= N231)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L11), A10 (= A12), A11 (= A13), G12 (= G14), R16 (= R18), K23 (= K25), Q74 (= Q76), Q77 (= Q79), L78 (= L80), G79 (= G81), T80 (= T82), A83 (= A85), Y101 (= Y104), G102 (= G105), D103 (= D106), Y137 (= Y143), G138 (= G144), E152 (= E159), N167 (= N174), T168 (≠ S175), Y195 (= Y202), 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), L434 (= L423), I436 (≠ L425), R438 (= R427)
- binding uridine-diphosphate-n-acetylglucosamine: L9 (= L11), A10 (= A12), A11 (= A13), G12 (= G14), R16 (= R18), K23 (= K25), Q74 (= Q76), Q77 (= Q79), G79 (= G81), T80 (= T82), A83 (= A85), Y101 (= Y104), G102 (= G105), D103 (= D106), Y137 (= Y143), G138 (= G144), E152 (= E159), N167 (= N174), T168 (≠ S175), Y195 (= Y202), 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), I435 (≠ L425), R437 (= R427), P439 (≠ E429)
- binding 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose: K357 (= K347), H360 (= H350), N374 (= N364), I375 (= I365), G376 (= G366), A377 (= A367)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L11), A9 (= A12), A10 (= A13), G11 (= G14), Q73 (= Q76), Q76 (= Q79), L77 (= L80), G78 (= G81), T79 (= T82), A82 (= A85), Y100 (= Y104), D102 (= D106), Y136 (= Y143), G137 (= G144), E151 (= E159), N166 (= N174), T167 (≠ S175), Y194 (= Y202), 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: H360 (= H350), G376 (= G366), A377 (= A367), F399 (= F389), G401 (= G391), S402 (= S392), A419 (= A409), A420 (= A410), I435 (≠ L425), R437 (= R427)
- binding uridine-diphosphate-n-acetylglucosamine: L8 (= L11), A9 (= A12), A10 (= A13), G11 (= G14), Q73 (= Q76), Q76 (= Q79), L77 (= L80), G78 (= G81), T79 (= T82), Y100 (= Y104), D102 (= D106), Y136 (= Y143), G137 (= G144), E151 (= E159), N166 (= N174), T167 (≠ S175), 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