Comparing AO353_04450 FitnessBrowser__pseudo3_N2E3:AO353_04450 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
O34450 N-acetylglucosamine-6-phosphate deacetylase; GlcNAc 6-P deacetylase; EC 3.5.1.25 from Bacillus subtilis (strain 168) (see paper)
40% identity, 85% coverage: 34:345/368 of query aligns to 50:369/396 of O34450
2vhlB The three-dimensional structure of the n-acetylglucosamine-6- phosphate deacetylase from bacillus subtilis (see paper)
40% identity, 85% coverage: 34:345/368 of query aligns to 49:368/393 of 2vhlB
1o12A Crystal structure of n-acetylglucosamine-6-phosphate deacetylase (tm0814) from thermotoga maritima at 2.5 a resolution
36% identity, 96% coverage: 10:361/368 of query aligns to 13:358/363 of 1o12A
7nutA Crystal structure of human amdhd2 in complex with zn and glcn6p (see paper)
34% identity, 95% coverage: 12:361/368 of query aligns to 27:394/401 of 7nutA
3iv8A N-acetylglucosamine-6-phosphate deacetylase from vibrio cholerae complexed with fructose 6-phosphate
35% identity, 87% coverage: 42:361/368 of query aligns to 52:375/379 of 3iv8A
O32445 N-acetylglucosamine-6-phosphate deacetylase; GlcNAc 6-P deacetylase; EC 3.5.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
35% identity, 87% coverage: 42:361/368 of query aligns to 51:374/378 of O32445
6fv4A The structure of n-acetyl-d-glucosamine-6-phosphate deacetylase d267a mutant from mycobacterium smegmatis in complex with n-acetyl-d- glucosamine-6-phosphate (see paper)
35% identity, 98% coverage: 1:361/368 of query aligns to 6:377/381 of 6fv4A
1yrrA Crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution (see paper)
33% identity, 88% coverage: 42:363/368 of query aligns to 51:378/381 of 1yrrA
6fv4B The structure of n-acetyl-d-glucosamine-6-phosphate deacetylase d267a mutant from mycobacterium smegmatis in complex with n-acetyl-d- glucosamine-6-phosphate (see paper)
35% identity, 98% coverage: 1:361/368 of query aligns to 6:377/385 of 6fv4B
2p50A Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
33% identity, 88% coverage: 42:363/368 of query aligns to 51:379/382 of 2p50A
P0AF18 N-acetylglucosamine-6-phosphate deacetylase; GlcNAc 6-P deacetylase; EC 3.5.1.25 from Escherichia coli (strain K12) (see 2 papers)
33% identity, 88% coverage: 42:363/368 of query aligns to 51:379/382 of P0AF18
2p53A Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase d273n mutant complexed with n-acetyl phosphonamidate-d-glucosamine-6- phosphate (see paper)
33% identity, 88% coverage: 42:363/368 of query aligns to 51:379/382 of 2p53A
6jkuA Crystal structure of n-acetylglucosamine-6-phosphate deacetylase from pasteurella multocida (see paper)
30% identity, 97% coverage: 6:361/368 of query aligns to 16:381/385 of 6jkuA
2p50B Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
32% identity, 88% coverage: 42:363/368 of query aligns to 51:353/356 of 2p50B
6fv3D Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase from mycobacterium smegmatis. (see paper)
32% identity, 98% coverage: 1:361/368 of query aligns to 4:347/350 of 6fv3D
1yrrB Crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution (see paper)
29% identity, 88% coverage: 42:363/368 of query aligns to 50:331/334 of 1yrrB
>AO353_04450 FitnessBrowser__pseudo3_N2E3:AO353_04450
MSEDNILTAQGWIRGRLIHEHGKIVRIEGQPCDPADNDLPYLLPGFIDLHVHGGGGKDIM
EGTPAFDTITKTHVRFGTTSLLATTMTAPPEEISRVLAEVGEFCEQRPKGCARVLGVHLE
GPYINPGKLGAQPNFAHTALMAEVEAYLALAPIRVITIAPEIAGHDKLIRALSDRGIRMQ
IGHTLGSYEEGVAALEAGASSFTHLYNAMSPLHHREPGIVGAALAHAKYAELIPDLLHVH
PGAIRVALRSIPCLYCVTDSTAAAGMPDGEYKLGSHTVTKCLGGVRLPDGTLAGSTLTMD
QALRNLVKIGLPLAEASQRLSQFPADYLGIQERGRLQPGAWADCVRLDRSLTLTAVMVEG
EDIDFKNA
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory