Comparing AO356_17550 FitnessBrowser__pseudo5_N2C3_1:AO356_17550 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 16 hits to proteins with known functional sites (download)
1o12A Crystal structure of n-acetylglucosamine-6-phosphate deacetylase (tm0814) from thermotoga maritima at 2.5 a resolution
36% identity, 96% coverage: 10:363/368 of query aligns to 13:360/363 of 1o12A
2vhlB The three-dimensional structure of the n-acetylglucosamine-6- phosphate deacetylase from bacillus subtilis (see paper)
37% identity, 86% coverage: 30:345/368 of query aligns to 37:368/393 of 2vhlB
O34450 N-acetylglucosamine-6-phosphate deacetylase; GlcNAc 6-P deacetylase; EC 3.5.1.25 from Bacillus subtilis (strain 168) (see paper)
37% identity, 86% coverage: 30:345/368 of query aligns to 38:369/396 of O34450
7nutA Crystal structure of human amdhd2 in complex with zn and glcn6p (see paper)
35% identity, 98% coverage: 5:363/368 of query aligns to 20:396/401 of 7nutA
3iv8A N-acetylglucosamine-6-phosphate deacetylase from vibrio cholerae complexed with fructose 6-phosphate
33% identity, 92% coverage: 24:361/368 of query aligns to 32:375/379 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)
33% identity, 92% coverage: 24:361/368 of query aligns to 31:374/378 of O32445
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: 42:366/368 of query aligns to 51:381/381 of 1yrrA
2p50A Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
33% identity, 88% coverage: 42:366/368 of query aligns to 51:382/382 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: 42:366/368 of query aligns to 51:382/382 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: 42:366/368 of query aligns to 51:382/382 of 2p53A
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, 99% coverage: 1:363/368 of query aligns to 6:379/381 of 6fv4A
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, 99% coverage: 1:363/368 of query aligns to 6:379/385 of 6fv4B
6jkuA Crystal structure of n-acetylglucosamine-6-phosphate deacetylase from pasteurella multocida (see paper)
30% identity, 90% coverage: 30:361/368 of query aligns to 49:381/385 of 6jkuA
2p50B Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
32% identity, 88% coverage: 42:366/368 of query aligns to 51:356/356 of 2p50B
6fv3D Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase from mycobacterium smegmatis. (see paper)
34% identity, 72% coverage: 1:266/368 of query aligns to 4:275/350 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: 42:366/368 of query aligns to 50:334/334 of 1yrrB
>AO356_17550 FitnessBrowser__pseudo5_N2C3_1:AO356_17550
MSEDNILTCDGWVRGRLLHEHGRVVAIEGQPCDPASNDLPYLLPGFIDLHVHGGGGKDIM
QGASAFETIARTHLRFGTTALLATTMTAPSEEIASVLQALGEFCEQRPNGSARVLGVHLE
GPYINPGKLGAQPNFAHTALLAEVESYLALAPIRVITIAPEIAGHDALIRALSARGVRMQ
IGHTLGSYEEGVAALAAGASSFTHLYNAMSPLHHREPGIVGAALAHAQYAELIPDLLHVH
PGAMRVALRSIPCLYCVTDSTAAAGMPDGEYKLGSHTVTKCLGGVRLADGTLAGSTLTMD
QALRNLVKIGLPIAEASQRLSQFPADYLGLPERGRLQPGAWADCVRLDRSLTLTDVMVEG
EAIDFQNA
Or try a new SitesBLAST search
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