Comparing CCNA_00452 FitnessBrowser__Caulo:CCNA_00452 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)
3iv8A N-acetylglucosamine-6-phosphate deacetylase from vibrio cholerae complexed with fructose 6-phosphate
42% identity, 97% coverage: 11:376/378 of query aligns to 5:375/379 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)
42% identity, 97% coverage: 11:376/378 of query aligns to 4:374/378 of O32445
2p50A Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
40% identity, 99% coverage: 4:377/378 of query aligns to 3:378/382 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)
40% identity, 99% coverage: 4:377/378 of query aligns to 3:378/382 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)
39% identity, 99% coverage: 4:377/378 of query aligns to 3:378/382 of 2p53A
1yrrA Crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution (see paper)
39% identity, 99% coverage: 4:377/378 of query aligns to 3:377/381 of 1yrrA
2p50B Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
37% identity, 99% coverage: 4:377/378 of query aligns to 3:352/356 of 2p50B
6jkuA Crystal structure of n-acetylglucosamine-6-phosphate deacetylase from pasteurella multocida (see paper)
36% identity, 99% coverage: 4:376/378 of query aligns to 10:381/385 of 6jkuA
1yrrB Crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution (see paper)
36% identity, 99% coverage: 4:377/378 of query aligns to 2:330/334 of 1yrrB
7nutA Crystal structure of human amdhd2 in complex with zn and glcn6p (see paper)
35% identity, 98% coverage: 5:376/378 of query aligns to 16:394/401 of 7nutA
2vhlB The three-dimensional structure of the n-acetylglucosamine-6- phosphate deacetylase from bacillus subtilis (see paper)
32% identity, 97% coverage: 10:376/378 of query aligns to 11:384/393 of 2vhlB
O34450 N-acetylglucosamine-6-phosphate deacetylase; GlcNAc 6-P deacetylase; EC 3.5.1.25 from Bacillus subtilis (strain 168) (see paper)
32% identity, 97% coverage: 10:376/378 of query aligns to 12:385/396 of O34450
1o12A Crystal structure of n-acetylglucosamine-6-phosphate deacetylase (tm0814) from thermotoga maritima at 2.5 a resolution
30% identity, 91% coverage: 33:376/378 of query aligns to 22:358/363 of 1o12A
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)
36% identity, 79% coverage: 36:334/378 of query aligns to 35:333/381 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)
36% identity, 79% coverage: 36:334/378 of query aligns to 35:333/385 of 6fv4B
6fv3D Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase from mycobacterium smegmatis. (see paper)
36% identity, 65% coverage: 36:279/378 of query aligns to 33:275/350 of 6fv3D
>CCNA_00452 FitnessBrowser__Caulo:CCNA_00452
MPAALINGRVLTESGVVEGKAVLVKDGLILDVIEAAQTPSDAKPRDLKGGLLVPGFIDTQ
VNGGGGVLFNDAPTVETIATIGAAHRRFGTTGFLPTLISDDLRVVDQAMRATEEAIARGV
PGVLGLHIEGPFLNPKRKGIHDAGKFRVIDDEALALLTSLKRGKTLVTLAPERTTPQIIR
RLADAGVIVAAGHTNALYATMRQALEHGLTGFTHLFNAMSPLTSREPGAVGAALESPDAW
CGIIVDGRHVDPVVLKIALRTRALDRFMLVTDAMPTVGLPDKRFNLQGRDIRVVDGVCVD
DHGTLAGSDLDMIGAVRNAIDLLDLSLDDAVMMASHAPASFLGLGHGRGLIAPGYAADLC
LLNDRLEVAATWIDGQEG
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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