Comparing Synpcc7942_0440 FitnessBrowser__SynE:Synpcc7942_0440 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)
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)
38% identity, 86% coverage: 16:337/375 of query aligns to 38:349/378 of O32445
3iv8A N-acetylglucosamine-6-phosphate deacetylase from vibrio cholerae complexed with fructose 6-phosphate
38% identity, 86% coverage: 16:337/375 of query aligns to 39:350/379 of 3iv8A
7nutA Crystal structure of human amdhd2 in complex with zn and glcn6p (see paper)
37% identity, 90% coverage: 23:361/375 of query aligns to 52:398/401 of 7nutA
2p50A Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
36% identity, 88% coverage: 1:331/375 of query aligns to 28:346/382 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)
36% identity, 88% coverage: 1:331/375 of query aligns to 28:346/382 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)
36% identity, 88% coverage: 1:331/375 of query aligns to 28:346/382 of 2p53A
1yrrA Crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution (see paper)
36% identity, 88% coverage: 1:331/375 of query aligns to 28:345/381 of 1yrrA
O34450 N-acetylglucosamine-6-phosphate deacetylase; GlcNAc 6-P deacetylase; EC 3.5.1.25 from Bacillus subtilis (strain 168) (see paper)
34% identity, 80% coverage: 12:311/375 of query aligns to 37:334/396 of O34450
2vhlB The three-dimensional structure of the n-acetylglucosamine-6- phosphate deacetylase from bacillus subtilis (see paper)
34% identity, 80% coverage: 12:311/375 of query aligns to 36:333/393 of 2vhlB
6jkuA Crystal structure of n-acetylglucosamine-6-phosphate deacetylase from pasteurella multocida (see paper)
34% identity, 84% coverage: 16:331/375 of query aligns to 45:350/385 of 6jkuA
2p50B Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase liganded with zn (see paper)
33% identity, 88% coverage: 1:331/375 of query aligns to 28:320/356 of 2p50B
1o12A Crystal structure of n-acetylglucosamine-6-phosphate deacetylase (tm0814) from thermotoga maritima at 2.5 a resolution
32% identity, 80% coverage: 32:331/375 of query aligns to 44:328/363 of 1o12A
1yrrB Crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution (see paper)
32% identity, 88% coverage: 1:331/375 of query aligns to 27:298/334 of 1yrrB
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)
33% identity, 70% coverage: 32:295/375 of query aligns to 54:308/385 of 6fv4B
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)
33% identity, 70% coverage: 32:295/375 of query aligns to 54:308/381 of 6fv4A
6fv3D Crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase from mycobacterium smegmatis. (see paper)
32% identity, 62% coverage: 32:265/375 of query aligns to 52:275/350 of 6fv3D
>Synpcc7942_0440 FitnessBrowser__SynE:Synpcc7942_0440
VQSIEPMSQTFDRLPPPQLRMIDLQGDWLSLGGIDLQINGALGLAFPEVQASDRNRLLAI
CRRLWEQGVDAFTPTLVTSSIAQFRQAIEAIADFVAQPLPPRHAKILGLHLEGPCLAESK
RGAHPQEHLQPLTVEVLSEICGDHLAQIRIVTLAPELDPTGEAIAWLRQQGVIVSLGHSQ
ATAEQAQVAFQQGATMVTHAFNAMPPLHHRQPGLLGAALTTDTVFAGLIADGQHIDPIML
KLLLRAGEGDRRLFLVSDALAPLGLPDGQYPWDERQITVTAGTCRLEDGTLAGTTLPLLA
GVQNLVRWQVCEPETAIMLATLAPLRALGVDWSDPRLLYLSRPVCQLLRWHQSDTGELTW
QRLCENDELPTPTSI
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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