Comparing Echvi_3893 FitnessBrowser__Cola:Echvi_3893 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 hits to proteins with known functional sites (download)
P46926 Glucosamine-6-phosphate isomerase 1; Glucosamine-6-phosphate deaminase 1; GNPDA 1; GlcN6P deaminase 1; Oscillin; EC 3.5.99.6 from Homo sapiens (Human) (see paper)
30% identity, 18% coverage: 196:336/775 of query aligns to 118:256/289 of P46926
Sites not aligning to the query:
1ne7A Human glucosamine-6-phosphate deaminase isomerase at 1.75 a resolution complexed with n-acetyl-glucosamine-6-phosphate and 2-deoxy-2-amino- glucitol-6-phosphate (see paper)
30% identity, 18% coverage: 196:336/775 of query aligns to 118:256/281 of 1ne7A
Sites not aligning to the query:
2wu1A Glucosamine-6-phosphate deaminase complexed with the allosteric activator n-acetyl-glucoamine-6-phosphate both in the active and allosteric sites.
31% identity, 15% coverage: 192:310/775 of query aligns to 114:230/266 of 2wu1A
Sites not aligning to the query:
1horA Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from escherichia coli at 2.1 angstroms resolution (see paper)
31% identity, 15% coverage: 192:310/775 of query aligns to 114:230/266 of 1horA
Sites not aligning to the query:
1fqoA Glucosamine 6-phosphate deaminase complexed with the substrate of the reverse reaction fructose 6-phosphate (open form) (see paper)
31% identity, 15% coverage: 192:310/775 of query aligns to 114:230/266 of 1fqoA
Sites not aligning to the query:
1deaA Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from escherichia coli at 2.1 angstroms resolution (see paper)
31% identity, 15% coverage: 192:310/775 of query aligns to 114:230/266 of 1deaA
Sites not aligning to the query:
P0A759 Glucosamine-6-phosphate deaminase; GlcN6P deaminase; GNPDA; Glucosamine-6-phosphate isomerase; EC 3.5.99.6 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 15% coverage: 192:310/775 of query aligns to 114:230/266 of P0A759
Sites not aligning to the query:
3hn6A Crystal structure of glucosamine-6-phosphate deaminase from borrelia burgdorferi
36% identity, 14% coverage: 207:315/775 of query aligns to 132:238/271 of 3hn6A
Sites not aligning to the query:
5hj5B Crystal structure of tertiary complex of glucosamine-6-phosphate deaminase from vibrio cholerae with beta-d-glucose-6-phosphate and fructose-6-phosphate
30% identity, 16% coverage: 184:310/775 of query aligns to 99:230/267 of 5hj5B
Sites not aligning to the query:
2bkxA Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the nagb superfamily (see paper)
22% identity, 33% coverage: 54:310/775 of query aligns to 28:224/242 of 2bkxA
2bkvB Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the nagb superfamily (see paper)
22% identity, 33% coverage: 54:310/775 of query aligns to 28:224/242 of 2bkvB
O35000 Glucosamine-6-phosphate deaminase 1; GlcN6P deaminase 1; GNPDA 1; Glucosamine-6-phosphate isomerase 1; EC 3.5.99.6 from Bacillus subtilis (strain 168) (see paper)
22% identity, 33% coverage: 54:310/775 of query aligns to 28:224/242 of O35000
>Echvi_3893 FitnessBrowser__Cola:Echvi_3893
MLSNYPLSEVEECFLKESGVKEITTKIPYLTVDNFPKLGLLTACRFLEWAAHNPNGVISL
PTGKTPEFFIKWTQFLLENWDSKKGKQIREDYGMSDLKKPVLKDLHFVQIDEFYPISSSQ
HNSFYHYVNKFYIDGFGLDPKKALLINSDDIPLAEGKHFSEIFPDLKVDLSLRFREAANK
QEKLQQESIFLIDKWCGEYEQKIREKGGIGFFLGGIGPDGHIAFNTRGSDIFSTTRLTET
NFETQAVAAGDLGGIEVSANRLVITIGLDTIVYNPEAVGIIIAAGEAKAQIVKDSLETDL
TNIHPATVLQKLKNGRFYLTKGGASKLTDSINTYYKTGEWTQAKTEKSILELCKKLGKYA
SRLKLEDLKNDPYTSLIPDLSENTVASVIQSTIDKLNRGIEKEENEVLLHTGPHHDDISL
GILPHITNQLSEKTNEAHFSVLTSGFTAVTNTFVIDTLLHTKKLLDEDQIQMVNYEDFFQ
TGYKLKMDKDVYHYLTNVASEDPEQQKRGLCHRVVRAVVEVFGVKNNQKLRETINDVISI
LKNSYDGEKNPPKIQKLKGMIREFEEELVWAHFGVKVRNVHHLRLGFYTGDIFTEQPDKK
RDVEPIVEMFREINPTKISLTLDPEGSGPDTHYKVLQATAEAVRQWSKEKDLSDLRIIGY
RNVWFKFEAAESNVIVPVSLGDLSVMEDSFANCYLSQVNASFPSYAHNGKFSTIAKRTWV
NQLNDVQLLLGKDYFYQHDMAKVRASHGLIFFKDMNVEEFIAHARELEKSIEGMI
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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