Comparing WP_054188081.1 NCBI__GCF_002893965.1:WP_054188081.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
2bkxA Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the nagb superfamily (see paper)
46% identity, 80% coverage: 31:238/259 of query aligns to 32:239/242 of 2bkxA
2bkvB Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the nagb superfamily (see paper)
46% identity, 80% coverage: 31:238/259 of query aligns to 32:239/242 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)
46% identity, 80% coverage: 31:238/259 of query aligns to 32:239/242 of O35000
5hj5B Crystal structure of tertiary complex of glucosamine-6-phosphate deaminase from vibrio cholerae with beta-d-glucose-6-phosphate and fructose-6-phosphate
42% identity, 82% coverage: 31:242/259 of query aligns to 37:249/267 of 5hj5B
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.
39% identity, 93% coverage: 1:242/259 of query aligns to 1:249/266 of 2wu1A
1horA Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from escherichia coli at 2.1 angstroms resolution (see paper)
39% identity, 93% coverage: 1:242/259 of query aligns to 1:249/266 of 1horA
1fqoA Glucosamine 6-phosphate deaminase complexed with the substrate of the reverse reaction fructose 6-phosphate (open form) (see paper)
39% identity, 93% coverage: 1:242/259 of query aligns to 1:249/266 of 1fqoA
1deaA Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from escherichia coli at 2.1 angstroms resolution (see paper)
39% identity, 93% coverage: 1:242/259 of query aligns to 1:249/266 of 1deaA
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)
39% identity, 93% coverage: 1:242/259 of query aligns to 1:249/266 of P0A759
2ri1A Crystal structure of glucosamine 6-phosphate deaminase (nagb) with glcn6p from s. Mutans (see paper)
40% identity, 92% coverage: 1:238/259 of query aligns to 3:233/235 of 2ri1A
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)
41% identity, 87% coverage: 30:255/259 of query aligns to 36:258/281 of 1ne7A
Sites not aligning to the query:
P46926 Glucosamine-6-phosphate deaminase 1; GlcN6P deaminase 1; Glucosamine-6-phosphate isomerase 1; Protein oscillin; EC 3.5.99.6 from Homo sapiens (Human) (see paper)
41% identity, 87% coverage: 30:255/259 of query aligns to 36:258/289 of P46926
Sites not aligning to the query:
3hn6A Crystal structure of glucosamine-6-phosphate deaminase from borrelia burgdorferi
38% identity, 85% coverage: 31:249/259 of query aligns to 40:261/271 of 3hn6A
O95479 GDH/6PGL endoplasmic bifunctional protein; EC 1.1.1.47; EC 1.1.1.363; EC 3.1.1.31 from Homo sapiens (Human) (see 6 papers)
28% identity, 55% coverage: 3:145/259 of query aligns to 555:706/791 of O95479
Sites not aligning to the query:
P56201 GDH/6PGL endoplasmic bifunctional protein; EC 1.1.1.47; EC 1.1.1.363; EC 3.1.1.31 from Oryctolagus cuniculus (Rabbit) (see paper)
26% identity, 74% coverage: 10:201/259 of query aligns to 568:757/797 of P56201
Sites not aligning to the query:
>WP_054188081.1 NCBI__GCF_002893965.1:WP_054188081.1
MEIVIVDSAEAAGTVVADIFEHAVHSGARTLGLATGSSPLSVYRELARRHREEGLSFAGV
QAFLLDEYVGLPEGHPESYAQVIRTELVNHLDLDAARVFSPDGTAPDPFAAAAAYDRAIA
SNGPVDVQLLGIGGNGHIGFNEPTSSLNSRTRVKTLTEQTRTDNARFFESPDDVPRHVIT
QGLGTICEAKHLVMIATGEHKAAAIAAAVEGPLAAVCPASVLQLHPHATVVIDEAAASQL
RLTEFYKTVSAHKPLAQHY
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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