Comparing Ac3H11_1552 FitnessBrowser__acidovorax_3H11:Ac3H11_1552 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 13 hits to proteins with known functional sites (download)
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
25% identity, 90% coverage: 1:523/584 of query aligns to 1:462/554 of P22106
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
25% identity, 85% coverage: 25:523/584 of query aligns to 27:442/497 of 1ct9A
Sites not aligning to the query:
P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 65% coverage: 1:381/584 of query aligns to 1:383/557 of P78753
Sites not aligning to the query:
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
26% identity, 59% coverage: 25:369/584 of query aligns to 23:361/509 of 6gq3A
Sites not aligning to the query:
P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
26% identity, 63% coverage: 1:369/584 of query aligns to 1:374/561 of P08243
Sites not aligning to the query:
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
33% identity, 21% coverage: 39:161/584 of query aligns to 64:193/455 of 1ao0A
Sites not aligning to the query:
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
33% identity, 21% coverage: 39:161/584 of query aligns to 75:208/476 of P00497
Sites not aligning to the query:
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
33% identity, 21% coverage: 39:161/584 of query aligns to 64:197/465 of 1gph1
Sites not aligning to the query:
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
32% identity, 22% coverage: 39:167/584 of query aligns to 65:201/238 of 1xfgA
Sites not aligning to the query:
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
32% identity, 22% coverage: 39:167/584 of query aligns to 65:201/238 of 1xffA
Sites not aligning to the query:
2j6hA E. Coli glucosamine-6-p synthase in complex with glucose-6p and 5-oxo- l-norleucine (see paper)
32% identity, 22% coverage: 39:167/584 of query aligns to 65:201/608 of 2j6hA
Sites not aligning to the query:
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
32% identity, 22% coverage: 39:167/584 of query aligns to 65:201/608 of 4amvA
Sites not aligning to the query:
1jxaA Glucosamine 6-phosphate synthase with glucose 6-phosphate (see paper)
32% identity, 22% coverage: 39:167/584 of query aligns to 65:201/608 of 1jxaA
Sites not aligning to the query:
>Ac3H11_1552 FitnessBrowser__acidovorax_3H11:Ac3H11_1552
MCGIAGVVNAAGVTKDDVWKMIDCIKYRGVDEQGVEDLGGAVLGHARLAVVDPENGMQPM
SSTDGKVWVVFNGEIFNFIELREQLKAKGYKFKSRCDTEVLVHLWCEKGEKMLDDLVGMF
AFFIWDQRTQTGMLARDRQGIKPCFYAPYQGGVAFASEMKAILALPKFERKVNESALGNV
FTFNYCPPPETCFEGIRHLMPGTFIRYGGGSFSEPVRYWEWPLDGERLDAEQADLERALD
EAVKLQMRFDVDGGLFLSGGVDSSVIANRLVPQWNRPRLDAIGLRIEHEGFSEYAYAERV
ATDLNINLSALDIQPSDIPEIARSVVRHAEQPHGDFSFFLFYLLSRKAHEMGKIVMFTGD
GPDEVMLGFRHNEQFFSEMTRANFSMRSYFDLISYSSEKDRKRMMSVSFLPHTEGALDKF
MSIIEPFRDLEPMEQVAAYELTALMPGNNSVKGDRMGACWSIEARAPFLDHRVSELLARL
PITSKFHQGVGKHFLKKAAENYYDRDFVFRPKTMPTLPIGEWIKGPLYQWARDTLALSDG
GRFDRNELLVMLEEHRSGLHNHTKQLRTVLMTKLWLQEFFPETV
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