Comparing AZOBR_RS09680 FitnessBrowser__azobra:AZOBR_RS09680 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 20 (the maximum) hits to proteins with known functional sites (download)
P43889 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see 3 papers)
40% identity, 98% coverage: 1:442/451 of query aligns to 1:456/456 of P43889
Q8Z9S7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Yersinia pestis
40% identity, 97% coverage: 7:442/451 of query aligns to 6:456/456 of Q8Z9S7
4kqlA Hin glmu bound to wg578 (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 4kqlA
4kpzA Hin glmu bound to a small molecule fragment (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 4kpzA
4kpxA Hin glmu bound to wg766 (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 4kpxA
4knxA Hin glmu bound to wg176 (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 4knxA
4knrA Hin glmu bound to wg188 (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 4knrA
4e1kA Glmu in complex with a quinazoline compound (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 4e1kA
2w0wA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 2
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 2w0wA
Sites not aligning to the query:
2w0vA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 1
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 2w0vA
Sites not aligning to the query:
2vd4A Structure of small-molecule inhibitor of glmu from haemophilus influenzae reveals an allosteric binding site (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 2vd4A
2v0lA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 2v0lA
Sites not aligning to the query:
2v0kA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1- phosphate uridyltransferase (glmu) (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 2v0kA
2v0iA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/450 of 2v0iA
Sites not aligning to the query:
2v0jA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
41% identity, 96% coverage: 5:437/451 of query aligns to 1:448/449 of 2v0jA
4fceA Crystal structure of yersinia pestis glmu in complex with alpha-d- glucosamine 1-phosphate (gp1)
41% identity, 95% coverage: 7:435/451 of query aligns to 3:441/441 of 4fceA
Q97R46 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) (see 2 papers)
39% identity, 97% coverage: 9:446/451 of query aligns to 5:459/459 of Q97R46
1hm9A Crystal structure of s.Pneumoniae n-acetylglucosamine-1-phosphate uridyltransferase, glmu, bound to acetyl coenzyme a and udp-n- acetylglucosamine (see paper)
39% identity, 97% coverage: 9:446/451 of query aligns to 4:458/458 of 1hm9A
1hm8A Crystal structure of s.Pneumoniae n-acetylglucosamine-1-phosphate uridyltransferase, glmu, bound to acetyl coenzyme a (see paper)
39% identity, 97% coverage: 9:446/451 of query aligns to 4:458/458 of 1hm8A
7kr9A Bifunctional enzyme glmu bound to zn(ii) (see paper)
39% identity, 97% coverage: 9:446/451 of query aligns to 4:453/453 of 7kr9A
>AZOBR_RS09680 FitnessBrowser__azobra:AZOBR_RS09680
MTQHRPLACVILAAGKGTRMKSDLPKVLHRVAGQPMVGHVLSAVRALDPDHVVVVVGPGM
DNVADAVAPYPTAVQHEQRGTADAVRAAFGLLEGFDGDVVVLYGDTPLVTPDTLRAMVAA
RRQPNDPAVVVLGMRPDDPGAYGRLILNARGGLEKIVEYLDASEEERQVSLCNAGLMAFD
GARMFDLINRIGNSNAKSEYYLTDVVQIARSNGMACAVVEAAPAEVVGVNSRAELSEVEK
LIQRRLRKAAMDNGATLTDPDSVTFCVDTRLGRDVIVGPHVVFGPGVVVADRVEIKAFSH
LEQVRVDSGAQVGPYARLRPGAEIGPDAHIGNFVEIKNAKIEAGAKVNHLTYIGDARVGA
KANIGAGTITCNYDGYAKSHTDIGAGAFIGSNTALVAPVRVGDGAIVGAGSVVTTDVEGD
ALVVARGRQQAYTGWAKRFRERKQNEKAKKA
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