Comparing WP_051335378.1 NCBI__GCF_000427445.1:WP_051335378.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
38% identity, 96% coverage: 18:453/456 of query aligns to 8:456/456 of P43889
4kqlA Hin glmu bound to wg578 (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 4kqlA
4kpzA Hin glmu bound to a small molecule fragment (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 4kpzA
4kpxA Hin glmu bound to wg766 (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 4kpxA
4knxA Hin glmu bound to wg176 (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 4knxA
4knrA Hin glmu bound to wg188 (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 4knrA
4e1kA Glmu in complex with a quinazoline compound (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 4e1kA
2w0wA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 2
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 2w0wA
Sites not aligning to the query:
2w0vA Crystal structure of glmu from haemophilus influenzae in complex with quinazoline inhibitor 1
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 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)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 2vd4A
2v0lA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 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)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 2v0kA
2v0jA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/449 of 2v0jA
2v0iA Characterization of substrate binding and catalysis of the potential antibacterial target n-acetylglucosamine-1-phosphate uridyltransferase (glmu) (see paper)
39% identity, 95% coverage: 18:448/456 of query aligns to 5:448/450 of 2v0iA
Sites not aligning to the query:
Q8Z9S7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Yersinia pestis
39% identity, 95% coverage: 19:453/456 of query aligns to 9:456/456 of Q8Z9S7
P0ACC7 Bifunctional protein GlmU; EC 2.7.7.23; EC 2.3.1.157 from Escherichia coli (strain K12) (see 6 papers)
39% identity, 95% coverage: 19:453/456 of query aligns to 9:456/456 of P0ACC7
Sites not aligning to the query:
2oi6B E. Coli glmu- complex with udp-glcnac, coa and glcn-1-po4 (see paper)
39% identity, 95% coverage: 19:451/456 of query aligns to 7:452/452 of 2oi6B
1hm9A Crystal structure of s.Pneumoniae n-acetylglucosamine-1-phosphate uridyltransferase, glmu, bound to acetyl coenzyme a and udp-n- acetylglucosamine (see paper)
37% identity, 95% coverage: 15:447/456 of query aligns to 1:448/458 of 1hm9A
1hm8A Crystal structure of s.Pneumoniae n-acetylglucosamine-1-phosphate uridyltransferase, glmu, bound to acetyl coenzyme a (see paper)
37% identity, 95% coverage: 15:447/456 of query aligns to 1:448/458 of 1hm8A
2oi7A E. Coli glmu- complex with udp-glcnac, desulpho-coa and glcnac-1-po4 (see paper)
40% identity, 94% coverage: 19:448/456 of query aligns to 6:448/449 of 2oi7A
>WP_051335378.1 NCBI__GCF_000427445.1:WP_051335378.1
MLAAPPLGSGRAGRTCLAIVLAAGEGTRMRSARSKVLHKLAGRTMLAHVLTAVVAAGADA
VAVVAGGDPEAIAAEAKTVAPQAELAIQAERLGTAHAALAARHVIARGYDDILIVFADTP
LVRPQTFAEMRKALAAGRRAVVALGFEARDPTGYGRLIVADGALIAIREDRDASDEERKL
RICNAGLMALDGAKALALLEAVGCANSKGEYYLTDVVAIARSRGLEARALAVDESEVRGV
NDRVQLAAAEAILQRRLREKAMLNGASLIDPESVTLSFDTILERDVVVEPHVVFGLGVSV
AEGAVIRSFSHLEGAVVGPKTTIGPFARLRPGTDLGPNVHIGNFVELKAAKVEAGAKINH
LSYIGDAVIGAKTNIGAGTITCNYDGFGKFRTEIGEGAFIGSNSALVAPVKIGAGAYVGS
GSVITADVAPDALALGRAVQVEKVGWAKAFRSRNQK
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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