Comparing WP_012592759.1 NCBI__GCF_000021745.1:WP_012592759.1 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)
P36623 Phosphoglycerate mutase; PGAM; BPG-dependent PGAM; MPGM; Phosphoglyceromutase; EC 5.4.2.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
59% identity, 98% coverage: 4:205/206 of query aligns to 9:210/211 of P36623
Q3JWH7 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Burkholderia pseudomallei (strain 1710b) (see paper)
49% identity, 91% coverage: 5:192/206 of query aligns to 4:216/249 of Q3JWH7
3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
49% identity, 91% coverage: 5:192/206 of query aligns to 4:216/248 of 3gp5A
3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
49% identity, 91% coverage: 5:192/206 of query aligns to 4:216/229 of 3gp3A
3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
49% identity, 91% coverage: 5:192/206 of query aligns to 4:216/230 of 3fdzA
1e59A E.Coli cofactor-dependent phosphoglycerate mutase complexed with vanadate (see paper)
47% identity, 91% coverage: 5:192/206 of query aligns to 4:216/239 of 1e59A
P62707 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Escherichia coli (strain K12) (see 6 papers)
47% identity, 91% coverage: 5:192/206 of query aligns to 6:218/250 of P62707
Sites not aligning to the query:
P18669 Phosphoglycerate mutase 1; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; PGAM-B; EC 5.4.2.11; EC 5.4.2.4 from Homo sapiens (Human) (see 4 papers)
47% identity, 91% coverage: 5:192/206 of query aligns to 6:220/254 of P18669
Sites not aligning to the query:
7xb8B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
47% identity, 91% coverage: 5:192/206 of query aligns to 4:218/249 of 7xb8B
7xb7B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
47% identity, 91% coverage: 5:192/206 of query aligns to 4:218/246 of 7xb7B
8it8C Phosphoglycerate mutase 1 complexed with a compound
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/240 of 8it8C
5zs8C Acetylation of lysine 100 of phosphoglycerate mutase 1 complexed with kh_ol
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/240 of 5zs8C
8itdC Phosphoglycerate mutase 1 complexed with a compound
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/242 of 8itdC
7xb9B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
47% identity, 91% coverage: 5:192/206 of query aligns to 4:218/231 of 7xb9B
5y65C Phosphoglycerate mutase 1 complexed with a small molecule inhibitor kh2
47% identity, 91% coverage: 5:192/206 of query aligns to 4:218/239 of 5y65C
1yfkA Crystal structure of human b type phosphoglycerate mutase (see paper)
47% identity, 91% coverage: 5:192/206 of query aligns to 4:218/243 of 1yfkA
8itcC Phosphoglycerate mutase 1 complexed with a compound
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/237 of 8itcC
8itbC Phosphoglycerate mutase 1 complexed with a compound
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/237 of 8itbC
8it7C Phosphoglycerate mutase 1 complexed with a compound
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/237 of 8it7C
8it6C Phosphoglycerate mutase 1 complexed with a compound
47% identity, 91% coverage: 5:192/206 of query aligns to 5:219/237 of 8it6C
>WP_012592759.1 NCBI__GCF_000021745.1:WP_012592759.1
MDRLLVLVRHGQSEWNLQNLFTGWKDPDLTDLGVSEAKAAGRALKTAGVGFDIGFTSDLL
RAQRTMKLLLAEFGQPDLQVTKNVSLNERDYGDLSGLNKAEAAQQWGDEQVHLWRRSYDV
PPPGGESLKDTVARVLPYYCQEILPAVLNGKRTLVTAHGNSLRALIMVLDKLTPKTIPGM
ELATGVPIVYRLKADSTVESKQVLEP
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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