Comparing WP_011800338.1 NCBI__GCF_000015505.1:WP_011800338.1 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)
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)
73% identity, 100% coverage: 1:249/250 of query aligns to 1:249/249 of Q3JWH7
3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
73% identity, 99% coverage: 1:247/250 of query aligns to 1:247/248 of 3gp5A
3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
74% identity, 92% coverage: 1:230/250 of query aligns to 1:230/230 of 3fdzA
3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
74% identity, 92% coverage: 1:229/250 of query aligns to 1:229/229 of 3gp3A
1e59A E.Coli cofactor-dependent phosphoglycerate mutase complexed with vanadate (see paper)
65% identity, 94% coverage: 3:238/250 of query aligns to 3:239/239 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)
64% identity, 98% coverage: 3:247/250 of query aligns to 5:249/250 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)
60% identity, 98% coverage: 2:247/250 of query aligns to 4:252/254 of P18669
Sites not aligning to the query:
7xb8B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
60% identity, 98% coverage: 2:246/250 of query aligns to 2:249/249 of 7xb8B
7xb7B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
60% identity, 97% coverage: 2:243/250 of query aligns to 2:246/246 of 7xb7B
1yfkA Crystal structure of human b type phosphoglycerate mutase (see paper)
60% identity, 96% coverage: 2:240/250 of query aligns to 2:243/243 of 1yfkA
8itdC Phosphoglycerate mutase 1 complexed with a compound
60% identity, 94% coverage: 2:237/250 of query aligns to 3:241/242 of 8itdC
8it8C Phosphoglycerate mutase 1 complexed with a compound
60% identity, 94% coverage: 2:236/250 of query aligns to 3:240/240 of 8it8C
5zs8C Acetylation of lysine 100 of phosphoglycerate mutase 1 complexed with kh_ol
60% identity, 94% coverage: 2:236/250 of query aligns to 3:240/240 of 5zs8C
5y65C Phosphoglycerate mutase 1 complexed with a small molecule inhibitor kh2
60% identity, 94% coverage: 2:236/250 of query aligns to 2:239/239 of 5y65C
8itcC Phosphoglycerate mutase 1 complexed with a compound
60% identity, 92% coverage: 2:232/250 of query aligns to 3:236/237 of 8itcC
8itbC Phosphoglycerate mutase 1 complexed with a compound
60% identity, 92% coverage: 2:232/250 of query aligns to 3:236/237 of 8itbC
8it7C Phosphoglycerate mutase 1 complexed with a compound
60% identity, 92% coverage: 2:232/250 of query aligns to 3:236/237 of 8it7C
8it6C Phosphoglycerate mutase 1 complexed with a compound
60% identity, 92% coverage: 2:232/250 of query aligns to 3:236/237 of 8it6C
8it5C Phosphoglycerate mutase 1 complexed with a compound
60% identity, 92% coverage: 2:232/250 of query aligns to 3:236/237 of 8it5C
5y35C Phosphoglycerate mutase 1 complexed with a small molecule inhibitor kh1
60% identity, 92% coverage: 2:232/250 of query aligns to 3:236/237 of 5y35C
>WP_011800338.1 NCBI__GCF_000015505.1:WP_011800338.1
MYKLVLIRHGESTWNLDNRFTGWTDVDLTETGIAQAKNSGQLLKAEGYDFDLAYTSVLKR
ATRTLWHVLDEMDQTWLPVEHSWRLNERHYGDLQGLNKAETAKKFGDEQVLVWRRSYDTP
PPPLAANDPRSERSDRRYANLLPGQVPLTECLKDTVERVLPFWNEAMAPAIKAGKRIVVA
AHGNSIRALVKYLDNISDSDIVGLNIPNGIPLVYELDENLKPLRSYYLGDSEAAAKAAAA
VGAQGKAVAA
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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