SitesBLAST
Comparing WP_066918409.1 NCBI__GCF_001579945.1:WP_066918409.1 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)
1e59A E.Coli cofactor-dependent phosphoglycerate mutase complexed with vanadate (see paper)
61% identity, 94% coverage: 4:239/250 of query aligns to 3:238/239 of 1e59A
- active site: H9 (= H10), R60 (= R61), E87 (= E88), H182 (= H183)
- binding tetrametavanadate: R8 (= R9), N15 (= N16), F20 (= F21), T21 (= T22), G22 (= G23), Y90 (= Y91), K98 (= K99), R114 (= R115), R115 (= R116), N184 (= N185)
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)
61% identity, 98% coverage: 4:249/250 of query aligns to 5:250/250 of P62707
- 10:17 (vs. 9:16, 75% identical) binding substrate
- H11 (= H10) active site, Tele-phosphohistidine intermediate
- K18 (≠ L17) modified: N6-acetyllysine
- TG 23:24 (= TG 22:23) binding substrate
- E89 (= E88) active site, Proton donor/acceptor
- ERHY 89:92 (= ERHY 88:91) binding substrate
- K100 (= K99) binding substrate; modified: N6-acetyllysine
- K106 (= K105) modified: N6-acetyllysine
- RR 116:117 (= RR 115:116) binding substrate
- H184 (= H183) Transition state stabilizer
- GN 185:186 (= GN 184:185) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
64% identity, 92% coverage: 4:233/250 of query aligns to 3:232/249 of Q3JWH7
- R8 (= R9) binding (2R)-2,3-bisphosphoglycerate
- H9 (= H10) active site, Tele-phosphohistidine intermediate; binding (2R)-2,3-bisphosphoglycerate
- N15 (= N16) binding (2R)-2,3-bisphosphoglycerate
- T21 (= T22) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- G22 (= G23) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- R60 (= R61) binding (2R)-2,3-bisphosphoglycerate
- E87 (= E88) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- Y90 (= Y91) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- K98 (= K99) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- R114 (= R115) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- R115 (= R116) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
- H182 (= H183) binding (2R)-2,3-bisphosphoglycerate
- G183 (= G184) binding (2R)-2,3-bisphosphoglycerate
- N184 (= N185) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
64% identity, 92% coverage: 4:233/250 of query aligns to 3:232/248 of 3gp5A
3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
64% identity, 91% coverage: 4:231/250 of query aligns to 3:230/230 of 3fdzA
- active site: H9 (= H10), R60 (= R61), E87 (= E88), H182 (= H183)
- binding (2R)-2,3-diphosphoglyceric acid: R8 (= R9), H9 (= H10), N15 (= N16), T21 (= T22), R60 (= R61), E87 (= E88), Y90 (= Y91), K98 (= K99), R114 (= R115), R115 (= R116), H182 (= H183), G183 (= G184), N184 (= N185)
3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
64% identity, 91% coverage: 4:230/250 of query aligns to 3:229/229 of 3gp3A
- active site: H9 (= H10), R60 (= R61), E87 (= E88), H182 (= H183)
- binding phosphite ion: R8 (= R9), H9 (= H10), R60 (= R61), E87 (= E88), H182 (= H183), G183 (= G184)
- binding phosphoserine: T21 (= T22), E87 (= E88), Y90 (= Y91), K98 (= K99), R114 (= R115), R115 (= R116), N184 (= N185)
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)
57% identity, 99% coverage: 4:250/250 of query aligns to 5:254/254 of P18669
- 10:17 (vs. 9:16, 75% identical) binding substrate
- H11 (= H10) active site, Tele-phosphohistidine intermediate
- SG 23:24 (≠ TG 22:23) binding substrate
- Y26 (≠ V25) modified: Phosphotyrosine
- ERHY 89:92 (= ERHY 88:91) binding substrate
- K100 (= K99) binding substrate
- RR 116:117 (= RR 115:116) binding substrate
- K251 (≠ E247) modified: N6-acetyllysine; alternate
- K253 (= K249) modified: N6-acetyllysine
- K254 (= K250) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7xb8B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
58% identity, 97% coverage: 4:245/250 of query aligns to 3:247/249 of 7xb8B
7xb7B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
58% identity, 96% coverage: 4:243/250 of query aligns to 3:245/246 of 7xb7B
1yfkA Crystal structure of human b type phosphoglycerate mutase (see paper)
57% identity, 95% coverage: 4:241/250 of query aligns to 3:243/243 of 1yfkA
8itdC Phosphoglycerate mutase 1 complexed with a compound
58% identity, 94% coverage: 4:238/250 of query aligns to 4:241/242 of 8itdC
8it8C Phosphoglycerate mutase 1 complexed with a compound
58% identity, 93% coverage: 4:236/250 of query aligns to 4:239/240 of 8it8C
5zs8C Acetylation of lysine 100 of phosphoglycerate mutase 1 complexed with kh_ol
58% identity, 93% coverage: 4:236/250 of query aligns to 4:239/240 of 5zs8C
5y65C Phosphoglycerate mutase 1 complexed with a small molecule inhibitor kh2
58% identity, 93% coverage: 4:236/250 of query aligns to 3:238/239 of 5y65C
- active site: H9 (= H10), R60 (= R61), E87 (= E88), H184 (= H183)
- binding ~{N}-[3,4-bis(oxidanyl)-9,10-bis(oxidanylidene)anthracen-2-yl]-4-(dimethylamino)benzenesulfonamide: N18 (= N19), R19 (≠ L20), F20 (= F21), R88 (= R89), K98 (= K99), W113 (= W114), R114 (= R115)
P07738 Bisphosphoglycerate mutase; BPGM; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; 2,3-diphosphoglycerate mutase; DPGM; BPG-dependent PGAM; EC 5.4.2.4; EC 5.4.2.11 from Homo sapiens (Human) (see 5 papers)
53% identity, 99% coverage: 4:250/250 of query aligns to 5:256/259 of P07738
- K5 (= K4) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
- 10:17 (vs. 9:16, 63% identical) binding substrate
- H11 (= H10) active site, Tele-phosphohistidine intermediate
- K18 (≠ L17) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
- CS 23:24 (≠ TG 22:23) binding substrate
- K29 (≠ D28) Not glycated
- K43 (≠ R42) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
- K46 (= K45) Not glycated
- R62 (= R61) binding substrate
- E89 (= E88) active site, Proton donor/acceptor
- ERHY 89:92 (= ERHY 88:91) binding substrate
- R90 (= R89) to C: in ECYT8; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity; dbSNP:rs121964925
- R100 (≠ K99) binding substrate
- RR 116:117 (= RR 115:116) binding substrate
- K143 (vs. gap) Not glycated
- K159 (= K154) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K181 (≠ R176) Not glycated
- H188 (= H183) Transition state stabilizer
- GN 189:190 (= GN 184:185) binding substrate
- K197 (= K192) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
- K246 (≠ D240) Not glycated
- K247 (≠ A241) Not glycated
- K253 (≠ E247) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 3 modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
- 258 Not glycated
- 259 Not glycated
2f90A Crystal structure of bisphosphoglycerate mutase in complex with 3- phosphoglycerate and alf4- (see paper)
53% identity, 99% coverage: 4:250/250 of query aligns to 3:254/254 of 2f90A
2h4zA Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate (see paper)
53% identity, 99% coverage: 4:250/250 of query aligns to 4:255/255 of 2h4zA
- active site: H10 (= H10), R61 (= R61), E88 (= E88), H187 (= H183)
- binding (2R)-2,3-diphosphoglyceric acid: R9 (= R9), H10 (= H10), C22 (≠ T22), S23 (≠ G23), R61 (= R61), E88 (= E88), Y91 (= Y91), R99 (≠ K99), R115 (= R115), R116 (= R116), H187 (= H183), N189 (= N185)
5y2uB X-ray structure of phosphoglycerate mutase 1(pgam1) complexed with a small molecule
58% identity, 93% coverage: 4:235/250 of query aligns to 3:237/237 of 5y2uB