SitesBLAST
Comparing 200919 FitnessBrowser__MR1:200919 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)
Q96G03 Phosphopentomutase; Glucose phosphomutase 2; Phosphodeoxyribomutase; Phosphoglucomutase-2; EC 5.4.2.7; EC 5.4.2.2 from Homo sapiens (Human) (see 2 papers)
38% identity, 94% coverage: 2:542/573 of query aligns to 12:575/612 of Q96G03
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 10 G → D: in dbSNP:rs17856324
O74478 Probable phosphoribomutase; PRM; Phosphoglucomutase 3 homolog; PGM 3 homolog; EC 5.4.2.7 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 94% coverage: 1:536/573 of query aligns to 1:550/587 of O74478
- S149 (= S149) modified: Phosphoserine
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
36% identity, 89% coverage: 32:539/573 of query aligns to 29:549/581 of P18159
- G162 (= G165) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ V242) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G403) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D414) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
Q03262 Phosphoribomutase; PRM; Phosphoglucomutase 3; PGM 3; EC 5.4.2.7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 93% coverage: 5:538/573 of query aligns to 13:586/622 of Q03262
- S158 (= S149) mutation to T: Loss of function.
- P326 (= P306) mutation to G: No effect.
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
27% identity, 88% coverage: 43:549/573 of query aligns to 2:443/455 of 1wqaA
- active site: R11 (= R53), S101 (= S149), H102 (= H150), K111 (= K159), D243 (= D305), D245 (= D307), D247 (= D309), R248 (= R310), G330 (= G403), R340 (≠ K413)
- binding magnesium ion: S101 (= S149), D243 (= D305), D245 (= D307), D247 (= D309)
2fuvA Phosphoglucomutase from salmonella typhimurium.
24% identity, 86% coverage: 45:538/573 of query aligns to 39:519/545 of 2fuvA
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
26% identity, 55% coverage: 41:358/573 of query aligns to 1:290/445 of P31120
- M1 (≠ F41) modified: Initiator methionine, Removed
- S100 (≠ T147) mutation to A: 2% of wild-type activity.; mutation to T: 20-fold increase in the non-specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated).
- S102 (= S149) active site, Phosphoserine intermediate; modified: Phosphoserine; by autocatalysis; mutation to A: Loss of activity in the absence or presence of glucosamine-1,6-diP.
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
25% identity, 86% coverage: 47:538/573 of query aligns to 4:422/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
25% identity, 86% coverage: 47:538/573 of query aligns to 4:422/445 of 7ojrA
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
25% identity, 46% coverage: 52:313/573 of query aligns to 15:246/459 of 4il8A
- active site: R16 (= R53), S104 (= S149), H105 (= H150), K114 (= K159), D238 (= D305), D240 (= D307), D242 (= D309), R243 (= R310)
- binding magnesium ion: S104 (= S149), D238 (= D305), D240 (= D307), D242 (= D309)
Sites not aligning to the query:
P26276 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 10 papers)
25% identity, 47% coverage: 47:313/573 of query aligns to 14:250/463 of P26276
- R15 (≠ G48) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ A50) binding ; binding
- R20 (= R53) mutation to A: No phosphoglucomutase activity.
- S108 (= S149) binding via phosphate group; modified: Phosphoserine; mutation S->A,V: About 5% activity, still subject to substrate inhibition and requires G1,6P as an activator; phosphorylation occurs at a different site.; mutation to C: KM for G1P unchanged, kcat decreases 24-fold; G1,6P stimulates reaction by 2-3 orders of magnitude. No stable protein phosphorylation detected, altered ligation of metal residue.
- N110 (= N151) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D305) binding
- D244 (= D307) binding
- D246 (= D309) binding
- R247 (= R310) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 262 R→A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- 285 binding
- 308 binding ; binding
- 325 E→A: Reduces KM and Vmax approximately 2-fold.
- 325:329 binding ; binding
- 329 H→A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- 368 P→G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- 421 R→C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- 421:425 binding ; binding
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 14:250/463 of Q02E40
- S108 (= S149) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 6:242/455 of 2h5aX
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 6:242/455 of 2h4lX
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 6:242/455 of 2fkfA
- active site: R12 (= R53), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D305), D236 (= D307), D238 (= D309), R239 (= R310)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ G48), H101 (= H150)
- binding zinc ion: S100 (= S149), D234 (= D305), D236 (= D307), D238 (= D309)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 6:242/455 of 1pcmX
- active site: R12 (= R53), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D305), D236 (= D307), D238 (= D309), R239 (= R310)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ A50), S100 (= S149)
- binding zinc ion: S100 (= S149), D234 (= D305), D236 (= D307), D238 (= D309)
Sites not aligning to the query:
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 9:245/458 of 1pcjX
- active site: R15 (= R53), S103 (= S149), H104 (= H150), K113 (= K159), D237 (= D305), D239 (= D307), D241 (= D309), R242 (= R310)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (≠ A50), S103 (= S149)
- binding zinc ion: S103 (= S149), D237 (= D305), D239 (= D307), D241 (= D309)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 6:242/455 of 1p5gX
- active site: R12 (= R53), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D305), D236 (= D307), D238 (= D309), R239 (= R310)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (≠ A50), S100 (= S149)
- binding zinc ion: S100 (= S149), D234 (= D305), D236 (= D307), D238 (= D309)
Sites not aligning to the query:
- active site: 321, 332
- binding 6-O-phosphono-alpha-D-glucopyranose: 277, 299, 300, 317, 319, 321, 413, 415, 416, 417
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 47% coverage: 47:313/573 of query aligns to 6:242/455 of 1p5dX
- active site: R12 (= R53), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D305), D236 (= D307), D238 (= D309), R239 (= R310)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (≠ A50), S100 (= S149), R239 (= R310)
- binding zinc ion: S100 (= S149), D234 (= D305), D236 (= D307), D238 (= D309)
Sites not aligning to the query:
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
24% identity, 70% coverage: 48:448/573 of query aligns to 18:421/562 of P36871
- T19 (= T49) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ Y78) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (≠ E81) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D96) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ Y102) to M: in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs200390982
- T115 (= T147) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S149) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (≠ P153) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ A235) to C: in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs1126728
- D263 (≠ N279) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D305) binding
- D290 (= D307) binding
- G291 (≠ A308) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D309) binding
- G330 (≠ L348) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E400) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D412) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (≠ Q447) to H: in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs11208257
Sites not aligning to the query:
- 467 modified: Phosphothreonine; by PAK1
- 516 L → P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
Query Sequence
>200919 FitnessBrowser__MR1:200919
MNTHLQLQIQHWLKNDPDPSTQAQLQALIDSGNEAELAARFAGRLEFGTAGLRGVVGAGP
MGMNRLVIRQTSAGLGAYLLEQIHDVAERGVVIGYDGRHDSYTFAHDTASVLTAMGIKVR
LTAKVAPTPLVAFGVKHFNAAAGIVVTASHNPPQYNGYKVYWENGAQIIPPHDSGIAAKI
EQAATQAIPFMELDDAIKQGKLIWLNDDYYETYRRGVMHAKVLQNHTAPEKVSLAYTAMH
GVGADMAETVLKDAGFTQVYSVAAQREPDGDFPTVNFPNPEEKGAMDLVIAEAKKHSAML
ACANDPDADRFAVAVRKDDGEYQMLTGDQVGVLFGHYLLSHASADQRLVGTTIVSSSLLS
KIANGFGVESYTTLTGFKWLMNVGIAQSQPDNQFLFAYEEALGYTVGNMVWDKDGLSALV
AFAQLTAELAAKGQTIWDRLEQIYREQGFHLNAQASIALKPETPNIGAYLREHPPLTIGE
HAVVSTDDLKALSRRFADGKVENINLPASDVLTYRLSNGARVIVRPSGTEPKIKCYYEVV
EPMTAQDTLATAQARATQAMEAFISAHQASLPK
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory