SitesBLAST
Comparing CCNA_00083 CCNA_00083 phosphoglucomutase/phosphomannomutase 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)
2fuvA Phosphoglucomutase from salmonella typhimurium.
60% identity, 100% coverage: 2:545/546 of query aligns to 2:543/545 of 2fuvA
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
27% identity, 71% coverage: 65:450/546 of query aligns to 41:429/560 of Q9VUY9
- S116 (= S145) modified: Phosphoserine
- E351 (≠ R366) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
- 17 natural variant: K -> Q
- 28 natural variant: K -> N
- 36 natural variant: T -> M
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
28% identity, 75% coverage: 42:450/546 of query aligns to 31:442/573 of 6snoA
- active site: R36 (= R47), S130 (= S145), H131 (= H146), K143 (= K155), D301 (= D304), D303 (= D306), D305 (= D308), R306 (= R309), G393 (= G395)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S145), E389 (= E391), S391 (= S393)
- binding zinc ion: S130 (= S145), D301 (= D304), D303 (= D306), D305 (= D308)
Sites not aligning to the query:
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
28% identity, 75% coverage: 42:450/546 of query aligns to 31:442/566 of 6snqA
- active site: R36 (= R47), S130 (= S145), H131 (= H146), K143 (= K155), D301 (= D304), D303 (= D306), D305 (= D308), R306 (= R309), G393 (= G395)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S145), T370 (≠ V372), G371 (= G373), E389 (= E391), S391 (= S393)
- binding zinc ion: S130 (= S145), D301 (= D304), D303 (= D306), D305 (= D308)
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)
27% identity, 78% coverage: 24:450/546 of query aligns to 11:429/562 of P36871
- T19 (≠ V32) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ A58) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (≠ L61) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D85) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ E91) 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 (= T143) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S145) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (vs. gap) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ G229) 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 (= D277) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D304) binding
- D290 (= D306) binding
- G291 (≠ A307) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D308) binding
- G330 (= G347) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E392) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D409) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (= Y441) 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
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
27% identity, 70% coverage: 42:425/546 of query aligns to 27:418/572 of 6y8yA
Sites not aligning to the query:
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
26% identity, 82% coverage: 28:477/546 of query aligns to 2:456/553 of 7pjcB
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
27% identity, 78% coverage: 24:450/546 of query aligns to 12:430/559 of 5jn5A
- active site: R24 (≠ A36), S118 (= S145), H119 (= H146), K131 (= K155), D289 (= D304), D291 (= D306), D293 (= D308), R294 (= R309), G381 (= G395), K390 (= K410)
- binding calcium ion: S118 (= S145), D289 (= D304), D291 (= D306), D293 (= D308)
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
28% identity, 74% coverage: 24:425/546 of query aligns to 12:410/499 of 7s0wB
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
27% identity, 78% coverage: 24:450/546 of query aligns to 11:429/562 of P00949
- R23 (≠ A36) binding
- S117 (= S145) active site, Phosphoserine intermediate; binding ; binding via phosphate group; modified: Phosphoserine
- D288 (= D304) binding
- D290 (= D306) binding
- D292 (= D308) binding ; binding
- R293 (= R309) binding
- T357 (≠ V372) binding
- E376 (= E391) binding
- S378 (= S393) binding
- K389 (= K410) binding
3pmgA Structure of rabbit muscle phosphoglucomutase at 2.4 angstroms resolution. Use of freezing point depressant and reduced temperature to enhance diffractivity (see paper)
27% identity, 78% coverage: 24:450/546 of query aligns to 10:428/561 of 3pmgA
- active site: R22 (≠ A36), S116 (= S145), H117 (= H146), K129 (= K155), D287 (= D304), D289 (= D306), D291 (= D308), R292 (= R309), G379 (= G395), K388 (= K410)
- binding magnesium ion: S116 (= S145), D287 (= D304), D289 (= D306), D291 (= D308)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
27% identity, 78% coverage: 24:450/546 of query aligns to 10:428/561 of 1c4gA
- active site: R22 (≠ A36), S116 (= S145), H117 (= H146), K129 (= K155), D287 (= D304), D289 (= D306), D291 (= D308), R292 (= R309), G379 (= G395), K388 (= K410)
- binding cobalt (ii) ion: S116 (= S145), D287 (= D304), D289 (= D306), D291 (= D308)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (≠ A36), S116 (= S145), H117 (= H146), K129 (= K155), R292 (= R309), E375 (= E391), S377 (= S393), K388 (= K410)
Sites not aligning to the query:
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
27% identity, 78% coverage: 24:450/546 of query aligns to 10:428/561 of 1c47A
- active site: R22 (≠ A36), S116 (= S145), H117 (= H146), K129 (= K155), D287 (= D304), D289 (= D306), D291 (= D308), R292 (= R309), G379 (= G395), K388 (= K410)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (≠ A36), S116 (= S145), D291 (= D308), R292 (= R309), E375 (= E391), K388 (= K410)
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
29% identity, 60% coverage: 80:406/546 of query aligns to 28:390/565 of 4qg5A
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 88% coverage: 41:519/546 of query aligns to 44:546/581 of P18159
- G162 (= G161) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ A236) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G395) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D411) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
23% identity, 88% coverage: 40:522/546 of query aligns to 4:433/455 of 1wqaA
- active site: R11 (= R47), S101 (= S145), H102 (= H146), K111 (= K155), D243 (= D304), D245 (= D306), D247 (= D308), R248 (= R309), G330 (= G395), R340 (≠ K410)
- binding magnesium ion: S101 (= S145), D243 (= D304), D245 (= D306), D247 (= D308)
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 65% coverage: 104:459/546 of query aligns to 77:433/554 of O74374
- T111 (= T143) modified: Phosphothreonine
- S113 (= S145) modified: Phosphoserine
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
25% identity, 68% coverage: 80:450/546 of query aligns to 59:449/570 of 1kfiA
- active site: S124 (= S145), H125 (= H146), D306 (= D304), D308 (= D306), D310 (= D308), R311 (= R309), K403 (= K410)
- binding sulfate ion: S124 (= S145), H125 (= H146), D310 (= D308), R311 (= R309)
- binding zinc ion: D306 (= D304), D308 (= D306), D310 (= D308)
Sites not aligning to the query:
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
25% identity, 68% coverage: 80:450/546 of query aligns to 60:450/571 of 1kfqA
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
25% identity, 64% coverage: 55:406/546 of query aligns to 36:386/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S117 (= S145), H118 (= H146), K130 (= K155), D286 (= D308), R287 (= R309), T350 (≠ V372), E369 (= E391), S371 (= S393), K382 (≠ D402)
- binding magnesium ion: S117 (= S145), D282 (= D304), D284 (= D306), D286 (= D308)
Sites not aligning to the query:
Query Sequence
>CCNA_00083 CCNA_00083 phosphoglucomutase/phosphomannomutase
MMHDRAGLRALPEDLVDLDALIGAYFEIKPDVSNPAQKVVFGTSGHRGSSLDGAFNEAHI
LAVTQAIVEYRAAQGVTGPLFVGRDTHGLSEPAWRSVLEVLAANGVEALVDSRDGFTPTP
AVSHAILTHNRQGGRQADGLLLTPSHNPPRDGGIKYNPPSGGPAGSDATSAIAARANELL
AQGLAGVKRVPFETARKAVGDYDFLGRYVDDLPAVIDIAAIRAAKVRIGADPLGGAAVAY
WGAIAERHALDLTVVNDAVDPRWAFMPLDTDGKIRMDCSSSSAMANLIGIMKGGAAYDVA
TGNDADADRHGIVTPDGGLMNPNHYLAAAISYLFSHRPGWGADTAVGKTLVSSSMIDRVV
SGLGRRLLEVPVGFKYFVPGLLDGSVGFGGEESAGAAFLRHDGGVWTTDKDGIQLALLAA
EIQAVTGKSASQLYAGLTDQYGAPAYARVDAPASREEKARLSKLSPSDVSAKTLAGEAIT
DILTAAPGNGEAIGGLKVCTQNAWFAARPSGTEDVYKVYAESFLGADHLKQVQAEAREVV
AGALKG
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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