SitesBLAST
Comparing SMc03925 FitnessBrowser__Smeli:SMc03925 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)
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
55% identity, 100% coverage: 2:542/542 of query aligns to 4:562/562 of P00949
- R23 (= R21) binding
- S117 (= S112) active site, Phosphoserine intermediate; binding ; binding via phosphate group; modified: Phosphoserine
- D288 (= D276) binding
- D290 (= D278) binding
- D292 (= D280) binding ; binding
- R293 (= R281) binding
- T357 (= T343) binding
- E376 (= E362) binding
- S378 (= S364) binding
- K389 (= K375) 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)
55% identity, 100% coverage: 2:542/542 of query aligns to 3:561/561 of 3pmgA
- active site: R22 (= R21), S116 (= S112), H117 (= H113), K129 (= K125), D287 (= D276), D289 (= D278), D291 (= D280), R292 (= R281), G379 (= G366), K388 (= K375)
- binding magnesium ion: S116 (= S112), D287 (= D276), D289 (= D278), D291 (= D280)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
55% identity, 100% coverage: 2:542/542 of query aligns to 3:561/561 of 1c4gA
- active site: R22 (= R21), S116 (= S112), H117 (= H113), K129 (= K125), D287 (= D276), D289 (= D278), D291 (= D280), R292 (= R281), G379 (= G366), K388 (= K375)
- binding cobalt (ii) ion: S116 (= S112), D287 (= D276), D289 (= D278), D291 (= D280)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (= R21), S116 (= S112), H117 (= H113), K129 (= K125), R292 (= R281), E375 (= E362), S377 (= S364), K388 (= K375), R514 (= R495)
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
55% identity, 100% coverage: 2:542/542 of query aligns to 3:561/561 of 1c47A
- active site: R22 (= R21), S116 (= S112), H117 (= H113), K129 (= K125), D287 (= D276), D289 (= D278), D291 (= D280), R292 (= R281), G379 (= G366), K388 (= K375)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (= R21), S116 (= S112), D291 (= D280), R292 (= R281), E375 (= E362), K388 (= K375)
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
54% identity, 100% coverage: 2:542/542 of query aligns to 4:562/562 of P36871
- T19 (= T17) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (= N35) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (= Q38) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D57) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ R63) 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 (≠ S110) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S112) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (= G116) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ V208) 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 (= D250) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D276) binding
- D290 (= D278) binding
- G291 (= G279) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D280) binding
- G330 (= G316) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E363) to K: in CDG1T; decreases strongly solubility
- E388 (= E374) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (= Y406) 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
- T467 (= T447) modified: Phosphothreonine; by PAK1
- L516 (≠ V496) to P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
54% identity, 100% coverage: 2:542/542 of query aligns to 17:573/573 of 6snoA
- active site: R36 (= R21), S130 (= S112), H131 (= H113), K143 (= K125), D301 (= D276), D303 (= D278), D305 (= D280), R306 (= R281), G393 (= G366)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S112), E389 (= E362), S391 (= S364), R514 (= R483), S516 (= S485), G517 (= G486), T518 (= T487), R526 (= R495)
- binding zinc ion: S130 (= S112), D301 (= D276), D303 (= D278), D305 (= D280)
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
54% identity, 100% coverage: 2:542/542 of query aligns to 17:566/566 of 6snqA
- active site: R36 (= R21), S130 (= S112), H131 (= H113), K143 (= K125), D301 (= D276), D303 (= D278), D305 (= D280), R306 (= R281), G393 (= G366)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S112), T370 (= T343), G371 (= G344), E389 (= E362), S391 (= S364), R512 (= R483), S514 (= S490), R519 (= R495)
- binding zinc ion: S130 (= S112), D301 (= D276), D303 (= D278), D305 (= D280)
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
54% identity, 100% coverage: 2:542/542 of query aligns to 5:559/559 of 5jn5A
- active site: R24 (= R21), S118 (= S112), H119 (= H113), K131 (= K125), D289 (= D276), D291 (= D278), D293 (= D280), R294 (= R281), G381 (= G366), K390 (= K375)
- binding calcium ion: S118 (= S112), D289 (= D276), D291 (= D278), D293 (= D280)
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
53% identity, 100% coverage: 2:542/542 of query aligns to 6:558/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: T21 (= T17), R25 (= R21), S117 (= S112), H118 (= H113), K130 (= K125), D286 (= D280), R287 (= R281), T350 (= T343), E369 (= E362), S371 (= S364), K382 (= K375), R499 (= R483), S501 (= S485), G502 (= G486), T503 (= T487), R511 (= R495)
- binding magnesium ion: S117 (= S112), D282 (= D276), D284 (= D278), D286 (= D280)
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
52% identity, 100% coverage: 1:542/542 of query aligns to 1:554/554 of O74374
- T111 (≠ S110) modified: Phosphothreonine
- S113 (= S112) modified: Phosphoserine
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
50% identity, 100% coverage: 2:542/542 of query aligns to 13:572/572 of 6y8yA
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
50% identity, 100% coverage: 2:542/542 of query aligns to 5:560/560 of Q9VUY9
- E6 (≠ R3) natural variant: E -> G
- K17 (= K14) natural variant: K -> Q
- K28 (≠ P25) natural variant: K -> N
- T36 (≠ A33) natural variant: T -> M
- S116 (= S112) modified: Phosphoserine
- E351 (≠ G337) natural variant: E -> K
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
50% identity, 100% coverage: 2:542/542 of query aligns to 2:553/553 of 7pjcB
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
51% identity, 96% coverage: 2:522/542 of query aligns to 5:499/499 of 7s0wB
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
50% identity, 100% coverage: 3:542/542 of query aligns to 8:571/571 of 1kfqA
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
50% identity, 100% coverage: 3:542/542 of query aligns to 7:570/570 of 1kfiA
- active site: S124 (= S112), H125 (= H113), D306 (= D276), D308 (= D278), D310 (= D280), R311 (= R281), K403 (= K375)
- binding sulfate ion: S124 (= S112), H125 (= H113), D310 (= D280), R311 (= R281), R513 (= R483), S515 (= S485), R525 (= R495)
- binding zinc ion: D306 (= D276), D308 (= D278), D310 (= D280)
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
47% identity, 95% coverage: 27:542/542 of query aligns to 1:565/565 of 4qg5A
2fuvA Phosphoglucomutase from salmonella typhimurium.
29% identity, 66% coverage: 54:413/542 of query aligns to 82:446/545 of 2fuvA
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
29% identity, 56% coverage: 87:389/542 of query aligns to 76:354/455 of 1wqaA
- active site: S101 (= S112), H102 (= H113), K111 (= K125), D243 (= D276), D245 (= D278), D247 (= D280), R248 (= R281), G330 (= G366), R340 (≠ K375)
- binding magnesium ion: S101 (= S112), D243 (= D276), D245 (= D278), D247 (= D280)
Sites not aligning to the query:
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
23% identity, 88% coverage: 10:487/542 of query aligns to 39:539/581 of P18159
- G162 (= G131) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ V215) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G366) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D376) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
Query Sequence
>SMc03925 FitnessBrowser__Smeli:SMc03925
MIRTVSTNPYGDQKPGTSGLRKKVPVFQQKNYAENFIQSIFDSLEGFEGQTLVIGGDGRY
YNREVIQKAVKMAAANGFGRVLVGRGGILSTPAASNVIRKYKAFGGIVLSASHNPGGPTE
DFGIKYNVGNGGPAPEKVTDAIYSRSKAIDSYKIADAPDVNLDVEGSQQVEDMTVTVIDP
VADYAELMESLFDFDAIRKLIAGGFRVVFDAMSAVTGPYAKEIIEKRLGAPKGSVMNFIP
LPDFGGHHPDPNLVHARALYETMMAPDAPDFGAASDGDGDRNLIIGKGIFVTPSDSLAML
AANAHLAPGYAKGLAGIARSMPTSGAADRVAEKLGVGIYETPTGWKFFGNLLDEGLATIC
GEESAGTGSNHVREKDGLWAVLLWLNILAARKESALEIARKHWATYGRNYYSRHDYEEVD
TDAANGLIAALRDKLAALPGKSFGALTVETADDFSYHDPVDKSVSKNQGVRILFKGGSRV
VFRLSGTGTSGATLRVYIERYEPDPTRHDLDTQEALADLIAVADEIAEIKANTGRDEPSV
IT
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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