SitesBLAST
Comparing WP_092346059.1 NCBI__GCF_900107645.1:WP_092346059.1 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)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
32% identity, 98% coverage: 6:467/473 of query aligns to 5:446/455 of 1wqaA
- active site: R11 (= R12), S101 (= S103), H102 (= H104), K111 (= K113), D243 (= D253), D245 (= D255), D247 (= D257), R248 (= R258), G330 (= G341), R340 (≠ K351)
- binding magnesium ion: S101 (= S103), D243 (= D253), D245 (= D255), D247 (= D257)
2fuvA Phosphoglucomutase from salmonella typhimurium.
30% identity, 95% coverage: 4:454/473 of query aligns to 39:520/545 of 2fuvA
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
29% identity, 96% coverage: 4:455/473 of query aligns to 42:550/581 of P18159
- G162 (= G119) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ C194) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G341) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D352) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
29% identity, 95% coverage: 5:454/473 of query aligns to 17:477/499 of 7s0wB
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
28% identity, 95% coverage: 5:454/473 of query aligns to 16:520/562 of P36871
- T19 (= T8) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ E18) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (= Q29) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D50) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ A56) 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 (= T101) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S103) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (≠ Y107) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ A187) 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 (≠ E227) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D253) binding Mg(2+)
- D290 (= D255) binding Mg(2+)
- G291 (≠ A256) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D257) binding Mg(2+)
- G330 (= G290) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E338) to K: in CDG1T; decreases strongly solubility
- E388 (= E350) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (≠ V382) 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 (vs. gap) modified: Phosphothreonine; by PAK1
- L516 (= L450) to P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
28% identity, 95% coverage: 5:454/473 of query aligns to 17:517/559 of 5jn5A
- active site: R24 (= R12), S118 (= S103), H119 (= H104), K131 (= K113), D289 (= D253), D291 (= D255), D293 (= D257), R294 (= R258), G381 (= G341), K390 (= K351)
- binding calcium ion: S118 (= S103), D289 (= D253), D291 (= D255), D293 (= D257)
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
28% identity, 95% coverage: 5:454/473 of query aligns to 29:524/566 of 6snqA
- active site: R36 (= R12), S130 (= S103), H131 (= H104), K143 (= K113), D301 (= D253), D303 (= D255), D305 (= D257), R306 (= R258), G393 (= G341)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S103), T370 (≠ V318), G371 (= G319), E389 (= E337), S391 (= S339), R512 (= R440), S514 (= S442), R519 (= R449)
- binding zinc ion: S130 (= S103), D301 (= D253), D303 (= D255), D305 (= D257)
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
28% identity, 95% coverage: 5:454/473 of query aligns to 29:531/573 of 6snoA
- active site: R36 (= R12), S130 (= S103), H131 (= H104), K143 (= K113), D301 (= D253), D303 (= D255), D305 (= D257), R306 (= R258), G393 (= G341)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S103), E389 (= E337), S391 (= S339), R514 (= R440), S516 (= S442), G517 (= G443), T518 (= T444), R526 (= R449)
- binding zinc ion: S130 (= S103), D301 (= D253), D303 (= D255), D305 (= D257)
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, 95% coverage: 5:454/473 of query aligns to 15:519/561 of 3pmgA
- active site: R22 (= R12), S116 (= S103), H117 (= H104), K129 (= K113), D287 (= D253), D289 (= D255), D291 (= D257), R292 (= R258), G379 (= G341), K388 (= K351)
- binding magnesium ion: S116 (= S103), D287 (= D253), D289 (= D255), D291 (= D257)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
27% identity, 95% coverage: 5:454/473 of query aligns to 15:519/561 of 1c4gA
- active site: R22 (= R12), S116 (= S103), H117 (= H104), K129 (= K113), D287 (= D253), D289 (= D255), D291 (= D257), R292 (= R258), G379 (= G341), K388 (= K351)
- binding cobalt (ii) ion: S116 (= S103), D287 (= D253), D289 (= D255), D291 (= D257)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (= R12), S116 (= S103), H117 (= H104), K129 (= K113), R292 (= R258), E375 (= E337), S377 (= S339), K388 (= K351), R514 (= R449)
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
27% identity, 95% coverage: 5:454/473 of query aligns to 15:519/561 of 1c47A
- active site: R22 (= R12), S116 (= S103), H117 (= H104), K129 (= K113), D287 (= D253), D289 (= D255), D291 (= D257), R292 (= R258), G379 (= G341), K388 (= K351)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (= R12), S116 (= S103), D291 (= D257), R292 (= R258), E375 (= E337), K388 (= K351)
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
27% identity, 95% coverage: 5:454/473 of query aligns to 16:520/562 of P00949
- R23 (= R12) binding alpha-D-glucose 1,6-bisphosphate
- S117 (= S103) active site, Phosphoserine intermediate; binding alpha-D-glucose 1,6-bisphosphate; binding via phosphate group; modified: Phosphoserine
- D288 (= D253) binding Mg(2+)
- D290 (= D255) binding Mg(2+)
- D292 (= D257) binding alpha-D-glucose 1,6-bisphosphate; binding Mg(2+)
- R293 (= R258) binding alpha-D-glucose 1,6-bisphosphate
- T357 (≠ V318) binding alpha-D-glucose 1,6-bisphosphate
- E376 (= E337) binding alpha-D-glucose 1,6-bisphosphate
- S378 (= S339) binding alpha-D-glucose 1,6-bisphosphate
- K389 (= K351) binding alpha-D-glucose 1,6-bisphosphate
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
29% identity, 95% coverage: 5:454/473 of query aligns to 17:520/560 of Q9VUY9
- K17 (= K5) natural variant: K -> Q
- K28 (vs. gap) natural variant: K -> N
- T36 (≠ L21) natural variant: T -> M
- S116 (= S103) modified: Phosphoserine
- E351 (≠ K312) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
27% identity, 87% coverage: 45:454/473 of query aligns to 66:530/572 of 6y8yA
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
29% identity, 99% coverage: 5:473/473 of query aligns to 14:536/553 of 7pjcB
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
29% identity, 90% coverage: 28:453/473 of query aligns to 11:515/565 of 4qg5A
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
28% identity, 88% coverage: 38:453/473 of query aligns to 50:515/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S117 (= S103), H118 (= H104), K130 (= K113), D286 (= D257), R287 (= R258), T350 (≠ V318), E369 (= E337), S371 (= S339), K382 (= K351), R499 (= R440), S501 (= S442), G502 (= G443), T503 (= T444), R511 (= R449)
- binding magnesium ion: S117 (= S103), D282 (= D253), D284 (= D255), D286 (= D257)
Sites not aligning to the query:
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 95% coverage: 7:453/473 of query aligns to 16:511/554 of O74374
- T111 (= T101) modified: Phosphothreonine
- S113 (= S103) modified: Phosphoserine
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
28% identity, 95% coverage: 5:451/473 of query aligns to 19:528/571 of 1kfqA
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
28% identity, 95% coverage: 5:451/473 of query aligns to 18:527/570 of 1kfiA
- active site: S124 (= S103), H125 (= H104), D306 (= D253), D308 (= D255), D310 (= D257), R311 (= R258), K403 (= K351)
- binding sulfate ion: S124 (= S103), H125 (= H104), D310 (= D257), R311 (= R258), R513 (= R440), S515 (= S442), R525 (= R449)
- binding zinc ion: D306 (= D253), D308 (= D255), D310 (= D257)
Query Sequence
>WP_092346059.1 NCBI__GCF_900107645.1:WP_092346059.1
MAHIKFGTSGWRAIFCEEFTLENVRIVVQAIADHLHAEGLADKGIVIGYDARFMGADFSR
ETARILAGTGIKGFFCQRDTPTPVISHELLRRKAAGAINFTASHNPYNYSGIKFSPVSGG
PALPATTNDIEERANTMTVESVSKGMDLKTAAEKGLFEEIDPREDYFTTLKSLIDLKAIA
AAGMTLAVNPLYGCGRGYLDRILDEAGVKVVRINDHVDPYFGGQPPEPSEEHIQDFISLI
KGDDSIALGLATDGDADRFGIIDSDGTYIEPNYILALLFDYMIRRKGLRGDAARSVATSH
LIDAVAAYHGVKVLETPVGFKFIGEYISENKILIGGEESAGLTIKGHVPEKDGILACLLV
AEMVAVEKKNLQELLTDLYSRVGEIYTKRINIQLSPELEAALPDKFANPPERIGELKITD
IIRIDGNKYLLEDGSWVLFRKSGTEPVVRLYAETKSYASLDKLIELGRKFILE
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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