SitesBLAST
Comparing WP_015449177.1 NCBI__GCF_000230695.2:WP_015449177.1 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)
2fuvA Phosphoglucomutase from salmonella typhimurium.
58% identity, 98% coverage: 9:547/548 of query aligns to 6:542/545 of 2fuvA
Q9VUY9 Phosphoglucomutase 1; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
25% identity, 88% coverage: 68:547/548 of query aligns to 41:542/560 of Q9VUY9
- S116 (= S149) modified: Phosphoserine
- E351 (≠ Q369) 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
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
25% identity, 91% coverage: 30:529/548 of query aligns to 7:534/572 of 6y8yA
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
25% identity, 80% coverage: 27:462/548 of query aligns to 11:438/562 of P00949
- R23 (vs. gap) binding alpha-D-glucose 1,6-bisphosphate
- S117 (= S149) active site, Phosphoserine intermediate; binding alpha-D-glucose 1,6-bisphosphate; binding via phosphate group; modified: Phosphoserine
- D288 (= D307) binding Mg(2+)
- D290 (= D309) binding Mg(2+)
- D292 (= D311) binding alpha-D-glucose 1,6-bisphosphate; binding Mg(2+)
- R293 (= R312) binding alpha-D-glucose 1,6-bisphosphate
- T357 (≠ V375) binding alpha-D-glucose 1,6-bisphosphate
- E376 (= E394) binding alpha-D-glucose 1,6-bisphosphate
- S378 (= S396) binding alpha-D-glucose 1,6-bisphosphate
- K389 (= K413) binding alpha-D-glucose 1,6-bisphosphate
3pmgA Structure of rabbit muscle phosphoglucomutase at 2.4 angstroms resolution. Use of freezing point depressant and reduced temperature to enhance diffractivity (see paper)
25% identity, 80% coverage: 27:462/548 of query aligns to 10:437/561 of 3pmgA
- active site: R22 (vs. gap), S116 (= S149), H117 (= H150), K129 (= K159), D287 (= D307), D289 (= D309), D291 (= D311), R292 (= R312), G379 (= G398), K388 (= K413)
- binding magnesium ion: S116 (= S149), D287 (= D307), D289 (= D309), D291 (= D311)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
25% identity, 80% coverage: 27:462/548 of query aligns to 10:437/561 of 1c4gA
- active site: R22 (vs. gap), S116 (= S149), H117 (= H150), K129 (= K159), D287 (= D307), D289 (= D309), D291 (= D311), R292 (= R312), G379 (= G398), K388 (= K413)
- binding cobalt (ii) ion: S116 (= S149), D287 (= D307), D289 (= D309), D291 (= D311)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (vs. gap), S116 (= S149), H117 (= H150), K129 (= K159), R292 (= R312), E375 (= E394), S377 (= S396), K388 (= K413)
Sites not aligning to the query:
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
25% identity, 80% coverage: 27:462/548 of query aligns to 10:437/561 of 1c47A
- active site: R22 (vs. gap), S116 (= S149), H117 (= H150), K129 (= K159), D287 (= D307), D289 (= D309), D291 (= D311), R292 (= R312), G379 (= G398), K388 (= K413)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (vs. gap), S116 (= S149), D291 (= D311), R292 (= R312), E375 (= E394), K388 (= K413)
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 80% coverage: 26:463/548 of query aligns to 23:452/566 of 6snqA
- active site: R36 (= R50), S130 (= S149), H131 (= H150), K143 (= K159), D301 (= D307), D303 (= D309), D305 (= D311), R306 (= R312), G393 (= G398)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S149), T370 (≠ V375), G371 (= G376), E389 (= E394), S391 (= S396)
- binding zinc ion: S130 (= S149), D301 (= D307), D303 (= D309), D305 (= D311)
Sites not aligning to the query:
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 80% coverage: 26:463/548 of query aligns to 23:452/573 of 6snoA
- active site: R36 (= R50), S130 (= S149), H131 (= H150), K143 (= K159), D301 (= D307), D303 (= D309), D305 (= D311), R306 (= R312), G393 (= G398)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S149), E389 (= E394), S391 (= S396)
- binding zinc ion: S130 (= S149), D301 (= D307), D303 (= D309), D305 (= D311)
Sites not aligning to the query:
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
26% identity, 93% coverage: 38:544/548 of query aligns to 9:536/553 of 7pjcB
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
25% identity, 80% coverage: 27:463/548 of query aligns to 11:439/562 of P36871
- T19 (= T46) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ I63) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (≠ S67) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D88) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ Q94) 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 (≠ G235) 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 (= D283) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D307) binding Mg(2+)
- D290 (= D309) binding Mg(2+)
- G291 (≠ H310) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D311) binding Mg(2+)
- G330 (≠ A347) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E395) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D412) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (≠ L444) 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
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 91% coverage: 42:538/548 of query aligns to 42:566/581 of P18159
- G162 (= G165) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (vs. gap) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G398) 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.
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
24% identity, 92% coverage: 44:548/548 of query aligns to 5:455/455 of 1wqaA
- active site: R11 (= R50), S101 (= S149), H102 (= H150), K111 (= K159), D243 (= D307), D245 (= D309), D247 (= D311), R248 (= R312), G330 (= G398), R340 (≠ K413)
- binding magnesium ion: S101 (= S149), D243 (= D307), D245 (= D309), D247 (= D311)
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
25% identity, 80% coverage: 27:463/548 of query aligns to 12:440/559 of 5jn5A
- active site: R24 (vs. gap), S118 (= S149), H119 (= H150), K131 (= K159), D289 (= D307), D291 (= D309), D293 (= D311), R294 (= R312), G381 (= G398), K390 (= K413)
- binding calcium ion: S118 (= S149), D289 (= D307), D291 (= D309), D293 (= D311)
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
26% identity, 78% coverage: 27:456/548 of query aligns to 12:433/499 of 7s0wB
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 63% coverage: 83:427/548 of query aligns to 53:392/554 of O74374
- T111 (= T147) modified: Phosphothreonine
- S113 (= S149) modified: Phosphoserine
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
24% identity, 68% coverage: 83:453/548 of query aligns to 59:449/570 of 1kfiA
- active site: S124 (= S149), H125 (= H150), D306 (= D307), D308 (= D309), D310 (= D311), R311 (= R312), K403 (= K413)
- binding sulfate ion: S124 (= S149), H125 (= H150), D310 (= D311), R311 (= R312)
- binding zinc ion: D306 (= D307), D308 (= D309), D310 (= D311)
Sites not aligning to the query:
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
24% identity, 68% coverage: 83:453/548 of query aligns to 60:450/571 of 1kfqA
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
26% identity, 80% coverage: 45:482/548 of query aligns to 20:460/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: T21 (= T46), R25 (= R50), S117 (= S149), H118 (= H150), K130 (= K159), D286 (= D311), R287 (= R312), T350 (≠ V375), E369 (= E394), S371 (= S396), K382 (= K413)
- binding magnesium ion: S117 (= S149), D282 (= D307), D284 (= D309), D286 (= D311)
Sites not aligning to the query:
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
23% identity, 90% coverage: 44:538/548 of query aligns to 1:529/565 of 4qg5A
Query Sequence
>WP_015449177.1 NCBI__GCF_000230695.2:WP_015449177.1
MSQKISPLAGKPAPSSILVDIPQLLAAYADLKPDPAVPAQRVAFGTSGHRGSSLERSFNE
AHILAISQAICEYRRSKGIDGPLFIGADTHALSQPAFENALEVLAANGVAAMISAGGEVT
PTPAVSHAILVYNKGRTSGLADGIVITPSHNPPDNGGFKYNPSNGGPADSDITKWVENRA
NALLEGGLKDVRRMPYAQARQAATTHEHDYLNSYVADLANIVDFDVIRSAGVHMGVDPLG
GAGVHYWAPIAERYKLDLTVVSAVVDPQFAFMSVDWDGKIRMDPSSKYAMQRLIGLKDQY
DVAFACDTDHDRHGVVTRSSGLMEPNHYLSVLIDYLFRHRPQWGAHAAVGKTVVSTALID
RVAKRLGRQLYEAPVGFKWFAPGLFDGSLGFGCEESAGASLLRRDGTAWVTDKDGLVPAL
LSAEITAREGKDPGELYAQLTRELGKPFASRVDAAATPAQKAKLAKLSPDQLKSDQLAGE
KIEQVLDKAPGNGAAIGGIKAIAASGWFAARPSGTEAIYKVYAESFKSEEHLQALLKEAQ
GIVDAALA
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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