SitesBLAST
Comparing 201480 FitnessBrowser__MR1:201480 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 19 hits to proteins with known functional sites (download)
2fuvA Phosphoglucomutase from salmonella typhimurium.
59% identity, 99% coverage: 2:548/550 of query aligns to 1:542/545 of 2fuvA
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
23% identity, 93% coverage: 40:550/550 of query aligns to 42:578/581 of P18159
- G162 (= G166) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ I228) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G399) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D415) 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+
25% identity, 92% coverage: 42:549/550 of query aligns to 5:455/455 of 1wqaA
- active site: R11 (= R48), S101 (= S150), H102 (= H151), K111 (= K160), D243 (= D308), D245 (= D310), D247 (= D312), R248 (= R313), G330 (= G399), R340 (≠ K414)
- binding magnesium ion: S101 (= S150), D243 (= D308), D245 (= D310), D247 (= D312)
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
26% identity, 88% coverage: 43:525/550 of query aligns to 16:510/553 of 7pjcB
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 77% coverage: 43:463/550 of query aligns to 16:432/554 of O74374
- T111 (= T148) modified: Phosphothreonine
- S113 (= S150) modified: Phosphoserine
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
25% identity, 75% coverage: 43:454/550 of query aligns to 19:429/560 of Q9VUY9
- K28 (≠ G54) natural variant: K -> N
- T36 (≠ I61) natural variant: T -> M
- S116 (= S150) modified: Phosphoserine
- E351 (≠ K370) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
- 17 natural variant: K -> Q
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
25% identity, 75% coverage: 43:454/550 of query aligns to 21:450/571 of 1kfqA
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
25% identity, 75% coverage: 43:454/550 of query aligns to 20:449/570 of 1kfiA
- active site: S124 (= S150), H125 (= H151), D306 (≠ P319), D308 (= D325), D310 (≠ N327), R311 (≠ H328), K403 (= K414)
- binding sulfate ion: S124 (= S150), H125 (= H151), D310 (≠ N327), R311 (≠ H328)
- binding zinc ion: D306 (≠ P319), D308 (= D325), D310 (≠ N327)
Sites not aligning to the query:
3pmgA Structure of rabbit muscle phosphoglucomutase at 2.4 angstroms resolution. Use of freezing point depressant and reduced temperature to enhance diffractivity (see paper)
24% identity, 92% coverage: 43:549/550 of query aligns to 17:540/561 of 3pmgA
- active site: R22 (vs. gap), S116 (= S150), H117 (= H151), K129 (= K160), D287 (= D308), D289 (= D310), D291 (= D312), R292 (= R313), G379 (= G399), K388 (= K414)
- binding magnesium ion: S116 (= S150), D287 (= D308), D289 (= D310), D291 (= D312)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
24% identity, 92% coverage: 43:549/550 of query aligns to 17:540/561 of 1c4gA
- active site: R22 (vs. gap), S116 (= S150), H117 (= H151), K129 (= K160), D287 (= D308), D289 (= D310), D291 (= D312), R292 (= R313), G379 (= G399), K388 (= K414)
- binding cobalt (ii) ion: S116 (= S150), D287 (= D308), D289 (= D310), D291 (= D312)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (vs. gap), S116 (= S150), H117 (= H151), K129 (= K160), R292 (= R313), E375 (= E395), S377 (= S397), K388 (= K414), R514 (≠ K521)
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
24% identity, 92% coverage: 43:549/550 of query aligns to 17:540/561 of 1c47A
- active site: R22 (vs. gap), S116 (= S150), H117 (= H151), K129 (= K160), D287 (= D308), D289 (= D310), D291 (= D312), R292 (= R313), G379 (= G399), K388 (= K414)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (vs. gap), S116 (= S150), D291 (= D312), R292 (= R313), E375 (= E395), K388 (= K414)
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
25% identity, 92% coverage: 43:549/550 of query aligns to 18:541/562 of P00949
- R23 (vs. gap) binding
- S117 (= S150) active site, Phosphoserine intermediate; binding ; binding via phosphate group; modified: Phosphoserine
- D288 (= D308) binding
- D290 (= D310) binding
- D292 (= D312) binding ; binding
- R293 (= R313) binding
- T357 (≠ V376) binding
- E376 (= E395) binding
- S378 (= S397) binding
- K389 (= K414) binding
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
27% identity, 83% coverage: 81:535/550 of query aligns to 28:529/565 of 4qg5A
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
23% identity, 85% coverage: 81:549/550 of query aligns to 70:552/573 of 6snoA
- active site: S130 (= S150), H131 (= H151), K143 (= K160), D301 (= D308), D303 (= D310), D305 (= D312), R306 (= R313), G393 (= G399)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S150), E389 (= E395), S391 (= S397), R514 (= R512), S516 (= S514), G517 (= G515), T518 (= T516), R526 (≠ K521)
- binding zinc ion: S130 (= S150), D301 (= D308), D303 (= D310), D305 (= D312)
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, 92% coverage: 43:549/550 of query aligns to 18:541/562 of P36871
- T19 (= T44) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ D59) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (≠ W62) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D86) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ Y92) 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 (= T148) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S150) 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 (≠ G236) 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 (= D284) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D308) binding
- D290 (= D310) binding
- G291 (≠ Y311) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D312) binding
- G330 (≠ A349) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E396) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D413) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (≠ F445) 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 (≠ A485) modified: Phosphothreonine; by PAK1
- L516 (≠ I522) to P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
23% identity, 92% coverage: 43:549/550 of query aligns to 31:545/566 of 6snqA
- active site: R36 (= R48), S130 (= S150), H131 (= H151), K143 (= K160), D301 (= D308), D303 (= D310), D305 (= D312), R306 (= R313), G393 (= G399)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S150), T370 (≠ V376), G371 (= G377), E389 (= E395), S391 (= S397), R512 (= R512), S514 (= S514), R519 (≠ K521)
- binding zinc ion: S130 (= S150), D301 (= D308), D303 (= D310), D305 (= D312)
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
24% identity, 75% coverage: 43:454/550 of query aligns to 27:438/572 of 6y8yA
Sites not aligning to the query:
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
24% identity, 74% coverage: 43:449/550 of query aligns to 19:425/499 of 7s0wB
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
24% identity, 57% coverage: 144:454/550 of query aligns to 111:429/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S117 (= S150), H118 (= H151), K130 (= K160), D286 (= D312), R287 (= R313), T350 (≠ V376), E369 (= E395), S371 (= S397), K382 (= K414)
- binding magnesium ion: S117 (= S150), D282 (= D308), D284 (= D310), D286 (= D312)
Sites not aligning to the query:
Query Sequence
>201480 FitnessBrowser__MR1:201480
MAIHQRAGQIASQMDLVNIPKLMSHYYSIKPNMDAAEQRVTFGTSGHRGTAFQGSFNQDH
IWAITQAVVDYRQSVNIEGPLFLGIDTHALSYAAYVSAIEVLAANKVTVYIQQNDGFTPT
PVVSHAIICANHAAAQNGALLSDGLIITPSHNPPQDGGIKYNPPHGGPAEGNITAWIESR
ANDYLRAALKGVNKLAYADALASGYVHAIDLITPYVADLENVVDMHAIAKANLKLGVDPL
GGSGIHYWAPIAKHYGIDITLVNDKVDPSFSFMSLDKDGKIRMDCSSPYAMAGLLAHKES
FDLCVGNDPDYDRHGIVCPGTGLMDPNHYLAVAIDYLLTHRPEWSDSLAIGKTLVSSALI
DKICVFHGKKLLEVPVGFKWFVDGLAEATIAFGGEESAGAAFLRRDGTTWCTDKDGFILV
LLAAEMLAVTGKTPGQRHQELVAQFGQSFYKRIDSPISLENKAKFAKLNADTLNATMLAG
EKIEAVLTHAPGNNASIGGIKVTTTNGWFAARPSGTEALFKIYGESFISEQHLAEIIKDA
QALIDKALSA
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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