SitesBLAST
Comparing PP_3578 FitnessBrowser__Putida:PP_3578 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2fuvA Phosphoglucomutase from salmonella typhimurium.
60% identity, 99% coverage: 7:544/545 of query aligns to 6:542/545 of 2fuvA
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
28% identity, 68% coverage: 81:450/545 of query aligns to 56:429/560 of Q9VUY9
- S116 (= S147) modified: Phosphoserine
- E351 (≠ D366) 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
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 60% coverage: 81:407/545 of query aligns to 53:383/554 of O74374
- T111 (= T145) modified: Phosphothreonine
- S113 (= S147) modified: Phosphoserine
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
27% identity, 85% coverage: 81:541/545 of query aligns to 53:536/553 of 7pjcB
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
24% identity, 88% coverage: 42:522/545 of query aligns to 5:433/455 of 1wqaA
- active site: R11 (= R48), S101 (= S147), H102 (= H148), K111 (= K157), D243 (= D305), D245 (= D307), D247 (= D309), R248 (= R310), G330 (= G395), R340 (≠ K410)
- binding magnesium ion: S101 (= S147), D243 (= D305), D245 (= D307), D247 (= D309)
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
27% identity, 93% coverage: 40:544/545 of query aligns to 42:576/581 of P18159
- G162 (= G163) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ A228) 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.
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
25% identity, 80% coverage: 43:479/545 of query aligns to 20:460/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: T21 (= T44), R25 (= R48), S117 (= S147), H118 (= H148), K130 (= K157), D286 (= D309), R287 (= R310), T350 (≠ V372), E369 (= E391), S371 (= S393), K382 (≠ D402)
- binding magnesium ion: S117 (= S147), D282 (= D305), D284 (= D307), D286 (= D309)
Sites not aligning to the query:
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 77% coverage: 43:460/545 of query aligns to 31:455/566 of 6snqA
- active site: R36 (= R48), S130 (= S147), H131 (= H148), K143 (= K157), D301 (= D305), D303 (= D307), D305 (= D309), R306 (= R310), G393 (= G395)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S147), T370 (≠ V372), G371 (= G373), E389 (= E391), S391 (= S393)
- binding zinc ion: S130 (= S147), D301 (= D305), D303 (= D307), D305 (= D309)
Sites not aligning to the query:
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 77% coverage: 43:460/545 of query aligns to 31:455/573 of 6snoA
- active site: R36 (= R48), S130 (= S147), H131 (= H148), K143 (= K157), D301 (= D305), D303 (= D307), D305 (= D309), R306 (= R310), G393 (= G395)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S147), E389 (= E391), S391 (= S393)
- binding zinc ion: S130 (= S147), D301 (= D305), D303 (= D307), D305 (= D309)
Sites not aligning to the query:
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
26% identity, 75% coverage: 43:450/545 of query aligns to 18:429/562 of P00949
- R23 (= R48) binding
- S117 (= S147) active site, Phosphoserine intermediate; binding ; binding via phosphate group; modified: Phosphoserine
- D288 (= D305) binding
- D290 (= D307) binding
- D292 (= D309) binding ; binding
- R293 (= R310) 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)
26% identity, 75% coverage: 43:450/545 of query aligns to 17:428/561 of 3pmgA
- active site: R22 (= R48), S116 (= S147), H117 (= H148), K129 (= K157), D287 (= D305), D289 (= D307), D291 (= D309), R292 (= R310), G379 (= G395), K388 (= K410)
- binding magnesium ion: S116 (= S147), D287 (= D305), D289 (= D307), D291 (= D309)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
26% identity, 75% coverage: 43:450/545 of query aligns to 17:428/561 of 1c4gA
- active site: R22 (= R48), S116 (= S147), H117 (= H148), K129 (= K157), D287 (= D305), D289 (= D307), D291 (= D309), R292 (= R310), G379 (= G395), K388 (= K410)
- binding cobalt (ii) ion: S116 (= S147), D287 (= D305), D289 (= D307), D291 (= D309)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (= R48), S116 (= S147), H117 (= H148), K129 (= K157), R292 (= R310), E375 (= E391), S377 (= S393), K388 (= K410)
Sites not aligning to the query:
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
26% identity, 75% coverage: 43:450/545 of query aligns to 17:428/561 of 1c47A
- active site: R22 (= R48), S116 (= S147), H117 (= H148), K129 (= K157), D287 (= D305), D289 (= D307), D291 (= D309), R292 (= R310), G379 (= G395), K388 (= K410)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (= R48), S116 (= S147), D291 (= D309), R292 (= R310), E375 (= E391), K388 (= K410)
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
27% identity, 67% coverage: 43:407/545 of query aligns to 20:408/570 of 1kfiA
- active site: S124 (= S147), H125 (= H148), D306 (= D305), D308 (= D307), D310 (= D309), R311 (= R310), K403 (≠ D402)
- binding sulfate ion: S124 (= S147), H125 (= H148), D310 (= D309), R311 (= R310)
- binding zinc ion: D306 (= D305), D308 (= D307), D310 (= D309)
Sites not aligning to the query:
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
27% identity, 67% coverage: 43:407/545 of query aligns to 21:409/571 of 1kfqA
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
28% identity, 62% coverage: 70:408/545 of query aligns to 18:392/565 of 4qg5A
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
26% identity, 71% coverage: 72:460/545 of query aligns to 52:442/562 of P36871
- D62 (= D86) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ A92) 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 (= T145) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S147) 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 (≠ G233) 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 (= D281) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D305) binding
- D290 (= D307) binding
- G291 (≠ H308) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D309) 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 (≠ L441) 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:
- 19 T → A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- 38 N → Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- 41 Q → R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- 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)
26% identity, 79% coverage: 31:463/545 of query aligns to 10:452/572 of 6y8yA
Sites not aligning to the query:
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
26% identity, 71% coverage: 72:460/545 of query aligns to 53:443/559 of 5jn5A
- active site: S118 (= S147), H119 (= H148), K131 (= K157), D289 (= D305), D291 (= D307), D293 (= D309), R294 (= R310), G381 (= G395), K390 (= K410)
- binding calcium ion: S118 (= S147), D289 (= D305), D291 (= D307), D293 (= D309)
Sites not aligning to the query:
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
25% identity, 70% coverage: 72:453/545 of query aligns to 53:433/499 of 7s0wB
Query Sequence
>PP_3578 FitnessBrowser__Putida:PP_3578
MTLSPLAGKPAPASVLVDIPRLLTAYYTGRPDATVAAQRVAFGTSGHRGSSLELSFNEYH
VLAISQAICLYRQEKGIDGPLFIGADTHALSAPATASALEVLAANGVQVMLSKDDEYTPT
PAVSHAILCHNRGRTQGLADGIVITPSHNPPQSGGFKYNPPNGGPADSDVTKWIEGKANE
LLAANLAGVKRMDHAQALQAPTTHRHDYVSNYVADLENVIDFDVIRGAGLRLGVDPLGGA
GVRYWSAIAKHYQLDLEVVNTEVDPTFRFMTVDWDGQIRMDPSSPYAMQGLIGLRERFDV
AFACDPDHDRHGIVTPDGLLQPNNYLAVAIDYLFRHRPQWRSDAAVGKTVVSSGLIDRVT
QRLGRDLYEVPVGFKFFAQGLFDGSLGFGGEESAGASFLRRDGSVWATDKDGLIPALLAA
EMTARTGRNPSQAYADLTEALGKPFATRVEAKADARQKALLSKLAPEQVKSTELAGEPIV
QILSHAPGNGQAIGGLKVMTANGWFAARPSGTEDIYKIYAESFIDEAHLQRLVEEAQVLV
DEAIA
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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