SitesBLAST
Comparing WP_061939910.1 NCBI__GCF_001584185.1:WP_061939910.1 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.
57% identity, 97% coverage: 7:545/556 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, 85% coverage: 81:551/556 of query aligns to 56:548/560 of Q9VUY9
- S116 (= S147) modified: Phosphoserine
- E351 (≠ R367) 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
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
26% identity, 87% coverage: 40:520/556 of query aligns to 42:546/581 of P18159
- G162 (= G163) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ A240) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G396) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D412) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
24% identity, 90% coverage: 43:541/556 of query aligns to 31:547/573 of 6snoA
- active site: R36 (= R48), S130 (= S147), H131 (= H148), K143 (= K157), D301 (= D305), D303 (= D307), D305 (= D309), R306 (= R310), G393 (= G396)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S147), E389 (= E392), S391 (= S394), R514 (= R509), S516 (= S511), G517 (= G512), T518 (= T513), R526 (≠ K518)
- binding zinc ion: S130 (= S147), D301 (= D305), D303 (= D307), D305 (= D309)
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
25% identity, 76% coverage: 43:465/556 of query aligns to 31:461/566 of 6snqA
- active site: R36 (= R48), S130 (= S147), H131 (= H148), K143 (= K157), D301 (= D305), D303 (= D307), D305 (= D309), R306 (= R310), G393 (= G396)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S147), T370 (≠ A373), G371 (= G374), E389 (= E392), S391 (= S394)
- binding zinc ion: S130 (= S147), D301 (= D305), D303 (= D307), D305 (= D309)
Sites not aligning to the query:
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
25% identity, 93% coverage: 31:546/556 of query aligns to 10:551/572 of 6y8yA
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 62% coverage: 81:425/556 of query aligns to 53:392/554 of O74374
- T111 (= T145) modified: Phosphothreonine
- S113 (= S147) modified: Phosphoserine
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, 76% coverage: 43:465/556 of query aligns to 17:447/561 of 3pmgA
- active site: R22 (vs. gap), S116 (= S147), H117 (= H148), K129 (= K157), D287 (= D305), D289 (= D307), D291 (= D309), R292 (= R310), G379 (= G396), K388 (= K411)
- binding magnesium ion: S116 (= S147), D287 (= D305), D289 (= D307), D291 (= D309)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
25% identity, 76% coverage: 43:465/556 of query aligns to 17:447/561 of 1c4gA
- active site: R22 (vs. gap), S116 (= S147), H117 (= H148), K129 (= K157), D287 (= D305), D289 (= D307), D291 (= D309), R292 (= R310), G379 (= G396), K388 (= K411)
- binding cobalt (ii) ion: S116 (= S147), D287 (= D305), D289 (= D307), D291 (= D309)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (vs. gap), S116 (= S147), H117 (= H148), K129 (= K157), R292 (= R310), E375 (= E392), S377 (= S394), K388 (= K411)
Sites not aligning to the query:
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
25% identity, 76% coverage: 43:465/556 of query aligns to 17:447/561 of 1c47A
- active site: R22 (vs. gap), S116 (= S147), H117 (= H148), K129 (= K157), D287 (= D305), D289 (= D307), D291 (= D309), R292 (= R310), G379 (= G396), K388 (= K411)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (vs. gap), S116 (= S147), D291 (= D309), R292 (= R310), E375 (= E392), K388 (= K411)
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
25% identity, 76% coverage: 43:465/556 of query aligns to 18:448/562 of P00949
- R23 (vs. gap) binding alpha-D-glucose 1,6-bisphosphate
- S117 (= S147) active site, Phosphoserine intermediate; binding alpha-D-glucose 1,6-bisphosphate; binding via phosphate group; modified: Phosphoserine
- D288 (= D305) binding Mg(2+)
- D290 (= D307) binding Mg(2+)
- D292 (= D309) binding alpha-D-glucose 1,6-bisphosphate; binding Mg(2+)
- R293 (= R310) binding alpha-D-glucose 1,6-bisphosphate
- T357 (≠ A373) binding alpha-D-glucose 1,6-bisphosphate
- E376 (= E392) binding alpha-D-glucose 1,6-bisphosphate
- S378 (= S394) binding alpha-D-glucose 1,6-bisphosphate
- K389 (= K411) binding alpha-D-glucose 1,6-bisphosphate
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
28% identity, 60% coverage: 81:414/556 of query aligns to 53:384/553 of 7pjcB
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
25% identity, 76% coverage: 43:465/556 of query aligns to 18:448/562 of P36871
- T19 (= T44) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ V61) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (≠ S65) 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 (≠ I92) 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 Mg(2+)
- D290 (= D307) binding Mg(2+)
- G291 (≠ H308) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D309) binding Mg(2+)
- G330 (= G346) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E393) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D410) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (≠ L442) 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
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
25% identity, 76% coverage: 43:465/556 of query aligns to 19:449/559 of 5jn5A
- active site: R24 (vs. gap), S118 (= S147), H119 (= H148), K131 (= K157), D289 (= D305), D291 (= D307), D293 (= D309), R294 (= R310), G381 (= G396), K390 (= K411)
- binding calcium ion: S118 (= S147), D289 (= D305), D291 (= D307), D293 (= D309)
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
25% identity, 69% coverage: 43:425/556 of query aligns to 19:404/499 of 7s0wB
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
23% identity, 91% coverage: 42:546/556 of query aligns to 5:455/455 of 1wqaA
- active site: R11 (= R48), S101 (= S147), H102 (= H148), K111 (= K157), D243 (= D305), D245 (= D307), D247 (= D309), R248 (= R310), G330 (= G396), R340 (≠ K411)
- binding magnesium ion: S101 (= S147), D243 (= D305), D245 (= D307), D247 (= D309)
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
24% identity, 63% coverage: 81:430/556 of query aligns to 60:423/571 of 1kfqA
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
24% identity, 63% coverage: 81:430/556 of query aligns to 59:422/570 of 1kfiA
- active site: S124 (= S147), H125 (= H148), D306 (= D305), D308 (= D307), D310 (= D309), R311 (= R310), K403 (= K411)
- 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:
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
27% identity, 62% coverage: 81:426/556 of query aligns to 28:401/565 of 4qg5A
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
26% identity, 65% coverage: 56:414/556 of query aligns to 36:385/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S117 (= S147), H118 (= H148), K130 (= K157), D286 (= D309), R287 (= R310), T350 (≠ A373), E369 (= E392), S371 (= S394), K382 (= K411)
- binding magnesium ion: S117 (= S147), D282 (= D305), D284 (= D307), D286 (= D309)
Sites not aligning to the query:
Query Sequence
>WP_061939910.1 NCBI__GCF_001584185.1:WP_061939910.1
MKISPLAGKPAPSALLVDVPKLVSAYYTNVPDPEVAEQRVAFGTSGHRGSSFDCSFNEAH
VLAISQAICAYRSKQGISGPLFIGIDTHALSIAACASAVEVLAANGVDIMLAEGDEYTPT
PAVSHAIIKYNRGRQSGLADGIVITPSHNPPEDGGVKYNPPNGGAADTDITGWIEAAANA
LLRAGLKDVKRMPLQKALRLASTHRYDYLNTYVDELDQVIDMALIRDAGVHLGVDPLGGA
GVHYWQRISERYQLNLSVVSEEVDPTFRFMTVDWDGRIRMDPSSSYAMQRLLGMKDRYDI
AFACDTDHDRHGIVTRSAGLLPANHYLAVMIDYLFQHRSQWPQAAGIGKTVVSSQIIDRI
ATRLKRRLYEVPAGFKWFAPGLSDGSLGFGGEESAGATFQRLDGSVWTTDKDGLVPALLA
AEITARGGRDPGEVYRRLASELGDPLSTRVEASATPAQKKMLAALSPQQIQSTELAGEKI
QDIISKAPGNDAAIGGVRVTTAGGWFAARPSGTEDIYKIYAESFHGAEHLQRIVQEAQAI
VDAALAATPTPAAAAK
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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