SitesBLAST
Comparing AZOBR_RS02670 FitnessBrowser__azobra:AZOBR_RS02670 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)
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
53% identity, 99% coverage: 4:543/543 of query aligns to 18:573/573 of 6snoA
- active site: R36 (= R22), S130 (= S113), H131 (= H114), K143 (= K126), D301 (= D277), D303 (= D279), D305 (= D281), R306 (= R282), G393 (= G367)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S113), E389 (= E363), S391 (= S365), R514 (= R484), S516 (= S486), G517 (= G487), T518 (= T488), R526 (= R496)
- binding zinc ion: S130 (= S113), D301 (= D277), D303 (= D279), D305 (= D281)
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
53% identity, 99% coverage: 4:543/543 of query aligns to 5:562/562 of P36871
- T19 (= T18) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (= N36) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (= Q39) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D58) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ R64) 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 (≠ S111) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S113) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (= G117) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ V209) 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 (= D251) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D277) binding
- D290 (= D279) binding
- G291 (= G280) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D281) binding
- G330 (= G317) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E364) to K: in CDG1T; decreases strongly solubility
- E388 (= E375) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
- Y420 (= Y407) 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 (= T448) modified: Phosphothreonine; by PAK1
- L516 (≠ V497) to P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
53% identity, 99% coverage: 4:543/543 of query aligns to 18:566/566 of 6snqA
- active site: R36 (= R22), S130 (= S113), H131 (= H114), K143 (= K126), D301 (= D277), D303 (= D279), D305 (= D281), R306 (= R282), G393 (= G367)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S113), T370 (= T344), G371 (= G345), E389 (= E363), S391 (= S365), R512 (= R484), S514 (= S491), R519 (= R496)
- binding zinc ion: S130 (= S113), D301 (= D277), D303 (= D279), D305 (= D281)
3pmgA Structure of rabbit muscle phosphoglucomutase at 2.4 angstroms resolution. Use of freezing point depressant and reduced temperature to enhance diffractivity (see paper)
52% identity, 99% coverage: 4:543/543 of query aligns to 4:561/561 of 3pmgA
- active site: R22 (= R22), S116 (= S113), H117 (= H114), K129 (= K126), D287 (= D277), D289 (= D279), D291 (= D281), R292 (= R282), G379 (= G367), K388 (= K376)
- binding magnesium ion: S116 (= S113), D287 (= D277), D289 (= D279), D291 (= D281)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
52% identity, 99% coverage: 4:543/543 of query aligns to 4:561/561 of 1c4gA
- active site: R22 (= R22), S116 (= S113), H117 (= H114), K129 (= K126), D287 (= D277), D289 (= D279), D291 (= D281), R292 (= R282), G379 (= G367), K388 (= K376)
- binding cobalt (ii) ion: S116 (= S113), D287 (= D277), D289 (= D279), D291 (= D281)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (= R22), S116 (= S113), H117 (= H114), K129 (= K126), R292 (= R282), E375 (= E363), S377 (= S365), K388 (= K376), R514 (= R496)
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
52% identity, 99% coverage: 4:543/543 of query aligns to 4:561/561 of 1c47A
- active site: R22 (= R22), S116 (= S113), H117 (= H114), K129 (= K126), D287 (= D277), D289 (= D279), D291 (= D281), R292 (= R282), G379 (= G367), K388 (= K376)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (= R22), S116 (= S113), D291 (= D281), R292 (= R282), E375 (= E363), K388 (= K376)
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
52% identity, 99% coverage: 4:543/543 of query aligns to 5:562/562 of P00949
- R23 (= R22) binding
- S117 (= S113) active site, Phosphoserine intermediate; binding ; binding via phosphate group; modified: Phosphoserine
- D288 (= D277) binding
- D290 (= D279) binding
- D292 (= D281) binding ; binding
- R293 (= R282) binding
- T357 (= T344) binding
- E376 (= E363) binding
- S378 (= S365) binding
- K389 (= K376) binding
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
52% identity, 99% coverage: 4:543/543 of query aligns to 6:559/559 of 5jn5A
- active site: R24 (= R22), S118 (= S113), H119 (= H114), K131 (= K126), D289 (= D277), D291 (= D279), D293 (= D281), R294 (= R282), G381 (= G367), K390 (= K376)
- binding calcium ion: S118 (= S113), D289 (= D277), D291 (= D279), D293 (= D281)
O74374 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
52% identity, 99% coverage: 5:543/543 of query aligns to 4:554/554 of O74374
- T111 (≠ S111) modified: Phosphothreonine
- S113 (= S113) modified: Phosphoserine
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
51% identity, 99% coverage: 8:543/543 of query aligns to 10:560/560 of Q9VUY9
- K17 (= K15) natural variant: K -> Q
- K28 (= K26) natural variant: K -> N
- T36 (≠ L34) natural variant: T -> M
- S116 (= S113) modified: Phosphoserine
- E351 (≠ S338) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
50% identity, 99% coverage: 5:543/543 of query aligns to 8:558/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: T21 (= T18), R25 (= R22), S117 (= S113), H118 (= H114), K130 (= K126), D286 (= D281), R287 (= R282), T350 (= T344), E369 (= E363), S371 (= S365), K382 (= K376), R499 (= R484), S501 (= S486), G502 (= G487), T503 (= T488), R511 (= R496)
- binding magnesium ion: S117 (= S113), D282 (= D277), D284 (= D279), D286 (= D281)
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
50% identity, 99% coverage: 4:543/543 of query aligns to 14:572/572 of 6y8yA
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
48% identity, 99% coverage: 5:543/543 of query aligns to 4:553/553 of 7pjcB
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
51% identity, 96% coverage: 4:523/543 of query aligns to 6:499/499 of 7s0wB
1kfiA Crystal structure of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase) from paramecium (see paper)
49% identity, 100% coverage: 3:543/543 of query aligns to 6:570/570 of 1kfiA
- active site: S124 (= S113), H125 (= H114), D306 (= D277), D308 (= D279), D310 (= D281), R311 (= R282), K403 (= K376)
- binding sulfate ion: S124 (= S113), H125 (= H114), D310 (= D281), R311 (= R282), R513 (= R484), S515 (= S486), R525 (= R496)
- binding zinc ion: D306 (= D277), D308 (= D279), D310 (= D281)
1kfqA Crystal structure of exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutse) from paramecium. Open form (see paper)
49% identity, 100% coverage: 3:543/543 of query aligns to 7:571/571 of 1kfqA
4qg5A Crystal structure of phosphoglucomutase from leishmania major at 3.5 angstrom resolution
48% identity, 95% coverage: 28:543/543 of query aligns to 1:565/565 of 4qg5A
2fuvA Phosphoglucomutase from salmonella typhimurium.
29% identity, 91% coverage: 15:509/543 of query aligns to 40:526/545 of 2fuvA
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
28% identity, 62% coverage: 88:426/543 of query aligns to 76:392/455 of 1wqaA
- active site: S101 (= S113), H102 (= H114), K111 (= K126), D243 (= D277), D245 (= D279), D247 (= D281), R248 (= R282), G330 (= G367), R340 (≠ K376)
- binding magnesium ion: S101 (= S113), D243 (= D277), D245 (= D279), D247 (= D281)
Sites not aligning to the query:
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 80% coverage: 53:488/543 of query aligns to 88:539/581 of P18159
- G162 (= G132) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ V216) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G367) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D377) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
Query Sequence
>AZOBR_RS02670 FitnessBrowser__azobra:AZOBR_RS02670
VVPVTCPTTPFDGQKPGTSGLRKAVKVFEQPRYLENFVQSIFDCVDGLSGATLVIGGDGR
YHNRTAVQTILRMAAANGVARAVVGRGGILSTPAASCVIRKRGAIGGVILSASHNPGGPD
GDFGIKFNAANGGPAPESMTDAFFARSKAITEYKTLESPDLDLDRLGETALGGIAVEVID
PVADYAELMESLFDMAAIRKLFASGFRMVFDAMHAVTGPYATEILERRLGAPAGTVINGT
PLEDFGGHHPDPNLAHAEELVGRLFGPDAPDFGAASDGDGDRNMILGRNVFVSPSDSLAV
LAANATHVPAFKGGLAGVARSMPTSRAVDRVAAKLGISCYETPTGWKFFGTLLDAGRINL
CGEESFGTGADHVREKDGLWAVLMWLNVLAARGLSVAELMAEHWGTYGRTYYGRHDYEAI
PQEAADALIAELRGTLSSLAGTDLGGRTVAAADEFAYTDPVDGSRSERQGLRVGFEDGSR
IVYRLSGTGTSGATLRVYFERYEPVGGEHGLDAPVALKPLADLAAELAGIERHTGRTKPD
VAT
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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