SitesBLAST
Comparing HSERO_RS13360 FitnessBrowser__HerbieS:HSERO_RS13360 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: 8:547/549 of query aligns to 6:543/545 of 2fuvA
Q9VUY9 Phosphoglucomutase; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
27% identity, 73% coverage: 44:442/549 of query aligns to 19:415/560 of Q9VUY9
- K28 (≠ N53) natural variant: K -> N
- T36 (≠ V62) natural variant: T -> M
- S116 (= S148) modified: Phosphoserine
- E351 (≠ K368) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
- 17 natural variant: K -> Q
6snqA Crystal structures of human pgm1 isoform 2 (see paper)
26% identity, 68% coverage: 44:419/549 of query aligns to 31:409/566 of 6snqA
- active site: R36 (= R49), S130 (= S148), H131 (= H149), K143 (= K158), D301 (= D306), D303 (= D308), D305 (= D310), R306 (= R311), G393 (= G397)
- binding 6-O-phosphono-alpha-D-glucopyranose: S130 (= S148), T370 (≠ V374), G371 (= G375), E389 (= E393), S391 (= S395)
- binding zinc ion: S130 (= S148), D301 (= D306), D303 (= D308), D305 (= D310)
Sites not aligning to the query:
6snoA Crystal structures of human pgm1 isoform 2 (see paper)
26% identity, 68% coverage: 44:419/549 of query aligns to 31:409/573 of 6snoA
- active site: R36 (= R49), S130 (= S148), H131 (= H149), K143 (= K158), D301 (= D306), D303 (= D308), D305 (= D310), R306 (= R311), G393 (= G397)
- binding 1-O-phosphono-alpha-D-glucopyranose: S130 (= S148), E389 (= E393), S391 (= S395)
- binding zinc ion: S130 (= S148), D301 (= D306), D303 (= D308), D305 (= D310)
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)
26% identity, 73% coverage: 44:444/549 of query aligns to 17:420/561 of 3pmgA
- active site: R22 (= R49), S116 (= S148), H117 (= H149), K129 (= K158), D287 (= D306), D289 (= D308), D291 (= D310), R292 (= R311), G379 (= G397), K388 (= K412)
- binding magnesium ion: S116 (= S148), D287 (= D306), D289 (= D308), D291 (= D310)
1c4gA Phosphoglucomutase vanadate based transition state analog complex
26% identity, 73% coverage: 44:444/549 of query aligns to 17:420/561 of 1c4gA
- active site: R22 (= R49), S116 (= S148), H117 (= H149), K129 (= K158), D287 (= D306), D289 (= D308), D291 (= D310), R292 (= R311), G379 (= G397), K388 (= K412)
- binding cobalt (ii) ion: S116 (= S148), D287 (= D306), D289 (= D308), D291 (= D310)
- binding alpha-d-glucose-1-phosphate-6-vanadate: R22 (= R49), S116 (= S148), H117 (= H149), K129 (= K158), R292 (= R311), E375 (= E393), S377 (= S395), K388 (= K412)
Sites not aligning to the query:
1c47A Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction
26% identity, 73% coverage: 44:444/549 of query aligns to 17:420/561 of 1c47A
- active site: R22 (= R49), S116 (= S148), H117 (= H149), K129 (= K158), D287 (= D306), D289 (= D308), D291 (= D310), R292 (= R311), G379 (= G397), K388 (= K412)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R22 (= R49), S116 (= S148), D291 (= D310), R292 (= R311), E375 (= E393), K388 (= K412)
P00949 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
26% identity, 73% coverage: 44:444/549 of query aligns to 18:421/562 of P00949
- R23 (= R49) binding
- S117 (= S148) active site, Phosphoserine intermediate; binding ; binding via phosphate group; modified: Phosphoserine
- D288 (= D306) binding
- D290 (= D308) binding
- D292 (= D310) binding ; binding
- R293 (= R311) binding
- T357 (≠ V374) binding
- E376 (= E393) binding
- S378 (= S395) binding
- K389 (= K412) binding
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 91% coverage: 41:537/549 of query aligns to 42:566/581 of P18159
- G162 (= G164) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ A241) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G397) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D413) mutation to N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
6y8yA Structure of baltic herring (clupea harengus) phosphoglucomutase 5 (pgm5) with bound glucose-1-phosphate (see paper)
25% identity, 73% coverage: 44:444/549 of query aligns to 27:430/572 of 6y8yA
Sites not aligning to the query:
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
23% identity, 88% coverage: 43:524/549 of query aligns to 5:433/455 of 1wqaA
- active site: R11 (= R49), S101 (= S148), H102 (= H149), K111 (= K158), D243 (= D306), D245 (= D308), D247 (= D310), R248 (= R311), G330 (= G397), R340 (≠ K412)
- binding magnesium ion: S101 (= S148), D243 (= D306), D245 (= D308), D247 (= D310)
P36871 Phosphoglucomutase-1; PGM 1; Glucose phosphomutase 1; EC 5.4.2.2 from Homo sapiens (Human) (see 11 papers)
26% identity, 68% coverage: 44:419/549 of query aligns to 18:396/562 of P36871
- T19 (= T45) to A: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1320810473
- N38 (≠ A64) to Y: in CDG1T; strongly reduces solubility; increases aggregation; dbSNP:rs587777402
- Q41 (= Q67) to R: in CDG1T; reduces solubility; increases aggregation; dbSNP:rs1300651770
- D62 (= D87) to H: in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity; dbSNP:rs587777403
- K68 (≠ E93) 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 (= T146) to A: in CDG1T; reduces mildly phosphoglucomutase activity; dbSNP:rs121918371
- S117 (= S148) active site, Phosphoserine intermediate; binding via phosphate groupe; modified: Phosphoserine
- G121 (≠ P152) to R: in CDG1T; there is 7% enzyme residual phosphoglucomutase activity; dbSNP:rs398122912
- R221 (≠ G234) 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 (= D282) to G: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs1465877146; to Y: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs587777404
- D288 (= D306) binding
- D290 (= D308) binding
- G291 (≠ H309) to R: in CDG1T; strongly reduces phosphoglucomutase activity; dbSNP:rs772768778
- D292 (= D310) binding
- G330 (= G349) to R: in CDG1T; decreases mildly solubility; dbSNP:rs777164338
- E377 (= E394) to K: in CDG1T; decreases strongly solubility
- E388 (≠ D411) to K: in CDG1T; decreases strongly solubility; dbSNP:rs1301021797
Sites not aligning to the query:
- 420 Y → H: in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type; dbSNP:rs11208257
- 467 modified: Phosphothreonine; by PAK1
- 516 L → P: in CDG1T; decreases strongly solubility; dbSNP:rs587777401
7s0wB Crystal structure of the t337m variant of human pgm-1 (see paper)
25% identity, 75% coverage: 44:455/549 of query aligns to 19:433/499 of 7s0wB
5jn5A Crystal structure of the d263y missense variant of human pgm1 (see paper)
25% identity, 68% coverage: 44:419/549 of query aligns to 19:397/559 of 5jn5A
- active site: R24 (= R49), S118 (= S148), H119 (= H149), K131 (= K158), D289 (= D306), D291 (= D308), D293 (= D310), R294 (= R311), G381 (= G397), K390 (= K412)
- binding calcium ion: S118 (= S148), D289 (= D306), D291 (= D308), D293 (= D310)
7pjcB The structure of candida albicans phosphoglucomutase with isothiazolone modification on cys359
26% identity, 68% coverage: 44:419/549 of query aligns to 16:388/553 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, 69% coverage: 44:420/549 of query aligns to 16:386/554 of O74374
- T111 (= T146) modified: Phosphothreonine
- S113 (= S148) modified: Phosphoserine
Q96G03 Phosphopentomutase; Glucose phosphomutase 2; Phosphodeoxyribomutase; Phosphoglucomutase-2; EC 5.4.2.7; EC 5.4.2.2 from Homo sapiens (Human) (see 2 papers)
22% identity, 70% coverage: 40:426/549 of query aligns to 54:452/612 of Q96G03
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 10 G → D: in dbSNP:rs17856324
7p5oB Crystal structure of aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
24% identity, 68% coverage: 44:419/549 of query aligns to 20:389/558 of 7p5oB
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: T21 (= T45), R25 (= R49), S117 (= S148), H118 (= H149), K130 (= K158), D286 (= D310), R287 (= R311), T350 (≠ V374), E369 (= E393), S371 (= S395), K382 (= K412)
- binding magnesium ion: S117 (= S148), D282 (= D306), D284 (= D308), D286 (= D310)
Sites not aligning to the query:
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
24% identity, 74% coverage: 143:549/549 of query aligns to 104:450/458 of 3uw2A
Sites not aligning to the query:
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
24% identity, 71% coverage: 38:427/549 of query aligns to 2:354/445 of P31120
- S100 (≠ T146) mutation to A: 2% of wild-type activity.; mutation to T: 20-fold increase in the non-specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated).
- S102 (= S148) active site, Phosphoserine intermediate; modified: Phosphoserine; by autocatalysis; mutation to A: Loss of activity in the absence or presence of glucosamine-1,6-diP.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>HSERO_RS13360 FitnessBrowser__HerbieS:HSERO_RS13360
MSSVNPLAGQRAAPSALVDLPVLVSNYYSLRPDVAEASHRVAFGTSGHRGNANAHSFNEW
HVLAITQAICDYRKEQGFKGPLFLGIDTHALSEPAWHSALEVLAANEVVTMLAEGSPYAP
TPAVSHAILTHNRVHRDALADGIVVTPSHNPPDNGGFKYNMPNGGPSDSNVTGWIEQRAN
AYLEQQLQGVRRVSFEKALKADTTRRYDYLDNYVSDLPNIIDLAAISGANVKIGVDPLGG
AGLHYWSAIADRYKLNLEVVNTEVDATFRFVPLDWDAQIRMDPSSPHAMSELIALKDRFD
VAMACDTDHDRHGIVAKSRGLMPANDYLSVAVYYLFRHRPAWRADAAIGKTLVSSQMINR
VAKHLERKLLEMPVGFKWFVDGLYDGSLAFGCEESAGASFVRFDGQPWSTDKDGITAALL
AAEMTARTGNDPGQIYEDLTHQLGAPLNGRKEAAATPEQKARLSKLSPQDVSSTELAGEP
IREVLTTAPANGKPFGGLKIVTDNGWFAARPSGTESIYKIYGESFRDQAHLDKIFAEAQD
IVTRALQAS
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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