SitesBLAST
Comparing WP_035130453.1 NCBI__GCF_000769915.1:WP_035130453.1 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)
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
47% identity, 93% coverage: 38:572/575 of query aligns to 34:575/581 of P18159
- G162 (= G165) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (= T238) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G402) 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.
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)
33% identity, 92% coverage: 14:541/575 of query aligns to 22:569/612 of Q96G03
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 10 G → D: in dbSNP:rs17856324
O74478 Probable phosphoribomutase; PRM; Phosphoglucomutase 3 homolog; PGM 3 homolog; EC 5.4.2.7 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 99% coverage: 3:571/575 of query aligns to 4:586/587 of O74478
- S149 (= S149) modified: Phosphoserine
Q03262 Phosphoribomutase; PRM; Phosphoglucomutase 3; PGM 3; EC 5.4.2.7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 78% coverage: 3:452/575 of query aligns to 9:483/622 of Q03262
- S158 (= S149) mutation to T: Loss of function.
- P326 (= P302) mutation to G: No effect.
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
25% identity, 86% coverage: 48:541/575 of query aligns to 5:430/455 of 1wqaA
- active site: R11 (= R54), S101 (= S149), H102 (= H150), K111 (= K159), D243 (= D301), D245 (= D303), D247 (= D305), R248 (= R306), G330 (= G402), R340 (≠ K412)
- binding magnesium ion: S101 (= S149), D243 (= D301), D245 (= D303), D247 (= D305)
2fuvA Phosphoglucomutase from salmonella typhimurium.
25% identity, 86% coverage: 46:541/575 of query aligns to 39:517/545 of 2fuvA
P26276 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 10 papers)
25% identity, 71% coverage: 30:437/575 of query aligns to 1:365/463 of P26276
- M1 (= M30) modified: Initiator methionine, Removed
- R15 (≠ K44) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ L46) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R54) mutation to A: No phosphoglucomutase activity.
- S108 (= S149) binding via phosphate group; modified: Phosphoserine; mutation S->A,V: About 5% activity, still subject to substrate inhibition and requires G1,6P as an activator; phosphorylation occurs at a different site.; mutation to C: KM for G1P unchanged, kcat decreases 24-fold; G1,6P stimulates reaction by 2-3 orders of magnitude. No stable protein phosphorylation detected, altered ligation of metal residue.
- N110 (= N151) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D301) binding Mg(2+)
- D244 (= D303) binding Mg(2+)
- D246 (= D305) binding Mg(2+)
- R247 (= R306) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q325) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ V355) binding alpha-D-glucose 1-phosphate
- H308 (≠ F378) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E398) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMS-GH 325:329 (≠ EESFGY 398:403) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (≠ Y403) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
Sites not aligning to the query:
- 368 P→G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- 421 R→C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- 421:425 binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
25% identity, 71% coverage: 30:437/575 of query aligns to 1:365/463 of Q02E40
- S108 (= S149) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 11:357/455 of 2h5aX
- active site: H101 (= H150), D234 (= D301), D236 (= D303), D238 (= D305), R239 (= R306), D332 (vs. gap)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (= T376), G299 (= G377), H300 (≠ F378), E317 (= E398), S319 (= S400), H321 (≠ Y403)
- binding zinc ion: S100 (= S149), D234 (= D301), D236 (= D303), D238 (= D305)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 11:357/455 of 2h4lX
- active site: H101 (= H150), D234 (= D301), D236 (= D303), D238 (= D305), R239 (= R306), D332 (vs. gap)
- binding 1-O-phosphono-alpha-D-ribofuranose: R12 (= R54), S100 (= S149), T298 (= T376), E317 (= E398)
- binding zinc ion: S100 (= S149), D234 (= D301), D236 (= D303), D238 (= D305)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 11:357/455 of 2fkfA
- active site: R12 (= R54), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D301), D236 (= D303), D238 (= D305), R239 (= R306), H321 (≠ Y403), D332 (vs. gap)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H150), S319 (= S400)
- binding zinc ion: S100 (= S149), D234 (= D301), D236 (= D303), D238 (= D305)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 11:357/455 of 1pcmX
- active site: R12 (= R54), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D301), D236 (= D303), D238 (= D305), R239 (= R306), H321 (≠ Y403), D332 (vs. gap)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S149), T298 (= T376), G299 (= G377), H300 (≠ F378), E317 (= E398), S319 (= S400), H321 (≠ Y403)
- binding zinc ion: S100 (= S149), D234 (= D301), D236 (= D303), D238 (= D305)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 11:357/455 of 1p5gX
- active site: R12 (= R54), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D301), D236 (= D303), D238 (= D305), R239 (= R306), H321 (≠ Y403), D332 (vs. gap)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S149), K277 (≠ V355), G299 (= G377), H300 (≠ F378), E317 (= E398), S319 (= S400), H321 (≠ Y403)
- binding zinc ion: S100 (= S149), D234 (= D301), D236 (= D303), D238 (= D305)
Sites not aligning to the query:
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 11:357/455 of 1p5dX
- active site: R12 (= R54), S100 (= S149), H101 (= H150), K110 (= K159), D234 (= D301), D236 (= D303), D238 (= D305), R239 (= R306), H321 (≠ Y403), D332 (vs. gap)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S149), R239 (= R306), T298 (= T376), G299 (= G377), H300 (≠ F378), E317 (= E398), S319 (= S400), H321 (≠ Y403)
- binding zinc ion: S100 (= S149), D234 (= D301), D236 (= D303), D238 (= D305)
Sites not aligning to the query:
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 14:360/458 of 1pcjX
- active site: R15 (= R54), S103 (= S149), H104 (= H150), K113 (= K159), D237 (= D301), D239 (= D303), D241 (= D305), R242 (= R306), H324 (≠ Y403), D335 (vs. gap)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S149), T301 (= T376), G302 (= G377), E320 (= E398), S322 (= S400), H324 (≠ Y403)
- binding zinc ion: S103 (= S149), D237 (= D301), D239 (= D303), D241 (= D305)
Sites not aligning to the query:
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
27% identity, 49% coverage: 53:331/575 of query aligns to 15:264/459 of 4il8A
- active site: R16 (= R54), S104 (= S149), H105 (= H150), K114 (= K159), D238 (= D301), D240 (= D303), D242 (= D305), R243 (= R306)
- binding magnesium ion: S104 (= S149), D238 (= D301), D240 (= D303), D242 (= D305)
Sites not aligning to the query:
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
25% identity, 67% coverage: 53:437/575 of query aligns to 15:361/459 of 1k2yX
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
23% identity, 69% coverage: 48:442/575 of query aligns to 4:368/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
23% identity, 69% coverage: 48:442/575 of query aligns to 4:368/445 of 7ojrA
Sites not aligning to the query:
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
25% identity, 50% coverage: 53:337/575 of query aligns to 12:275/458 of 3uw2A
Sites not aligning to the query:
Query Sequence
>WP_035130453.1 NCBI__GCF_000769915.1:WP_035130453.1
MDIKKEILDKVNVWLSPLFDNQTQEAVKEMMTSSPKELEDSFYKNLEFGTGGMRGIMGPG
TNRINKYTLGKATQGLSNYLKKVFTGEEIKVAIAYDCRNNSNTLAKVVADVFSANGIKVF
LFTDLRPTPELSFAVRYLSCHAGIVLTASHNPPEYNGYKVYWQDGGQLVPPQDGEIINII
EALEYNQINFNANENLIEYIDNDVDKAFLGASLGAATFNTPQEAKDALKVVFTPLHGTSV
KLIPDLLEDAGYSNVHIVNEQAVPDGNFPTVKSPNPEEPEALAMAIELANQTNADIVVGT
DPDSDRLGVAVRNSEGIMTLLNGNQTMMLMTHFLLEEWKKQGKLTGNQFIGSTIVSTPML
MELATDYGVQCKVGLTGFKWIAKMIVDFPELQFIGGGEESFGYMVGDFVRDKDAVTSTLL
LCEIAAQAKANASSLYQELLKLYTKYGFYKEYLISLTKKGMDGAQEIKQMMIDLRESPLK
EINGERVVMVEDYQASTSKNLFTDEEEALTLPKSNVLIYYLEDGTKICARPSGTEPKIKF
YFSVNDTLDKVENAREVETILDHKIRNIIEEMNLI
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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