SitesBLAST
Comparing WP_017752866.1 NCBI__GCF_000816635.1:WP_017752866.1 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)
P18159 Phosphoglucomutase; PGM; Alpha-phosphoglucomutase; Glucose phosphomutase; EC 5.4.2.2 from Bacillus subtilis (strain 168) (see paper)
48% identity, 99% coverage: 2:572/577 of query aligns to 3:577/581 of P18159
- G162 (= G159) mutation to D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- T240 (≠ S239) mutation to I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- G407 (= G406) mutation to D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology.
- D418 (= D417) 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)
32% identity, 94% coverage: 8:550/577 of query aligns to 21:574/612 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)
31% identity, 97% coverage: 3:561/577 of query aligns to 6:567/587 of O74478
- S149 (= S143) 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)
32% identity, 91% coverage: 28:551/577 of query aligns to 41:590/622 of Q03262
- S158 (= S143) mutation to T: Loss of function.
- P326 (= P303) mutation to G: No effect.
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
23% identity, 87% coverage: 42:545/577 of query aligns to 5:430/455 of 1wqaA
- active site: R11 (= R48), S101 (= S143), H102 (= H144), K111 (= K153), D243 (= D302), D245 (= D304), D247 (= D306), R248 (= R307), G330 (= G406), R340 (≠ K416)
- binding magnesium ion: S101 (= S143), D243 (= D302), D245 (= D304), D247 (= D306)
2fuvA Phosphoglucomutase from salmonella typhimurium.
24% identity, 88% coverage: 40:546/577 of query aligns to 39:518/545 of 2fuvA
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 11:243/455 of 2h5aX
Sites not aligning to the query:
- active site: 332
- binding 1-O-phosphono-alpha-D-xylopyranose: 9, 298, 299, 300, 317, 319, 321, 413, 415, 416, 417
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 11:243/455 of 2h4lX
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 11:243/455 of 2fkfA
- active site: R12 (= R48), S100 (= S143), H101 (= H144), K110 (= K153), D234 (= D302), D236 (= D304), D238 (= D306), R239 (= R307)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H144)
- binding zinc ion: S100 (= S143), D234 (= D302), D236 (= D304), D238 (= D306)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 11:243/455 of 1pcmX
- active site: R12 (= R48), S100 (= S143), H101 (= H144), K110 (= K153), D234 (= D302), D236 (= D304), D238 (= D306), R239 (= R307)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S143)
- binding zinc ion: S100 (= S143), D234 (= D302), D236 (= D304), D238 (= D306)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 11:243/455 of 1p5gX
- active site: R12 (= R48), S100 (= S143), H101 (= H144), K110 (= K153), D234 (= D302), D236 (= D304), D238 (= D306), R239 (= R307)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S143)
- binding zinc ion: S100 (= S143), D234 (= D302), D236 (= D304), D238 (= D306)
Sites not aligning to the query:
- active site: 321, 332
- binding 6-O-phosphono-alpha-D-glucopyranose: 9, 277, 299, 300, 317, 319, 321, 413, 415, 416, 417
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 11:243/455 of 1p5dX
- active site: R12 (= R48), S100 (= S143), H101 (= H144), K110 (= K153), D234 (= D302), D236 (= D304), D238 (= D306), R239 (= R307)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S143), R239 (= R307)
- binding zinc ion: S100 (= S143), D234 (= D302), D236 (= D304), D238 (= D306)
Sites not aligning to the query:
- active site: 321, 332
- binding 1-O-phosphono-alpha-D-glucopyranose: 9, 298, 299, 300, 317, 319, 321, 413, 415, 417
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
26% identity, 47% coverage: 47:316/577 of query aligns to 14:251/458 of 1pcjX
- active site: R15 (= R48), S103 (= S143), H104 (= H144), K113 (= K153), D237 (= D302), D239 (= D304), D241 (= D306), R242 (= R307)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S143)
- binding zinc ion: S103 (= S143), D237 (= D302), D239 (= D304), D241 (= D306)
Sites not aligning to the query:
- active site: 324, 335
- binding 1-O-phosphono-alpha-D-mannopyranose: 12, 301, 302, 320, 322, 324, 416, 418, 419, 420
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 15:247/459 of 4il8A
- active site: R16 (= R48), S104 (= S143), H105 (= H144), K114 (= K153), D238 (= D302), D240 (= D304), D242 (= D306), R243 (= R307)
- binding magnesium ion: S104 (= S143), D238 (= D302), D240 (= D304), D242 (= D306)
Sites not aligning to the query:
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)
26% identity, 46% coverage: 47:311/577 of query aligns to 19:251/463 of P26276
- R20 (= R48) mutation to A: No phosphoglucomutase activity.
- S108 (= S143) 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 (= N145) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D302) binding Mg(2+)
- D244 (= D304) binding Mg(2+)
- D246 (= D306) binding Mg(2+)
- R247 (= R307) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 15 R→A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- 17 binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- 262 R→A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- 285 binding alpha-D-glucose 1-phosphate
- 308 binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- 325 E→A: Reduces KM and Vmax approximately 2-fold.
- 325:329 binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- 329 H→A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- 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)
26% identity, 46% coverage: 47:311/577 of query aligns to 19:251/463 of Q02E40
- S108 (= S143) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
26% identity, 46% coverage: 47:311/577 of query aligns to 15:247/459 of 1k2yX
Sites not aligning to the query:
Q9VUY9 Phosphoglucomutase 1; PGM; Glucose phosphomutase; EC 5.4.2.2 from Drosophila melanogaster (Fruit fly) (see 4 papers)
23% identity, 88% coverage: 32:538/577 of query aligns to 8:507/560 of Q9VUY9
- K17 (≠ E41) natural variant: K -> Q
- K28 (≠ N59) natural variant: K -> N
- T36 (= T67) natural variant: T -> M
- S116 (= S143) modified: Phosphoserine
- E351 (= E371) natural variant: E -> K
Sites not aligning to the query:
- 6 natural variant: E -> G
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
21% identity, 83% coverage: 85:565/577 of query aligns to 41:448/449 of 6mlwA
- active site: S98 (= S143), H99 (= H144), K108 (= K153), D238 (= D302), D240 (= D304), D242 (= D306), R243 (= R307), H325 (≠ G406)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G378), H304 (≠ F379), E321 (= E402), S323 (= S404), H325 (≠ G406), R415 (= R534), S417 (= S536), N418 (≠ G537), T419 (= T538), R424 (≠ K543)
- binding magnesium ion: S98 (= S143), D238 (= D302), D240 (= D304), D242 (= D306)
Sites not aligning to the query:
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
21% identity, 83% coverage: 85:565/577 of query aligns to 41:448/449 of 5bmpA
- active site: S98 (= S143), H99 (= H144), K108 (= K153), D238 (= D302), D240 (= D304), D242 (= D306), R243 (= R307), H325 (≠ G406)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ I355), G303 (= G378), E321 (= E402), S323 (= S404), H325 (≠ G406), R415 (= R534), S417 (= S536), N418 (≠ G537), T419 (= T538), R424 (≠ K543)
- binding magnesium ion: S98 (= S143), D238 (= D302), D240 (= D304), D242 (= D306)
Sites not aligning to the query:
Query Sequence
>WP_017752866.1 NCBI__GCF_000816635.1:WP_017752866.1
MYREKYEQWLNSEFIDEDTKKELRNIKDEQEIEDRFYKDLEFGTGGLRGVMAAGTNRMNI
YTIGKTTQGLSDYLLNKYKNADISVSIGYDSRIMSKEFAERAALNLCANGIKVNLFESLR
PTPMLSYAVRYFKSKAGIVITASHNPKQYNGYKVYGEDGGQVTDTLAKEILYSIENVDDI
SKIKNMSRSGAENKKLLNIVGEEVDRSYLEKVKGLGIRKELVKSKAKELNIIYTPIHGSG
NVPVRRALSELGYENVFVVKEQEKPDGNFPTAPYPNPEDPKVFEIALDMAKKIKPDIIFG
TDPDCDRIGVIVKNSNGEYKILTGNQTGILLTNYILSSLKEFNSIPENGAIVKTIVTTEA
ASKIAEDYGVEIIDVLTGFKYIGEKIKEFKKSGDKNFIFGFEESYGYLAGDFVRDKDAVI
ASTLICEMSLYYKSKGMSLYDALIALYDKYGYYREKLVSVELKGKEGHEKIEKIMQYLRH
SMKNIVGSVKIVKKMDYKLSVEKDLVSIKEIPINLPKSNVLKFILEDKSCFVVRPSGTEP
KIKIYLSVIGNTLDDSKNRIENFQKKIDNIFDDARES
Or try a new SitesBLAST search
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