SitesBLAST
Comparing WP_043917781.1 NCBI__GCF_000877395.1:WP_043917781.1 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)
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
50% identity, 99% coverage: 4:443/446 of query aligns to 7:443/445 of P31120
- S100 (= S100) 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 (= S102) 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
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
46% identity, 98% coverage: 4:442/446 of query aligns to 4:440/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
46% identity, 98% coverage: 4:442/446 of query aligns to 4:440/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
38% identity, 96% coverage: 4:430/446 of query aligns to 3:424/441 of 3i3wA
- active site: R9 (= R10), S99 (= S102), H100 (= H103), K109 (= K112), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H330)
- binding zinc ion: S99 (= S102), D237 (= D241), D239 (= D243), D241 (= D245)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
34% identity, 97% coverage: 3:435/446 of query aligns to 4:443/455 of 1wqaA
- active site: R11 (= R10), S101 (= S102), H102 (= H103), K111 (= K112), D243 (= D241), D245 (= D243), D247 (= D245), R248 (= R246), G330 (≠ H330), R340 (≠ G340)
- binding magnesium ion: S101 (= S102), D243 (= D241), D245 (= D243), D247 (= D245)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 21:435/458 of 1pcjX
- active site: S103 (= S102), H104 (= H103), K113 (= K112), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H330), D335 (≠ G340)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S102), T301 (≠ V307), G302 (= G308), E320 (= E326), S322 (= S328), H324 (= H330), R416 (= R411), S418 (= S413), N419 (≠ G414), T420 (= T415)
- binding zinc ion: S103 (= S102), D237 (= D241), D239 (= D243), D241 (= D245)
Sites not aligning to the query:
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 18:432/455 of 2h5aX
- active site: H101 (= H103), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), D332 (≠ G340)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (≠ V307), G299 (= G308), H300 (≠ D309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 18:432/455 of 2h4lX
- active site: H101 (= H103), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), D332 (≠ G340)
- binding 1-O-phosphono-alpha-D-ribofuranose: S100 (= S102), T298 (≠ V307), E317 (= E326), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 18:432/455 of 2fkfA
- active site: S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H330), D332 (≠ G340)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H103), S319 (= S328), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 18:432/455 of 1pcmX
- active site: S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H330), D332 (≠ G340)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S102), T298 (≠ V307), G299 (= G308), H300 (≠ D309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R411), S415 (= S413)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 18:432/455 of 1p5gX
- active site: S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H330), D332 (≠ G340)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S102), K277 (≠ M286), G299 (= G308), H300 (≠ D309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 18:432/455 of 1p5dX
- active site: S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H330), D332 (≠ G340)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S102), R239 (= R246), T298 (≠ V307), G299 (= G308), H300 (≠ D309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R411), S415 (= S413), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
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)
29% identity, 92% coverage: 17:428/446 of query aligns to 26:440/463 of P26276
- S108 (= S102) 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 (= N104) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D241) binding Mg(2+)
- D244 (= D243) binding Mg(2+)
- D246 (= D245) binding Mg(2+)
- R247 (= R246) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q261) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M286) binding alpha-D-glucose 1-phosphate
- H308 (≠ D309) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E326) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 326:330) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H330) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P371) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R411) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RASGT 411:415) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
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
- 20 R→A: No phosphoglucomutase activity.
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
29% identity, 92% coverage: 17:428/446 of query aligns to 26:440/463 of Q02E40
- S108 (= S102) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
28% identity, 92% coverage: 17:428/446 of query aligns to 22:436/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
28% identity, 92% coverage: 17:428/446 of query aligns to 22:436/459 of 4il8A
- active site: S104 (= S102), H105 (= H103), K114 (= K112), D238 (= D241), D240 (= D243), D242 (= D245), R243 (= R246), A325 (≠ H330), D336 (≠ G340)
- binding magnesium ion: S104 (= S102), D238 (= D241), D240 (= D243), D242 (= D245)
Sites not aligning to the query:
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
29% identity, 89% coverage: 45:439/446 of query aligns to 41:444/449 of 6mlwA
- active site: S98 (= S102), H99 (= H103), K108 (= K112), D238 (= D241), D240 (= D243), D242 (= D245), R243 (= R246), H325 (= H330)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G308), H304 (≠ D309), E321 (= E326), S323 (= S328), H325 (= H330), R415 (= R411), S417 (= S413), N418 (≠ G414), T419 (= T415), R424 (= R420)
- binding magnesium ion: S98 (= S102), D238 (= D241), D240 (= D243), D242 (= D245)
Sites not aligning to the query:
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
29% identity, 89% coverage: 45:439/446 of query aligns to 41:444/449 of 5bmpA
- active site: S98 (= S102), H99 (= H103), K108 (= K112), D238 (= D241), D240 (= D243), D242 (= D245), R243 (= R246), H325 (= H330)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ V285), G303 (= G308), E321 (= E326), S323 (= S328), H325 (= H330), R415 (= R411), S417 (= S413), N418 (≠ G414), T419 (= T415), R424 (= R420)
- binding magnesium ion: S98 (= S102), D238 (= D241), D240 (= D243), D242 (= D245)
Sites not aligning to the query:
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
29% identity, 89% coverage: 45:439/446 of query aligns to 40:443/448 of 6nqhA
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H330)
- binding magnesium ion: D237 (= D241), D239 (= D243), D241 (= D245)
- binding 1-O-phosphono-alpha-D-xylopyranose: S97 (= S102), H98 (= H103), K107 (= K112), D239 (= D243), R242 (= R246), R280 (≠ V285), S301 (≠ V307), G302 (= G308), E320 (= E326), S322 (= S328), H324 (= H330), R414 (= R411), S416 (= S413), N417 (≠ G414), T418 (= T415), R423 (= R420)
Sites not aligning to the query:
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
29% identity, 89% coverage: 45:439/446 of query aligns to 40:443/448 of 6np8A
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H330)
- binding calcium ion: S97 (= S102), D237 (= D241), D239 (= D243), D241 (= D245)
- binding 6-O-phosphono-alpha-D-mannopyranose: R280 (≠ V285), G302 (= G308), H303 (≠ D309), E320 (= E326), S322 (= S328), H324 (= H330), R414 (= R411), S416 (= S413), N417 (≠ G414), T418 (= T415), R423 (= R420)
Sites not aligning to the query:
Query Sequence
>WP_043917781.1 NCBI__GCF_000877395.1:WP_043917781.1
MGLFGTDGVRGRANQGNMTAEMALRLGAAAGRYFRREGDGAGHRVVIGKDTRLSGYMLEN
ALTAGLTSTGMNVLLLGPVPTPAVGLLARSMRADLGVMISASHNPAEDNGIKFFGPDGFK
LSDEAEAEIEAMVRDGVRLAQARNIGRAKRIDDGRGRYVEYVKTTIPTGMSLDGLKIVVD
CANGASYRAAPDVLSELGATVIPVGVSPDGHNINDGVGSTHPEACAATVREAGADLGISL
DGDADRVMILDAQGRVADGDQIMALFAVRWAEEGRLKGPALVATVMSNLGLERFVNGRGI
DLHRTRVGDRYVVEEMRTGGFNLGGEQSGHIVMTDYATTGDGLIAGLQFAAEMVRTGRAA
ADLMHSFEPVPQKLTNVRYADGARPLDATEVKAAIAAAEDRLKGQGRLLIRASGTEPLIR
VMAECEDEGLLQDVVAEVAGAVERAA
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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