SitesBLAST
Comparing N515DRAFT_2990 FitnessBrowser__Dyella79:N515DRAFT_2990 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)
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)
59% identity, 59% coverage: 321:779/779 of query aligns to 8:463/463 of P26276
- R15 (= R328) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y330) binding ; binding
- R20 (= R333) mutation to A: No phosphoglucomutase activity.
- S108 (= S421) 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 (= N423) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D556) binding
- D244 (= D558) binding
- D246 (= D560) binding
- R247 (= R561) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (= R576) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K599) binding
- H308 (= H622) binding ; binding
- E325 (= E639) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 639:643) binding ; binding
- H329 (= H643) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P684) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R737) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RPSNT 737:741) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
59% identity, 59% coverage: 321:779/779 of query aligns to 8:463/463 of Q02E40
- S108 (= S421) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
59% identity, 59% coverage: 321:779/779 of query aligns to 3:458/458 of 1pcjX
- active site: R15 (= R333), S103 (= S421), H104 (= H422), K113 (= K431), D237 (= D556), D239 (= D558), D241 (= D560), R242 (= R561), H324 (= H643), D335 (= D654)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y330), S103 (= S421), T301 (= T620), G302 (= G621), E320 (= E639), S322 (= S641), H324 (= H643), R416 (= R737), S418 (= S739), N419 (= N740), T420 (= T741)
- binding zinc ion: S103 (= S421), D237 (= D556), D239 (= D558), D241 (= D560)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
59% identity, 58% coverage: 325:779/779 of query aligns to 4:455/455 of 2h5aX
- active site: H101 (= H422), D234 (= D556), D236 (= D558), D238 (= D560), R239 (= R561), D332 (= D654)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y330), T298 (= T620), G299 (= G621), H300 (= H622), E317 (= E639), S319 (= S641), H321 (= H643), R413 (= R737), S415 (= S739), N416 (= N740), T417 (= T741)
- binding zinc ion: S100 (= S421), D234 (= D556), D236 (= D558), D238 (= D560)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
59% identity, 58% coverage: 325:779/779 of query aligns to 4:455/455 of 2h4lX
- active site: H101 (= H422), D234 (= D556), D236 (= D558), D238 (= D560), R239 (= R561), D332 (= D654)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y330), R12 (= R333), S100 (= S421), T298 (= T620), E317 (= E639), R413 (= R737), S415 (= S739), N416 (= N740), T417 (= T741)
- binding zinc ion: S100 (= S421), D234 (= D556), D236 (= D558), D238 (= D560)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
59% identity, 58% coverage: 325:779/779 of query aligns to 4:455/455 of 2fkfA
- active site: R12 (= R333), S100 (= S421), H101 (= H422), K110 (= K431), D234 (= D556), D236 (= D558), D238 (= D560), R239 (= R561), H321 (= H643), D332 (= D654)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R328), H101 (= H422), S319 (= S641), R413 (= R737), S415 (= S739), N416 (= N740), T417 (= T741)
- binding zinc ion: S100 (= S421), D234 (= D556), D236 (= D558), D238 (= D560)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
59% identity, 58% coverage: 325:779/779 of query aligns to 4:455/455 of 1pcmX
- active site: R12 (= R333), S100 (= S421), H101 (= H422), K110 (= K431), D234 (= D556), D236 (= D558), D238 (= D560), R239 (= R561), H321 (= H643), D332 (= D654)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y330), S100 (= S421), T298 (= T620), G299 (= G621), H300 (= H622), E317 (= E639), S319 (= S641), H321 (= H643), R413 (= R737), S415 (= S739)
- binding zinc ion: S100 (= S421), D234 (= D556), D236 (= D558), D238 (= D560)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
59% identity, 58% coverage: 325:779/779 of query aligns to 4:455/455 of 1p5gX
- active site: R12 (= R333), S100 (= S421), H101 (= H422), K110 (= K431), D234 (= D556), D236 (= D558), D238 (= D560), R239 (= R561), H321 (= H643), D332 (= D654)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y330), S100 (= S421), K277 (= K599), G299 (= G621), H300 (= H622), E317 (= E639), S319 (= S641), H321 (= H643), R413 (= R737), S415 (= S739), N416 (= N740), T417 (= T741)
- binding zinc ion: S100 (= S421), D234 (= D556), D236 (= D558), D238 (= D560)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
59% identity, 58% coverage: 325:779/779 of query aligns to 4:455/455 of 1p5dX
- active site: R12 (= R333), S100 (= S421), H101 (= H422), K110 (= K431), D234 (= D556), D236 (= D558), D238 (= D560), R239 (= R561), H321 (= H643), D332 (= D654)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y330), S100 (= S421), R239 (= R561), T298 (= T620), G299 (= G621), H300 (= H622), E317 (= E639), S319 (= S641), H321 (= H643), R413 (= R737), S415 (= S739), T417 (= T741)
- binding zinc ion: S100 (= S421), D234 (= D556), D236 (= D558), D238 (= D560)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
59% identity, 59% coverage: 321:779/779 of query aligns to 4:459/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
59% identity, 59% coverage: 321:779/779 of query aligns to 4:459/459 of 4il8A
- active site: R16 (= R333), S104 (= S421), H105 (= H422), K114 (= K431), D238 (= D556), D240 (= D558), D242 (= D560), R243 (= R561), A325 (≠ H643), D336 (= D654)
- binding magnesium ion: S104 (= S421), D238 (= D556), D240 (= D558), D242 (= D560)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
57% identity, 57% coverage: 338:779/779 of query aligns to 4:436/436 of 3rsmA
- active site: C87 (≠ S421), K91 (= K431), D215 (= D556), D217 (= D558), D219 (= D560), R220 (= R561), H302 (= H643), D313 (= D654)
- binding phosphate ion: C87 (≠ S421), D215 (= D556), D217 (= D558), D219 (= D560), R220 (= R561)
- binding zinc ion: D215 (= D556), D217 (= D558), D219 (= D560)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
56% identity, 59% coverage: 322:779/779 of query aligns to 2:458/458 of 3uw2A
- active site: R13 (= R333), S109 (= S421), H110 (= H422), K119 (= K431), D243 (= D556), D245 (= D558), D247 (= D560), R248 (= R561), H330 (= H643)
- binding zinc ion: D243 (= D556), D245 (= D558), D247 (= D560)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
32% identity, 57% coverage: 326:769/779 of query aligns to 4:451/455 of 1wqaA
- active site: R11 (= R333), S101 (= S421), H102 (= H422), K111 (= K431), D243 (= D556), D245 (= D558), D247 (= D560), R248 (= R561), G330 (≠ H643), R340 (≠ D654)
- binding magnesium ion: S101 (= S421), D243 (= D556), D245 (= D558), D247 (= D560)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
33% identity, 56% coverage: 327:765/779 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R333), S97 (= S421), H98 (= H422), K107 (= K431), D237 (= D556), D239 (= D558), D241 (= D560), R242 (= R561), H324 (= H643)
- binding magnesium ion: D237 (= D556), D239 (= D558), D241 (= D560)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R333), S97 (= S421), H98 (= H422), K107 (= K431), D239 (= D558), R242 (= R561), R280 (≠ K599), S301 (≠ T620), G302 (= G621), E320 (= E639), S322 (= S641), H324 (= H643), R414 (= R737), S416 (= S739), N417 (= N740), T418 (= T741), R423 (≠ V746)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
33% identity, 56% coverage: 327:765/779 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R333), S97 (= S421), H98 (= H422), K107 (= K431), D237 (= D556), D239 (= D558), D241 (= D560), R242 (= R561), H324 (= H643)
- binding calcium ion: S97 (= S421), D237 (= D556), D239 (= D558), D241 (= D560)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y330), R280 (≠ K599), G302 (= G621), H303 (= H622), E320 (= E639), S322 (= S641), H324 (= H643), R414 (= R737), S416 (= S739), N417 (= N740), T418 (= T741), R423 (≠ V746)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
33% identity, 56% coverage: 327:765/779 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R333), S97 (= S421), H98 (= H422), K107 (= K431), D237 (= D556), D239 (= D558), D241 (= D560), R242 (= R561), H324 (= H643)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G621), E320 (= E639), S322 (= S641), H324 (= H643), R414 (= R737), S416 (= S739), N417 (= N740), T418 (= T741), R423 (≠ V746)
- binding magnesium ion: S97 (= S421), D237 (= D556), D239 (= D558), D241 (= D560)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
33% identity, 56% coverage: 327:765/779 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R333), S97 (= S421), H98 (= H422), K107 (= K431), D237 (= D556), D239 (= D558), D241 (= D560), R242 (= R561), H324 (= H643)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K599), G302 (= G621), H303 (= H622), E320 (= E639), H324 (= H643), R414 (= R737), S416 (= S739), N417 (= N740), T418 (= T741), R423 (≠ V746)
- binding magnesium ion: S97 (= S421), D237 (= D556), D239 (= D558), D241 (= D560)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
33% identity, 56% coverage: 327:765/779 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R333), S97 (= S421), H98 (= H422), K107 (= K431), D237 (= D556), D239 (= D558), D241 (= D560), R242 (= R561), H324 (= H643)
- binding calcium ion: S97 (= S421), D237 (= D556), D239 (= D558), D241 (= D560)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
33% identity, 56% coverage: 327:765/779 of query aligns to 6:447/448 of 6n1eA
Query Sequence
>N515DRAFT_2990 FitnessBrowser__Dyella79:N515DRAFT_2990
MAMDIAMGLRERTFDWQRLLPLAGGTLLLVGGLFCAWQSWLIADESAAIERVHRAQDQLA
QSLADELASQRRTLQQQLDTLDPAAVQADPKYAATLLRGKVPQAQAIEFYSGTLDEVLHA
NYRDFGYAKAAQLMAAQTADGDTLAQTLPKGVGDRRLSFVLPMGPRQHPNAWVLFELPFA
PVEERFNAVPPEGGRLELRQGDDRGRGDARLLANGNGSALSEPVGKVVAGSNLSVVAAPP
GAYIVLPKSVLLAALLTLLGLGGGVYLLWMRGRVPGVSFGRPKISNEEPILSDLIDNTPE
PAKPEARPAKPAAPAAPVPVTVDPTIFRAYDVRGIVGKSLNTDVARLLGQSIGTVMREKG
LREIVVGRDGRLSGPELTAALSDGLREAGIDVIDIGAVPTPVVYYAAYRFNTGSGVAVTG
SHNPPDYNGFKIVVGGETLSEGSIQDLYRRIAANELERGGKGSLRQIDVVPDYVERITSD
VQAGRRMKVVVDCGNGIPGSVAPQVLEGIGCEVIQLYCDVDGTFPNHHPDPSDPHNLEDL
ILAVKSTGADLGVAFDGDGDRLGVVTKTGEIIFPDRTLMLFARDVLSRQPGATIIYDVKC
TGHLKGQILDAGGSPLMWRTGHSLIKSKMRETGAELAGEMSGHFFFKERWYGFDDGIYAG
ARLLEILAGDLDERTPEQIFATCPKGVSTPELKIEMKEGEHYKFIEKFRQSASFGDAALT
TIDGVRADWPDGWGLVRPSNTTPILVLRFDADNDAALKRIQNVFREQLHAVDPALKLPF
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