SitesBLAST
Comparing 353476 FitnessBrowser__Btheta:353476 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)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
37% identity, 95% coverage: 12:448/462 of query aligns to 6:441/455 of 1wqaA
- active site: R11 (vs. gap), S101 (= S106), H102 (= H107), K111 (= K116), D243 (= D251), D245 (= D253), D247 (= D255), R248 (= R256), G330 (= G337), R340 (= R347)
- binding magnesium ion: S101 (= S106), D243 (= D251), D245 (= D253), D247 (= D255)
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 47:440/459 of 4il8A
- active site: S104 (= S106), H105 (= H107), K114 (= K116), D238 (= D251), D240 (= D253), D242 (= D255), R243 (= R256), A325 (≠ G337), D336 (≠ R347)
- binding magnesium ion: S104 (= S106), D238 (= D251), D240 (= D253), D242 (= D255)
Sites not aligning to the query:
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 43:436/455 of 2h5aX
- active site: H101 (= H107), D234 (= D251), D236 (= D253), D238 (= D255), R239 (= R256), D332 (≠ R347)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (≠ V314), G299 (= G315), H300 (≠ E316), E317 (= E333), S319 (≠ N335), H321 (≠ G337), R413 (= R426), S415 (= S428), N416 (= N429), T417 (= T430)
- binding zinc ion: S100 (= S106), D234 (= D251), D236 (= D253), D238 (= D255)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 43:436/455 of 2h4lX
- active site: H101 (= H107), D234 (= D251), D236 (= D253), D238 (= D255), R239 (= R256), D332 (≠ R347)
- binding 1-O-phosphono-alpha-D-ribofuranose: S100 (= S106), T298 (≠ V314), E317 (= E333), R413 (= R426), S415 (= S428), N416 (= N429), T417 (= T430)
- binding zinc ion: S100 (= S106), D234 (= D251), D236 (= D253), D238 (= D255)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 43:436/455 of 2fkfA
- active site: S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D251), D236 (= D253), D238 (= D255), R239 (= R256), H321 (≠ G337), D332 (≠ R347)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H107), S319 (≠ N335), R413 (= R426), S415 (= S428), N416 (= N429), T417 (= T430)
- binding zinc ion: S100 (= S106), D234 (= D251), D236 (= D253), D238 (= D255)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 43:436/455 of 1pcmX
- active site: S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D251), D236 (= D253), D238 (= D255), R239 (= R256), H321 (≠ G337), D332 (≠ R347)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S106), T298 (≠ V314), G299 (= G315), H300 (≠ E316), E317 (= E333), S319 (≠ N335), H321 (≠ G337), R413 (= R426), S415 (= S428)
- binding zinc ion: S100 (= S106), D234 (= D251), D236 (= D253), D238 (= D255)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 43:436/455 of 1p5gX
- active site: S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D251), D236 (= D253), D238 (= D255), R239 (= R256), H321 (≠ G337), D332 (≠ R347)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S106), K277 (≠ S293), G299 (= G315), H300 (≠ E316), E317 (= E333), S319 (≠ N335), H321 (≠ G337), R413 (= R426), S415 (= S428), N416 (= N429), T417 (= T430)
- binding zinc ion: S100 (= S106), D234 (= D251), D236 (= D253), D238 (= D255)
Sites not aligning to the query:
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 43:436/455 of 1p5dX
- active site: S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D251), D236 (= D253), D238 (= D255), R239 (= R256), H321 (≠ G337), D332 (≠ R347)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S106), R239 (= R256), T298 (≠ V314), G299 (= G315), H300 (≠ E316), E317 (= E333), S319 (≠ N335), H321 (≠ G337), R413 (= R426), S415 (= S428), T417 (= T430)
- binding zinc ion: S100 (= S106), D234 (= D251), D236 (= D253), D238 (= D255)
Sites not aligning to the query:
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 87% coverage: 49:449/462 of query aligns to 46:439/458 of 1pcjX
- active site: S103 (= S106), H104 (= H107), K113 (= K116), D237 (= D251), D239 (= D253), D241 (= D255), R242 (= R256), H324 (≠ G337), D335 (≠ R347)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S106), T301 (≠ V314), G302 (= G315), E320 (= E333), S322 (≠ N335), H324 (≠ G337), R416 (= R426), S418 (= S428), N419 (= N429), T420 (= T430)
- binding zinc ion: S103 (= S106), D237 (= D251), D239 (= D253), D241 (= D255)
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)
30% identity, 87% coverage: 49:449/462 of query aligns to 51:444/463 of P26276
- S108 (= S106) 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 (= N108) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D251) binding
- D244 (= D253) binding
- D246 (= D255) binding
- R247 (= R256) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Y271) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ S293) binding
- H308 (≠ E316) binding ; binding
- E325 (= E333) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EGNGG 333:337) binding ; binding
- H329 (≠ G337) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P375) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R426) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RKSNT 426:430) binding ; binding
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 ; binding
- 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)
30% identity, 87% coverage: 49:449/462 of query aligns to 51:444/463 of Q02E40
- S108 (= S106) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
29% identity, 87% coverage: 49:449/462 of query aligns to 47:440/459 of 1k2yX
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
29% identity, 87% coverage: 49:449/462 of query aligns to 30:417/436 of 3rsmA
- active site: C87 (≠ S106), K91 (= K116), D215 (= D251), D217 (= D253), D219 (= D255), R220 (= R256), H302 (≠ G337), D313 (≠ R347)
- binding phosphate ion: C87 (≠ S106), D215 (= D251), D217 (= D253), D219 (= D255), R220 (= R256)
- binding zinc ion: D215 (= D251), D217 (= D253), D219 (= D255)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6nqhA
- active site: S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D251), D239 (= D253), D241 (= D255), R242 (= R256), H324 (≠ G337)
- binding magnesium ion: D237 (= D251), D239 (= D253), D241 (= D255)
- binding 1-O-phosphono-alpha-D-xylopyranose: S97 (= S106), H98 (= H107), K107 (= K116), D239 (= D253), R242 (= R256), R280 (vs. gap), S301 (≠ A313), G302 (= G315), E320 (= E333), S322 (≠ N335), H324 (≠ G337), R414 (= R426), S416 (= S428), N417 (= N429), T418 (= T430), R423 (= R435)
Sites not aligning to the query:
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6np8A
- active site: S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D251), D239 (= D253), D241 (= D255), R242 (= R256), H324 (≠ G337)
- binding calcium ion: S97 (= S106), D237 (= D251), D239 (= D253), D241 (= D255)
- binding 6-O-phosphono-alpha-D-mannopyranose: R280 (vs. gap), G302 (= G315), H303 (≠ E316), E320 (= E333), S322 (≠ N335), H324 (≠ G337), R414 (= R426), S416 (= S428), N417 (= N429), T418 (= T430), R423 (= R435)
Sites not aligning to the query:
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6nolA
- active site: S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D251), D239 (= D253), D241 (= D255), R242 (= R256), H324 (≠ G337)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G315), E320 (= E333), S322 (≠ N335), H324 (≠ G337), R414 (= R426), S416 (= S428), N417 (= N429), T418 (= T430), R423 (= R435)
- binding magnesium ion: S97 (= S106), D237 (= D251), D239 (= D253), D241 (= D255)
Sites not aligning to the query:
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6nnpA
- active site: S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D251), D239 (= D253), D241 (= D255), R242 (= R256), H324 (≠ G337)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (vs. gap), G302 (= G315), H303 (≠ E316), E320 (= E333), H324 (≠ G337), R414 (= R426), S416 (= S428), N417 (= N429), T418 (= T430), R423 (= R435)
- binding magnesium ion: S97 (= S106), D237 (= D251), D239 (= D253), D241 (= D255)
Sites not aligning to the query:
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6nn2A
- active site: S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D251), D239 (= D253), D241 (= D255), R242 (= R256), H324 (≠ G337)
- binding calcium ion: S97 (= S106), D237 (= D251), D239 (= D253), D241 (= D255)
Sites not aligning to the query:
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
26% identity, 89% coverage: 49:460/462 of query aligns to 40:446/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (vs. gap), G302 (= G315), E320 (= E333), S322 (≠ N335), H324 (≠ G337), R414 (= R426), S416 (= S428), N417 (= N429), T418 (= T430), R423 (= R435)
- binding magnesium ion: S97 (= S106), D237 (= D251), D239 (= D253), D241 (= D255)
Query Sequence
>353476 FitnessBrowser__Btheta:353476
MTLIKSISGIRGTIGGGAGEGLNPLDIVKFTSAYATLIRKTCKAQSNKIVVGRDARISGE
MVKNVVVGTLMGMGWDVVDIDLASTPTTELAVTMEGACGGIILTASHNPKQWNALKLLNE
HGEFLNAEEGNEVLRIAEAEEFDYADVDHLGSYRKDLTYNQKHIDSVLALDLVDVEAIKK
ANFRVAIDCVNSVGGIILPELLERLGVKHVEKLYCEPTGNFQHNPEPLEKNLGDIMNLMK
GGKADVAFVVDPDVDRLAMICENGVMYGEEYTLVTVADYVLKHTPGNTVSNLSSTRALRD
VTRKYGMEYSASAVGEVNVVTKMKATNAVIGGEGNGGVIYPASHYGRDALVGIALFLSHL
AHEGKKVSELRATYPPYFIAKNRVDLIPEIDVDAILAKVKEIYKNEEINDIDGVKIDFAD
KWVHLRKSNTEPIIRVYSEASTMGAAEEIGQKIMDVINELAK
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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