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Comparing GFF3376 FitnessBrowser__Marino:GFF3376 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)
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)
66% identity, 52% coverage: 426:880/880 of query aligns to 9:463/463 of P26276
- R15 (= R432) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y434) binding ; binding
- R20 (= R437) mutation to A: No phosphoglucomutase activity.
- S108 (= S525) 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 (= N527) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D659) binding
- D244 (= D661) binding
- D246 (= D663) binding
- R247 (= R664) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (= R679) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K702) binding
- H308 (= H725) binding ; binding
- E325 (= E742) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 742:746) binding ; binding
- H329 (= H746) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P785) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R838) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (= RASNT 838:842) 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)
66% identity, 52% coverage: 426:880/880 of query aligns to 9:463/463 of Q02E40
- S108 (= S525) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 4:458/458 of 1pcjX
- active site: R15 (= R437), S103 (= S525), H104 (= H526), K113 (= K535), D237 (= D659), D239 (= D661), D241 (= D663), R242 (= R664), H324 (= H746), D335 (= D757)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y434), S103 (= S525), T301 (= T723), G302 (= G724), E320 (= E742), S322 (= S744), H324 (= H746), R416 (= R838), S418 (= S840), N419 (= N841), T420 (= T842)
- binding zinc ion: S103 (= S525), D237 (= D659), D239 (= D661), D241 (= D663)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 1:455/455 of 2h5aX
- active site: H101 (= H526), D234 (= D659), D236 (= D661), D238 (= D663), R239 (= R664), D332 (= D757)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y434), T298 (= T723), G299 (= G724), H300 (= H725), E317 (= E742), S319 (= S744), H321 (= H746), R413 (= R838), S415 (= S840), N416 (= N841), T417 (= T842)
- binding zinc ion: S100 (= S525), D234 (= D659), D236 (= D661), D238 (= D663)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 1:455/455 of 2h4lX
- active site: H101 (= H526), D234 (= D659), D236 (= D661), D238 (= D663), R239 (= R664), D332 (= D757)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y434), R12 (= R437), S100 (= S525), T298 (= T723), E317 (= E742), R413 (= R838), S415 (= S840), N416 (= N841), T417 (= T842)
- binding zinc ion: S100 (= S525), D234 (= D659), D236 (= D661), D238 (= D663)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 1:455/455 of 2fkfA
- active site: R12 (= R437), S100 (= S525), H101 (= H526), K110 (= K535), D234 (= D659), D236 (= D661), D238 (= D663), R239 (= R664), H321 (= H746), D332 (= D757)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R432), H101 (= H526), S319 (= S744), R413 (= R838), S415 (= S840), N416 (= N841), T417 (= T842)
- binding zinc ion: S100 (= S525), D234 (= D659), D236 (= D661), D238 (= D663)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 1:455/455 of 1pcmX
- active site: R12 (= R437), S100 (= S525), H101 (= H526), K110 (= K535), D234 (= D659), D236 (= D661), D238 (= D663), R239 (= R664), H321 (= H746), D332 (= D757)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y434), S100 (= S525), T298 (= T723), G299 (= G724), H300 (= H725), E317 (= E742), S319 (= S744), H321 (= H746), R413 (= R838), S415 (= S840)
- binding zinc ion: S100 (= S525), D234 (= D659), D236 (= D661), D238 (= D663)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 1:455/455 of 1p5gX
- active site: R12 (= R437), S100 (= S525), H101 (= H526), K110 (= K535), D234 (= D659), D236 (= D661), D238 (= D663), R239 (= R664), H321 (= H746), D332 (= D757)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y434), S100 (= S525), K277 (= K702), G299 (= G724), H300 (= H725), E317 (= E742), S319 (= S744), H321 (= H746), R413 (= R838), S415 (= S840), N416 (= N841), T417 (= T842)
- binding zinc ion: S100 (= S525), D234 (= D659), D236 (= D661), D238 (= D663)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
66% identity, 52% coverage: 426:880/880 of query aligns to 1:455/455 of 1p5dX
- active site: R12 (= R437), S100 (= S525), H101 (= H526), K110 (= K535), D234 (= D659), D236 (= D661), D238 (= D663), R239 (= R664), H321 (= H746), D332 (= D757)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y434), S100 (= S525), R239 (= R664), T298 (= T723), G299 (= G724), H300 (= H725), E317 (= E742), S319 (= S744), H321 (= H746), R413 (= R838), S415 (= S840), T417 (= T842)
- binding zinc ion: S100 (= S525), D234 (= D659), D236 (= D661), D238 (= D663)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
65% identity, 52% coverage: 426:880/880 of query aligns to 5:459/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
65% identity, 52% coverage: 426:880/880 of query aligns to 5:459/459 of 4il8A
- active site: R16 (= R437), S104 (= S525), H105 (= H526), K114 (= K535), D238 (= D659), D240 (= D661), D242 (= D663), R243 (= R664), A325 (≠ H746), D336 (= D757)
- binding magnesium ion: S104 (= S525), D238 (= D659), D240 (= D661), D242 (= D663)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
63% identity, 51% coverage: 430:880/880 of query aligns to 2:436/436 of 3rsmA
- active site: C87 (≠ S525), K91 (= K535), D215 (= D659), D217 (= D661), D219 (= D663), R220 (= R664), H302 (= H746), D313 (= D757)
- binding phosphate ion: C87 (≠ S525), D215 (= D659), D217 (= D661), D219 (= D663), R220 (= R664)
- binding zinc ion: D215 (= D659), D217 (= D661), D219 (= D663)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
55% identity, 51% coverage: 426:874/880 of query aligns to 2:452/458 of 3uw2A
- active site: R13 (= R437), S109 (= S525), H110 (= H526), K119 (= K535), D243 (= D659), D245 (= D661), D247 (= D663), R248 (= R664), H330 (= H746)
- binding zinc ion: D243 (= D659), D245 (= D661), D247 (= D663)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
33% identity, 49% coverage: 431:863/880 of query aligns to 7:440/449 of 6mlwA
- active site: R13 (= R437), S98 (= S525), H99 (= H526), K108 (= K535), D238 (= D659), D240 (= D661), D242 (= D663), R243 (= R664), H325 (= H746)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G724), H304 (= H725), E321 (= E742), S323 (= S744), H325 (= H746), R415 (= R838), S417 (= S840), N418 (= N841), T419 (= T842), R424 (≠ V847)
- binding magnesium ion: S98 (= S525), D238 (= D659), D240 (= D661), D242 (= D663)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
33% identity, 49% coverage: 431:863/880 of query aligns to 7:440/449 of 5bmpA
- active site: R13 (= R437), S98 (= S525), H99 (= H526), K108 (= K535), D238 (= D659), D240 (= D661), D242 (= D663), R243 (= R664), H325 (= H746)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ K702), G303 (= G724), E321 (= E742), S323 (= S744), H325 (= H746), R415 (= R838), S417 (= S840), N418 (= N841), T419 (= T842), R424 (≠ V847)
- binding magnesium ion: S98 (= S525), D238 (= D659), D240 (= D661), D242 (= D663)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
33% identity, 49% coverage: 431:863/880 of query aligns to 6:439/448 of 6nqhA
- active site: R12 (= R437), S97 (= S525), H98 (= H526), K107 (= K535), D237 (= D659), D239 (= D661), D241 (= D663), R242 (= R664), H324 (= H746)
- binding magnesium ion: D237 (= D659), D239 (= D661), D241 (= D663)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R437), S97 (= S525), H98 (= H526), K107 (= K535), D239 (= D661), R242 (= R664), R280 (≠ K702), S301 (≠ T723), G302 (= G724), E320 (= E742), S322 (= S744), H324 (= H746), R414 (= R838), S416 (= S840), N417 (= N841), T418 (= T842), R423 (≠ V847)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
33% identity, 49% coverage: 431:863/880 of query aligns to 6:439/448 of 6np8A
- active site: R12 (= R437), S97 (= S525), H98 (= H526), K107 (= K535), D237 (= D659), D239 (= D661), D241 (= D663), R242 (= R664), H324 (= H746)
- binding calcium ion: S97 (= S525), D237 (= D659), D239 (= D661), D241 (= D663)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y434), R280 (≠ K702), G302 (= G724), H303 (= H725), E320 (= E742), S322 (= S744), H324 (= H746), R414 (= R838), S416 (= S840), N417 (= N841), T418 (= T842), R423 (≠ V847)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
33% identity, 49% coverage: 431:863/880 of query aligns to 6:439/448 of 6nolA
- active site: R12 (= R437), S97 (= S525), H98 (= H526), K107 (= K535), D237 (= D659), D239 (= D661), D241 (= D663), R242 (= R664), H324 (= H746)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G724), E320 (= E742), S322 (= S744), H324 (= H746), R414 (= R838), S416 (= S840), N417 (= N841), T418 (= T842), R423 (≠ V847)
- binding magnesium ion: S97 (= S525), D237 (= D659), D239 (= D661), D241 (= D663)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
33% identity, 49% coverage: 431:863/880 of query aligns to 6:439/448 of 6nnpA
- active site: R12 (= R437), S97 (= S525), H98 (= H526), K107 (= K535), D237 (= D659), D239 (= D661), D241 (= D663), R242 (= R664), H324 (= H746)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K702), G302 (= G724), H303 (= H725), E320 (= E742), H324 (= H746), R414 (= R838), S416 (= S840), N417 (= N841), T418 (= T842), R423 (≠ V847)
- binding magnesium ion: S97 (= S525), D237 (= D659), D239 (= D661), D241 (= D663)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
33% identity, 49% coverage: 431:863/880 of query aligns to 6:439/448 of 6nn2A
- active site: R12 (= R437), S97 (= S525), H98 (= H526), K107 (= K535), D237 (= D659), D239 (= D661), D241 (= D663), R242 (= R664), H324 (= H746)
- binding calcium ion: S97 (= S525), D237 (= D659), D239 (= D661), D241 (= D663)
Query Sequence
>GFF3376 FitnessBrowser__Marino:GFF3376
MKLGKKKDADASVDEKPAKKAVKKEKTSSSGPKLKRLNSVAVNQSLVVVLAGVIAVALLH
FLVVQPSAKERFESLKVLEADAAALRLNQYFDQVQKSVNGLATQPHVVQALNSRNEIPTT
EVQLADSLPGIEAVHLFPYRDIPRTSSSEGLLGFSGLELARRAETGQRLFPDAFPRDNRW
FVQMATPVRNPTSNAVIGSLLIIFDSGQIQPLLQVVNSSLGGQLALVQTVSGSPRTVVSN
GSGSGNAESRRLSNPDWTVAYTPAKSSAAPVDTVMIALLVGVPALIAAIIVWVLLGGAQK
GLRQDVTALIQWAHKVFGGERVKLPTFRWDMVASTGEVLYRLSQVVDKRVAKAGETAKPR
PAGSGKAGGGAAKGGDEPLFQDKDMPDIDMLDGDEDVLGFGSGDDTVFGSGDTPDVEEVT
LPQVELPQDIFRAYDIRGIVGETLTAEGVEVIGRAIGSEARERGVDSLCIGYDGRHSSPD
LADALARGVMAAGCNVIHVGAVPTPVLYFATHELQTGSGVMVTGSHNPANYNGLKIMLGG
ETLSGEAIQKLYQRIQTGDFASGRGSQSTEDVRRAYLDRIVGDIAVAAPLKVVVDAGNGI
AGELAPMLIEELGCEVIPLYCEVDGDFPNHHPDPGKPANLADLIARVESEGADIGLAFDG
DGDRLGVVTNSGKIIWPDRLMMLFARDVVSRNPGADVLYDVKCSRRLAGVISEAGGRPIM
WKTGHSLMKAKMKETGALLAGEMSGHIFFGERWYGFDDGLYSAARLLEILGIEDRHSDEV
FEDFPDDISTPELNVQVTESSKFDIIKRLGESGDFGDGNISTIDGIRVDYADGWGLCRAS
NTTPVLVLRFEAETDEALERIKSVFRDQLQKAAPDLVADF
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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