SitesBLAST
Comparing WP_071387277.1 NCBI__GCF_000967895.1:WP_071387277.1 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)
49% identity, 55% coverage: 379:831/831 of query aligns to 12:463/463 of P26276
- R15 (= R382) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y384) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R387) mutation to A: No phosphoglucomutase activity.
- S108 (= S475) 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 (= N477) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D609) binding Mg(2+)
- D244 (= D611) binding Mg(2+)
- D246 (= D613) binding Mg(2+)
- R247 (≠ S614) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (= R629) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K652) binding alpha-D-glucose 1-phosphate
- H308 (≠ Q675) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E692) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ ELSGH 692:696) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H696) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P735) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R789) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (= RASNT 789:793) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
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)
49% identity, 55% coverage: 379:831/831 of query aligns to 12:463/463 of Q02E40
- S108 (= S475) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 7:458/458 of 1pcjX
- active site: R15 (= R387), S103 (= S475), H104 (= H476), K113 (= K485), D237 (= D609), D239 (= D611), D241 (= D613), R242 (≠ S614), H324 (= H696), D335 (= D707)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y384), S103 (= S475), T301 (= T673), G302 (= G674), E320 (= E692), S322 (= S694), H324 (= H696), R416 (= R789), S418 (= S791), N419 (= N792), T420 (= T793)
- binding zinc ion: S103 (= S475), D237 (= D609), D239 (= D611), D241 (= D613)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 4:455/455 of 2h5aX
- active site: H101 (= H476), D234 (= D609), D236 (= D611), D238 (= D613), R239 (≠ S614), D332 (= D707)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y384), T298 (= T673), G299 (= G674), H300 (≠ Q675), E317 (= E692), S319 (= S694), H321 (= H696), R413 (= R789), S415 (= S791), N416 (= N792), T417 (= T793)
- binding zinc ion: S100 (= S475), D234 (= D609), D236 (= D611), D238 (= D613)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 4:455/455 of 2h4lX
- active site: H101 (= H476), D234 (= D609), D236 (= D611), D238 (= D613), R239 (≠ S614), D332 (= D707)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y384), R12 (= R387), S100 (= S475), T298 (= T673), E317 (= E692), R413 (= R789), S415 (= S791), N416 (= N792), T417 (= T793)
- binding zinc ion: S100 (= S475), D234 (= D609), D236 (= D611), D238 (= D613)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 4:455/455 of 2fkfA
- active site: R12 (= R387), S100 (= S475), H101 (= H476), K110 (= K485), D234 (= D609), D236 (= D611), D238 (= D613), R239 (≠ S614), H321 (= H696), D332 (= D707)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R382), H101 (= H476), S319 (= S694), R413 (= R789), S415 (= S791), N416 (= N792), T417 (= T793)
- binding zinc ion: S100 (= S475), D234 (= D609), D236 (= D611), D238 (= D613)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 4:455/455 of 1pcmX
- active site: R12 (= R387), S100 (= S475), H101 (= H476), K110 (= K485), D234 (= D609), D236 (= D611), D238 (= D613), R239 (≠ S614), H321 (= H696), D332 (= D707)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y384), S100 (= S475), T298 (= T673), G299 (= G674), H300 (≠ Q675), E317 (= E692), S319 (= S694), H321 (= H696), R413 (= R789), S415 (= S791)
- binding zinc ion: S100 (= S475), D234 (= D609), D236 (= D611), D238 (= D613)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 4:455/455 of 1p5gX
- active site: R12 (= R387), S100 (= S475), H101 (= H476), K110 (= K485), D234 (= D609), D236 (= D611), D238 (= D613), R239 (≠ S614), H321 (= H696), D332 (= D707)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y384), S100 (= S475), K277 (= K652), G299 (= G674), H300 (≠ Q675), E317 (= E692), S319 (= S694), H321 (= H696), R413 (= R789), S415 (= S791), N416 (= N792), T417 (= T793)
- binding zinc ion: S100 (= S475), D234 (= D609), D236 (= D611), D238 (= D613)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 4:455/455 of 1p5dX
- active site: R12 (= R387), S100 (= S475), H101 (= H476), K110 (= K485), D234 (= D609), D236 (= D611), D238 (= D613), R239 (≠ S614), H321 (= H696), D332 (= D707)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y384), S100 (= S475), R239 (≠ S614), T298 (= T673), G299 (= G674), H300 (≠ Q675), E317 (= E692), S319 (= S694), H321 (= H696), R413 (= R789), S415 (= S791), T417 (= T793)
- binding zinc ion: S100 (= S475), D234 (= D609), D236 (= D611), D238 (= D613)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 8:459/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
49% identity, 55% coverage: 379:831/831 of query aligns to 8:459/459 of 4il8A
- active site: R16 (= R387), S104 (= S475), H105 (= H476), K114 (= K485), D238 (= D609), D240 (= D611), D242 (= D613), R243 (≠ S614), A325 (≠ H696), D336 (= D707)
- binding magnesium ion: S104 (= S475), D238 (= D609), D240 (= D611), D242 (= D613)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
47% identity, 55% coverage: 379:831/831 of query aligns to 1:436/436 of 3rsmA
- active site: C87 (≠ S475), K91 (= K485), D215 (= D609), D217 (= D611), D219 (= D613), R220 (≠ S614), H302 (= H696), D313 (= D707)
- binding phosphate ion: C87 (≠ S475), D215 (= D609), D217 (= D611), D219 (= D613), R220 (≠ S614)
- binding zinc ion: D215 (= D609), D217 (= D611), D219 (= D613)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
45% identity, 55% coverage: 376:831/831 of query aligns to 2:458/458 of 3uw2A
- active site: R13 (= R387), S109 (= S475), H110 (= H476), K119 (= K485), D243 (= D609), D245 (= D611), D247 (= D613), R248 (≠ S614), H330 (= H696)
- binding zinc ion: D243 (= D609), D245 (= D611), D247 (= D613)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
34% identity, 53% coverage: 381:822/831 of query aligns to 7:448/449 of 6mlwA
- active site: R13 (= R387), S98 (= S475), H99 (= H476), K108 (= K485), D238 (= D609), D240 (= D611), D242 (= D613), R243 (≠ S614), H325 (= H696)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G674), H304 (≠ Q675), E321 (= E692), S323 (= S694), H325 (= H696), R415 (= R789), S417 (= S791), N418 (= N792), T419 (= T793), R424 (≠ T798)
- binding magnesium ion: S98 (= S475), D238 (= D609), D240 (= D611), D242 (= D613)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
34% identity, 53% coverage: 381:822/831 of query aligns to 7:448/449 of 5bmpA
- active site: R13 (= R387), S98 (= S475), H99 (= H476), K108 (= K485), D238 (= D609), D240 (= D611), D242 (= D613), R243 (≠ S614), H325 (= H696)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ K652), G303 (= G674), E321 (= E692), S323 (= S694), H325 (= H696), R415 (= R789), S417 (= S791), N418 (= N792), T419 (= T793), R424 (≠ T798)
- binding magnesium ion: S98 (= S475), D238 (= D609), D240 (= D611), D242 (= D613)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
34% identity, 53% coverage: 381:822/831 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R387), S97 (= S475), H98 (= H476), K107 (= K485), D237 (= D609), D239 (= D611), D241 (= D613), R242 (≠ S614), H324 (= H696)
- binding magnesium ion: D237 (= D609), D239 (= D611), D241 (= D613)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R387), S97 (= S475), H98 (= H476), K107 (= K485), D239 (= D611), R242 (≠ S614), R280 (≠ K652), S301 (≠ T673), G302 (= G674), E320 (= E692), S322 (= S694), H324 (= H696), R414 (= R789), S416 (= S791), N417 (= N792), T418 (= T793), R423 (≠ T798)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
34% identity, 53% coverage: 381:822/831 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R387), S97 (= S475), H98 (= H476), K107 (= K485), D237 (= D609), D239 (= D611), D241 (= D613), R242 (≠ S614), H324 (= H696)
- binding calcium ion: S97 (= S475), D237 (= D609), D239 (= D611), D241 (= D613)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y384), R280 (≠ K652), G302 (= G674), H303 (≠ Q675), E320 (= E692), S322 (= S694), H324 (= H696), R414 (= R789), S416 (= S791), N417 (= N792), T418 (= T793), R423 (≠ T798)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
34% identity, 53% coverage: 381:822/831 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R387), S97 (= S475), H98 (= H476), K107 (= K485), D237 (= D609), D239 (= D611), D241 (= D613), R242 (≠ S614), H324 (= H696)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G674), E320 (= E692), S322 (= S694), H324 (= H696), R414 (= R789), S416 (= S791), N417 (= N792), T418 (= T793), R423 (≠ T798)
- binding magnesium ion: S97 (= S475), D237 (= D609), D239 (= D611), D241 (= D613)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
34% identity, 53% coverage: 381:822/831 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R387), S97 (= S475), H98 (= H476), K107 (= K485), D237 (= D609), D239 (= D611), D241 (= D613), R242 (≠ S614), H324 (= H696)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K652), G302 (= G674), H303 (≠ Q675), E320 (= E692), H324 (= H696), R414 (= R789), S416 (= S791), N417 (= N792), T418 (= T793), R423 (≠ T798)
- binding magnesium ion: S97 (= S475), D237 (= D609), D239 (= D611), D241 (= D613)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
34% identity, 53% coverage: 381:822/831 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R387), S97 (= S475), H98 (= H476), K107 (= K485), D237 (= D609), D239 (= D611), D241 (= D613), R242 (≠ S614), H324 (= H696)
- binding calcium ion: S97 (= S475), D237 (= D609), D239 (= D611), D241 (= D613)
Query Sequence
>WP_071387277.1 NCBI__GCF_000967895.1:WP_071387277.1
MKAPQRTLAFYNRLGIWVALLFISLGLSMQSLQVNLFAQATLDKEYAHAMAQQMAQSLRV
KLAETQMQQKNAARHSQTIAYLDQEDLSWKRTLKSLITGAEQILILDNLSALGLQDKLGY
AVQELATNTLKGKEFPLEAVQLNGEIHFYLATPIKDYTQTIKGILLIEYGTDWLDQLRQG
AAAKHGLISTRQVLKDDPSKGLQVFEIGAKSASRLTIVTESINDYWFLTFIPADTRPQLA
TTSIVTPWIVALLGTLITLFIITWLQKREVDYNQLMLLNYVRQLFRKGENKWPNFNIKIF
HDVAKAMEHLAHSKGMIQSAEENHAPIAAREKQKIDLTQPTNKSLTSNTASRAVSKHSSA
PIPQVMVEEVEHDTAVAHSIFRAYDIRGTVNDNLTPDVAEQIGLALGSELLIRGESKIVL
GWDGRLSSPELAAALQKGLLSTGCNVINIGSVVTGMMYYACHELDTTNGIIVTGSHNDSS
LNGFKIIINRQTLIKESLMALYHRIQRKDFRTGQGLIEEKNISHDYLDRIQSDIQLSRPL
KVVFDAGNGIAGPIGLKLLKTMGLEVVPLFCNVDGNFPNHKPNPSDPKSLIALQQAVVEQ
GADLGIAVDGDGDSIGLVDEKGSIIMPDRILMLLAKDIISRHPGCDVIYDIKSSRRLNQV
IAQCGGRPTMWKTGQSLMKAKMEELQATLGGELSGHIYFRDRWYGFDDSLYVSARLLELL
SHQLDTVSEIFSEFPDDVSTDEITINTDNKSKFDIIQKLASEPSLQQGARVSTIDGIRSD
FQDGWGLIRASNTSPKLTLRFAGDNNDALLRIQLLYKDALLRHAPGLNIPF
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