SitesBLAST
Comparing GFF2879 FitnessBrowser__Phaeo:GFF2879 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)
2fdrA Crystal structure of conserved haloacid dehalogenase-like protein of unknown function atu0790 from agrobacterium tumefaciens str. C58
33% identity, 95% coverage: 10:219/222 of query aligns to 4:218/222 of 2fdrA
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 81% coverage: 11:189/222 of query aligns to 77:258/1055 of Q8VZ10
- D80 (= D14) mutation to N: Complete rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
Sites not aligning to the query:
- 431:434 CINC→SINS: No rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
- 859 E→K: In soq1-2; high light intensity-dependent and irreversible nonphotochemical quenching (NPQ) due to a decrease in chlorophyll excited-state lifetime.
4eenA Crystal structure of had family hydrolase dr_1622 from deinococcus radiodurans r1 (target efi-501256) with bound magnesium
32% identity, 74% coverage: 11:174/222 of query aligns to 7:170/229 of 4eenA
- active site: D10 (= D14), D12 (= D16), V16 (= V20), S18 (= S22), M44 (≠ D48), Y45 (≠ L49), T47 (≠ V51), S109 (= S113), N110 (= N114), K144 (= K148), E168 (= E172), D169 (= D173)
- binding magnesium ion: D10 (= D14), D12 (= D16), D169 (= D173)
3s6jE The crystal structure of a hydrolase from pseudomonas syringae
30% identity, 81% coverage: 12:191/222 of query aligns to 6:186/220 of 3s6jE
- active site: D8 (= D14), D10 (= D16), S16 (= S22), I44 (≠ F50), T110 (≠ S113), S111 (≠ N114), K143 (= K148), G167 (≠ E172), D168 (= D173)
- binding calcium ion: D8 (= D14), D10 (= D16), D168 (= D173)
P77247 Hexitol phosphatase B; 2-deoxyglucose-6-phosphate phosphatase; Mannitol-1-phosphatase; Sorbitol-6-phosphatase; Sugar-phosphatase; EC 3.1.3.68; EC 3.1.3.22; EC 3.1.3.50; EC 3.1.3.23 from Escherichia coli (strain K12) (see paper)
28% identity, 82% coverage: 7:189/222 of query aligns to 3:189/222 of P77247
- D13 (= D14) binding ; mutation to A: Loss of phosphatase activity.
- D15 (= D16) binding
- D173 (= D173) binding
1te2A Putative phosphatase ynic from escherichia coli k12
28% identity, 80% coverage: 12:189/222 of query aligns to 7:185/218 of 1te2A
- active site: D9 (= D14), D11 (= D16), S17 (= S22), D44 (= D45), S111 (= S113), A112 (≠ N114), K144 (= K148), E168 (= E172), D169 (= D173)
- binding calcium ion: D9 (= D14), D11 (= D16), D169 (= D173)
- binding 2-phosphoglycolic acid: D9 (= D14), M10 (≠ C15), D11 (= D16), G47 (≠ D48), S111 (= S113), A112 (≠ N114), K144 (= K148)
3qypB Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron, glu47asn mutant complexed with calcium and phosphate (see paper)
26% identity, 83% coverage: 9:192/222 of query aligns to 10:195/228 of 3qypB
- active site: D15 (= D14), D17 (= D16), S23 (= S22), N51 (≠ V51), V116 (≠ A112), T117 (≠ S113), K151 (= K148), E175 (= E172), N176 (≠ D173)
- binding calcium ion: D15 (= D14), D17 (= D16), N51 (≠ V51), N176 (≠ D173)
- binding phosphate ion: D15 (= D14), M16 (≠ C15), D17 (= D16), N51 (≠ V51), T117 (≠ S113), G118 (≠ N114)
7ocqA Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
30% identity, 77% coverage: 12:181/222 of query aligns to 13:183/686 of 7ocqA
Sites not aligning to the query:
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonyl-4~{H}-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-3,4,5-tris(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate: 252, 253, 254, 279, 280, 335, 369, 370
7ocnA Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
30% identity, 77% coverage: 12:181/222 of query aligns to 13:183/690 of 7ocnA
7ocpA NADPH bound to the dehydrogenase domain of the bifunctional mannitol- 1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
30% identity, 77% coverage: 12:181/222 of query aligns to 13:183/688 of 7ocpA
Sites not aligning to the query:
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 250, 251, 253, 254, 279, 280, 334, 335, 336, 339, 369, 370
3qu2A Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron, a closed cap conformation (see paper)
26% identity, 83% coverage: 9:192/222 of query aligns to 3:188/221 of 3qu2A
- active site: D8 (= D14), D10 (= D16), S16 (= S22), E44 (≠ V51), V109 (≠ A112), T110 (≠ S113), K144 (= K148), E168 (= E172), N169 (≠ D173)
- binding magnesium ion: D8 (= D14), D10 (= D16), E44 (≠ V51), N169 (≠ D173)
7ocqB Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
29% identity, 77% coverage: 12:181/222 of query aligns to 13:178/679 of 7ocqB
Sites not aligning to the query:
- binding 1,4-dihydronicotinamide adenine dinucleotide: 245, 246, 247, 248, 249, 274, 275, 329, 330, 334, 363, 403, 405, 407, 591, 594
7ocrB NADPH and fructose-6-phosphate bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
29% identity, 77% coverage: 12:181/222 of query aligns to 13:177/675 of 7ocrB
Sites not aligning to the query:
- binding fructose -6-phosphate: 362, 403, 508, 513, 516, 587, 590, 594, 595, 601
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 244, 246, 247, 248, 273, 274, 329, 330, 333, 361, 362, 406, 587, 590
7ocsC Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld-d16a from acinetobacter baumannii (see paper)
29% identity, 77% coverage: 12:181/222 of query aligns to 13:183/572 of 7ocsC
- binding D-Mannitol-1-phosphate: M16 (≠ C15), D17 (= D16), E24 (= E23), R27 (≠ S26), L31 (= L30), C51 (= C46), L52 (≠ M47), G53 (= G52), L54 (≠ G53), R77 (vs. gap), T117 (≠ S113), S118 (≠ N114), K150 (= K148)
7ocsA Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld-d16a from acinetobacter baumannii (see paper)
29% identity, 77% coverage: 12:181/222 of query aligns to 13:183/682 of 7ocsA
- binding D-Mannitol-1-phosphate: M16 (≠ C15), D17 (= D16), E24 (= E23), R27 (≠ S26), L31 (= L30), C51 (= C46), L52 (≠ M47), L54 (≠ G53), T117 (≠ S113), S118 (≠ N114), K150 (= K148)
Sites not aligning to the query:
4g9bA Crystal structure of beta-phosphoglucomutase homolog from escherichia coli, target efi-501172, with bound mg, open lid
32% identity, 57% coverage: 91:217/222 of query aligns to 95:213/227 of 4g9bA
Sites not aligning to the query:
P95649 Protein CbbY; RuCbby; EC 3.1.3.- from Cereibacter sphaeroides (Rhodobacter sphaeroides) (see paper)
27% identity, 81% coverage: 11:189/222 of query aligns to 5:192/230 of P95649
- D10 (= D16) mutation to N: Loss of catalytic activity.
- E17 (= E23) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- H20 (≠ S26) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- Y42 (≠ C46) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- R54 (vs. gap) mutation to A: 97% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- K78 (≠ Y78) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
4uasA Crystal structure of cbby from rhodobacter sphaeroides in complex with phosphate (see paper)
27% identity, 81% coverage: 11:189/222 of query aligns to 5:192/225 of 4uasA
- active site: D8 (= D14), V9 (≠ C15), D10 (= D16), T16 (≠ S22), T47 (≠ V51), T115 (≠ S113), T116 (≠ N114), K151 (= K148), E175 (= E172), D176 (= D173)
- binding magnesium ion: D8 (= D14), D10 (= D16), D176 (= D173)
- binding phosphate ion: D8 (= D14), V9 (≠ C15), D10 (= D16), T115 (≠ S113), T116 (≠ N114), K151 (= K148)
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
27% identity, 82% coverage: 9:190/222 of query aligns to 3:187/221 of P71447
- D8 (= D14) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
- D10 (= D16) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
- T16 (≠ S22) mutation to P: 500-fold reduction in the rate constant for Asp-8 phosphorylation by beta-G1,6bisP. 6,700-fold reduction in the apparent rate constant for cycling of the phosphorylated enzyme to convert beta-G1P to G6P. 13-fold increase in the estimated rate constant for phosphoryl transfer from the phospho-Asp8 to water.
- H20 (vs. gap) mutation to A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P.; mutation to N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.; mutation to Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- K45 (≠ D48) mutation to A: 20'000-fold decrease in kcat/KM.
- G46 (= G52) mutation to A: 1'000'000-fold decrease in kcat/KM.; mutation to P: 100'000-fold decrease in kcat/KM.; mutation to V: 10'000-fold decrease in kcat/KM.
- R49 (≠ M55) mutation to K: 1'000'000-fold decrease in kcat/KM.
- S52 (≠ V58) mutation to A: Wild-type activity.
- K76 (≠ Y78) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- D170 (= D173) mutation to A: Impaired, but active with an increase in the affinity for G1P.
5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
26% identity, 82% coverage: 9:190/222 of query aligns to 3:187/224 of 5olwA
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ D48), S114 (= S113), A115 (≠ N114), K145 (= K148), E169 (= E172), D170 (= D173)
- binding calcium ion: D8 (= D14), D10 (= D16), P89 (vs. gap), V92 (≠ L91), E124 (≠ D118), N127 (≠ R121), E169 (= E172), D170 (= D173), S171 (= S174)
Query Sequence
>GFF2879 FitnessBrowser__Phaeo:GFF2879
MPITYPTPKLVIFDCDGVLVDSETLSNQVLVENLGRHGLQLSLADCMDLFVGGTMQGVMK
KAQELGADLPANWVDEVYGETYARLRQGVDLVPGIPDLLALLQARGIAFCVASNGSEDKM
RITLGQNGLWDQFHPQAMFSAHTLKTGKPDPDLFLAAACHFDVQARDCLVIEDSENGAIA
AARAGMRCLGFDPHGKGTRLKRHNAEHITAMSEVPRLIGLRP
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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