SitesBLAST
Comparing 206412 MicrobesOnline__882:206412 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
P76014 PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL; EC 2.7.1.121 from Escherichia coli (strain K12) (see 3 papers)
55% identity, 97% coverage: 1:204/210 of query aligns to 1:204/210 of P76014
4lrzA Crystal structure of the e.Coli dhar(n)-dhal complex (see paper)
55% identity, 96% coverage: 3:204/210 of query aligns to 4:205/211 of 4lrzA
- binding adenosine-5'-diphosphate: D31 (= D30), D36 (= D35), D38 (= D37), H39 (= H38), G79 (= G78), A80 (= A79), S81 (= S80), L84 (= L83), G122 (= G121), T130 (= T129), M131 (= M130), G178 (= G177), D192 (= D191), P193 (= P192), G194 (= G193)
- binding magnesium ion: D31 (= D30), D36 (= D35), D36 (= D35), D38 (= D37), D38 (= D37)
3cr3A Structure of a transient complex between dha-kinase subunits dham and dhal from lactococcus lactis (see paper)
39% identity, 98% coverage: 3:208/210 of query aligns to 2:191/192 of 3cr3A
- binding adenosine-5'-diphosphate: D29 (= D30), D34 (= D35), D36 (= D37), H37 (= H38), N40 (= N41), G77 (= G78), A78 (= A79), S79 (= S80), L82 (= L83), G115 (= G121), A117 (≠ P123), T123 (= T129), D174 (= D191), P175 (= P192), G176 (= G193)
- binding magnesium ion: D29 (= D30), D34 (= D35), D34 (= D35), D36 (= D37), D36 (= D37)
Q9CIV7 PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL; EC 2.7.1.121 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see paper)
39% identity, 98% coverage: 3:208/210 of query aligns to 2:191/192 of Q9CIV7
- D29 (= D30) binding
- D34 (= D35) binding
- D36 (= D37) binding
- HGAN 37:40 (≠ HGIN 38:41) binding
- AS 78:79 (= AS 79:80) binding
- R114 (= R120) mutation to A: Reduces activity 3-fold.; mutation to E: Reduces activity 100-fold.
- G115 (= G121) binding
- M124 (= M130) binding
- R161 (= R178) mutation to A: Loss of activity.
- Y164 (= Y181) mutation to A: Reduces activity about 20-fold.
- DPG 174:176 (= DPG 191:193) binding
Q3LXA3 Triokinase/FMN cyclase; Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing); EC 2.7.1.28; EC 2.7.1.29; EC 4.6.1.15 from Homo sapiens (Human) (see 4 papers)
32% identity, 87% coverage: 12:193/210 of query aligns to 378:558/575 of Q3LXA3
- D401 (= D35) mutation to A: Abolishes both kinase and FMN cyclase activities.
- D403 (= D37) mutation to A: Abolishes both kinase and FMN cyclase activities.
- C404 (≠ H38) mutation to A: Decreases both kinase and FMN cyclase activities.
- G445 (= G78) to S: in TKFCD; very severe decrease of triokinase and glycerone kinase activities; dbSNP:rs1590578831
- S446 (≠ A79) mutation to A: Decreases both kinase and FMN cyclase activities.
- R543 (= R178) to I: in TKFCD; reduced protein levels in patient cells; very severe decrease of triokinase and glycerone kinase activities; dbSNP:rs547013163
- D556 (= D191) mutation to A: Abolishes both kinase and FMN cyclase activities.
Sites not aligning to the query:
- 112 T→A: Highly decreases kinase activity. No effect on FMN cyclase activity.
- 185 A → T: in dbSNP:rs2260655
- 204 K→A: Slightly decreases kinase activity. No effect on FMN cyclase activity.
- 221 H→A: Abolishes kinase activity but not FMN cyclase activity.
P45510 Dihydroxyacetone kinase; DHA kinase; Glycerone kinase; EC 2.7.1.29 from Citrobacter freundii (see 2 papers)
30% identity, 88% coverage: 23:206/210 of query aligns to 373:548/552 of P45510
- D380 (= D30) mutation to A: Loss of kinase activity.
- D385 (= D35) mutation to A: Loss of kinase activity.
- DGDT 385:388 (≠ DADH 35:38) binding
- D387 (= D37) mutation to A: Loss of kinase activity.
- T388 (≠ H38) mutation to H: Reduced kinase activity.
- SS 431:432 (≠ AS 79:80) binding
- G468 (= G121) binding
- TM 476:477 (= TM 129:130) binding
- DPG 533:535 (= DPG 191:193) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 220 active site, Tele-hemiaminal-histidine intermediate
Query Sequence
>206412 MicrobesOnline__882:206412
MQLTRKHVLTWLARLGDIMRENKAYLTDLDAAIGDADHGINMDRGFGKVQEKLAAFEDKD
IGAILKDTGMVLLSSVGGASGPLYGTFFMKAGLAVAGKDTLDATETLTMLEAGVAGLVSR
GRPVLQDKTMYDAWAPALDAFRAALGKGDDLALALDAAVDAAGEGMRATIPMQARKGRAS
YLGERSIGHQDPGATSTVFMLTALRDVVRG
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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