SitesBLAST

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)
37% identity, 98% coverage: 3:208/210 of query aligns to 2:191/192 of Q9CIV7

query
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Q9CIV7

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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

3cr3A Structure of a transient complex between dha-kinase subunits dham and dhal from lactococcus lactis (see paper)
37% identity, 98% coverage: 3:208/210 of query aligns to 2:191/192 of 3cr3A

query
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3cr3A

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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)

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

query
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Q3LXA3

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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)
31% identity, 90% coverage: 19:206/210 of query aligns to 369:548/552 of P45510

query
sites
P45510

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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

1un9A Crystal structure of the dihydroxyacetone kinase from c. Freundii in complex with amp-pnp and mg2+ (see paper)
23% identity, 90% coverage: 19:206/210 of query aligns to 369:535/537 of 1un9A

query
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1un9A

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binding phosphoaminophosphonic acid-adenylate ester: D385 (= D35), D387 (= D37), T388 (≠ H38), T391 (≠ N41), G430 (= G78), S431 (≠ A79), S432 (= S80), L435 (= L83), G468 (= G121), A470 (≠ P123), T476 (= T129), M477 (= M130), D520 (= D191), G522 (= G193)
binding magnesium ion: D380 (= D30), D385 (= D35), D385 (= D35), D387 (= D37), D387 (= D37)

Sites not aligning to the query:

binding Dihydroxyacetone: 57, 61, 83, 109, 114, 220

Query Sequence

>8501868 FitnessBrowser__Miya:8501868
MQITRDHILTWLARLGDIMRDNRTYLTDLDAAIGDADHGINMDRGFSKVQEKLPAFADKD
IGAILKDTGMLLLSTVGGASGPLYGTFFMKAGLAVAGKDTLDAPDVQALLDAGVDGVVSR
GRPVLHDKTMFDAWKPAIDAYRDAVAGGADLLAGLDAAVAAAEDGMRGTIPLQAHKGRAS
YLGERSIGHQDPGATSTVLLLTALRDVVRG

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