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)
38% identity, 89% coverage: 18:206/213 of query aligns to 16:189/192 of Q9CIV7

query
sites
Q9CIV7

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D29 (= D31) binding Mg(2+)
D34 (= D36) binding Mg(2+)
D36 (= D38) binding Mg(2+)
HGAN 37:40 (≠ HGVN 39:42) binding ADP
AS 78:79 (≠ SM 79:80) binding ADP
R114 (≠ I120) mutation to A: Reduces activity 3-fold.; mutation to E: Reduces activity 100-fold.
G115 (= G121) binding ADP
M124 (≠ L130) binding ADP
R161 (= R178) mutation to A: Loss of activity.
Y164 (≠ R181) mutation to A: Reduces activity about 20-fold.
DPG 174:176 (≠ DAG 191:193) binding ADP

3cr3A Structure of a transient complex between dha-kinase subunits dham and dhal from lactococcus lactis (see paper)
38% identity, 89% coverage: 18:206/213 of query aligns to 16:189/192 of 3cr3A

query
sites
3cr3A

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binding adenosine-5'-diphosphate: D29 (= D31), D34 (= D36), D36 (= D38), H37 (= H39), N40 (= N42), G77 (= G78), A78 (≠ S79), S79 (≠ M80), L82 (= L83), G115 (= G121), A117 (= A123), T123 (= T129), D174 (= D191), P175 (≠ A192), G176 (= G193)
binding magnesium ion: D29 (= D31), D34 (= D36), D34 (= D36), D36 (= D38), D36 (= D38)

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, 79% coverage: 26:193/213 of query aligns to 391:558/575 of Q3LXA3

query
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Q3LXA3

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D401 (= D36) mutation to A: Abolishes both kinase and FMN cyclase activities.
D403 (= D38) mutation to A: Abolishes both kinase and FMN cyclase activities.
C404 (≠ H39) 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 (= S79) 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, 97% coverage: 1:206/213 of query aligns to 350:548/552 of P45510

query
sites
P45510

M

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D380 (= D31) mutation to A: Loss of kinase activity.
D385 (= D36) mutation to A: Loss of kinase activity.
DGDT 385:388 (≠ DGDH 36:39) binding ATP
D387 (= D38) mutation to A: Loss of kinase activity.
T388 (≠ H39) mutation to H: Reduced kinase activity.
SS 431:432 (≠ SM 79:80) binding ATP
G468 (= G121) binding ATP
TM 476:477 (≠ TL 129:130) binding ATP
DPG 533:535 (≠ DAG 191:193) binding ATP

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)
28% identity, 97% coverage: 1:206/213 of query aligns to 350:535/537 of 1un9A

query
sites
1un9A

M

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binding phosphoaminophosphonic acid-adenylate ester: D385 (= D36), D387 (= D38), T388 (≠ H39), T391 (≠ N42), G430 (= G78), S431 (= S79), S432 (≠ M80), L435 (= L83), G468 (= G121), A470 (= A123), T476 (= T129), M477 (≠ L130), D520 (= D191), G522 (= G193)
binding magnesium ion: D380 (= D31), D385 (= D36), D385 (= D36), D387 (= D38), D387 (= D38)

Sites not aligning to the query:

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

Query Sequence

>WP_008507124.1 NCBI__GCF_000182725.1:WP_008507124.1
MQTLNNAKAGDIVLTMAERIVENRAYLSEIDGKIGDGDHGVNMAKGFNMAAERLQGKNET
LAASLDTLGTVLMTEIGGSMGPLYGVMFTEFAEKIDGVDNIDATAFSHMLHAGLEGIQSI
GSAKVGDKTLLDTLVPAVEAFDEANAAGKSFAEALEALVAAAEKGRDSTINLVARIGRAS
RLGERSLGVLDAGATSCAIILKVLGEGARERLQ

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