SitesBLAST

active site: E57 (= E55), H61 (= H59), H62 (= H60), H79 (= H77), E80 (≠ D78), D88 (= D86)
binding : N43 (≠ T41), R44 (≠ E42), G47 (≠ A45), R51 (≠ G49), L54 (= L52)

P61459 Pterin-4-alpha-carbinolamine dehydratase; PHS; 4-alpha-hydroxy-tetrahydropterin dehydratase; Dimerization cofactor of hepatocyte nuclear factor 1-alpha; DCoH; Dimerization cofactor of HNF1; Phenylalanine hydroxylase-stimulating protein; Pterin carbinolamine dehydratase; PCD; EC 4.2.1.96 from Rattus norvegicus (Rat) (see 2 papers)
55% identity, 99% coverage: 2:97/97 of query aligns to 5:100/104 of P61459

query
sites
P61459

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C82 (≠ V79) mutation to R: Reduced dehydratase activity. No impact on hydroxytetrahydrobiopterin-binding.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine

P61457 Pterin-4-alpha-carbinolamine dehydratase; PHS; 4-alpha-hydroxy-tetrahydropterin dehydratase; Dimerization cofactor of hepatocyte nuclear factor 1-alpha; DCoH; Dimerization cofactor of HNF1; Phenylalanine hydroxylase-stimulating protein; Pterin carbinolamine dehydratase; PCD; EC 4.2.1.96 from Homo sapiens (Human) (see 6 papers)
55% identity, 99% coverage: 2:97/97 of query aligns to 5:100/104 of P61457

query
sites
P61457

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T79 (= T76) to I: in HPABH4D; increased proteolytic degradation; reduced interaction with HNF1B; loss of HNF1B-coactivator activity; dbSNP:rs121913014
C82 (≠ V79) to R: in HPABH4D; increased proteolytic degradation; reduced dehydratase activity; no impact on hydroxytetrahydrobiopterin-binding; reduced interaction with HNF1B; partial impact on HNF1B-coactivator activity; dbSNP:rs104894177
R88 (≠ L85) to Q: in HPABH4D; when associated in cis with 27-E--T-104 del; uncertain significance; no impact on HNF1B interaction; no impact on HNF1B-coactivator activity; dbSNP:rs115117837
E97 (≠ D94) to K: in HPABH4D; increased proteolytic degradation; loss of HNF1B interaction; loss of HNF1B-coactivator activity; dbSNP:rs397518416

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
27:104 natural variant: Missing (in HPABH4D; when associated in cis with Q-88; reduced protein levels; loss of HNF1B interaction; loss of HNF1B-coactivator activity; dbSNP:rs727505360)
87:104 natural variant: Missing (in HPABH4D; increased proteolytic degradation; loss of HNF1B interaction; loss of HNF1B-coactivator activity; dbSNP:rs104894172)
98:104 natural variant: Missing (in HPABH4D; increased proteolytic degradation; loss of HNF1B interaction; loss of HNF1B-coactivator activity; dbSNP:rs121913015)

1dcpA Dcoh, a bifunctional protein-binding transcriptional coactivator, complexed with biopterin (see paper)
55% identity, 98% coverage: 3:97/97 of query aligns to 1:95/99 of 1dcpA

query
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1dcpA

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active site: E53 (= E55), H57 (= H59), H58 (= H60), H75 (= H77), E76 (≠ D78), D84 (= D86)
binding 7,8-dihydrobiopterin: D56 (= D58), H57 (= H59), H58 (= H60), T74 (= T76), H75 (= H77)

2v6tB Crystal structure of a complex of pterin-4a-carbinolamine dehydratase from toxoplasma gondii with 7,8-dihydrobiopterin (see paper)
53% identity, 78% coverage: 22:97/97 of query aligns to 21:96/100 of 2v6tB

query
sites
2v6tB

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active site: D54 (≠ E55), H58 (= H59), H59 (= H60), H76 (= H77), D77 (= D78), D85 (= D86)
binding 2-amino-6-(1,2-dihydroxy-propyl)-7,8-dihydro-6h-pteridin-4-one: D57 (= D58), H58 (= H59), H59 (= H60), D77 (= D78)

Q02I31 Putative pterin-4-alpha-carbinolamine dehydratase; PHS; 4-alpha-hydroxy-tetrahydropterin dehydratase; Pterin carbinolamine dehydratase; PCD; EC 4.2.1.96 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
33% identity, 90% coverage: 11:97/97 of query aligns to 21:111/118 of Q02I31

query
sites
Q02I31

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Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: Phosphothreonine

Query Sequence

>3606703 FitnessBrowser__Dino:3606703
MAQKLDDSTRDEHLAPLMRAGWEMVEGRDAIKKTFVFGDFTEAFAFMTGTALWAEKWDHH
PEWSNVYKTVEVTLTTHDVGGLSELDIKLASKMDNLA

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