SitesBLAST

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)
34% identity, 70% coverage: 25:98/105 of query aligns to 24:99/104 of P61459

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P61459

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C82 (≠ L81) 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)
34% identity, 70% coverage: 25:98/105 of query aligns to 24:99/104 of P61457

query
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P61457

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T79 (= T78) to I: in HPABH4D; increased proteolytic degradation; reduced interaction with HNF1B; loss of HNF1B-coactivator activity; dbSNP:rs121913014
C82 (≠ L81) 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 (= R87) to Q: no impact on HNF1B interaction; no impact on HNF1B-coactivator activity; dbSNP:rs115117837
E97 (= E96) 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; 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)

1f93A Crystal structure of a complex between the dimerization domain of hnf-1 alpha and the coactivator dcoh (see paper)
34% identity, 70% coverage: 25:98/105 of query aligns to 23:98/103 of 1f93A

query
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1f93A

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active site: E57 (= E57), H61 (= H61), H62 (= H62), H79 (= H79), E80 (= E80), D88 (= D88)
binding : N43 (≠ K43), R44 (≠ E44), G47 (≠ M47), R51 (≠ A51), L54 (≠ Y54)

2v6tB Crystal structure of a complex of pterin-4a-carbinolamine dehydratase from toxoplasma gondii with 7,8-dihydrobiopterin (see paper)
27% identity, 75% coverage: 19:97/105 of query aligns to 14:94/100 of 2v6tB

query
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2v6tB

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active site: D54 (≠ E57), H58 (= H61), H59 (= H62), H76 (= H79), D77 (≠ E80), D85 (= D88)
binding 2-amino-6-(1,2-dihydroxy-propyl)-7,8-dihydro-6h-pteridin-4-one: D57 (≠ W60), H58 (= H61), H59 (= H62), D77 (≠ E80)

Query Sequence

>WP_012992173.1 NCBI__GCF_000025605.1:WP_012992173.1
MSEQQDLKVYLPHEVISLIKEKLPSWSYEEGYLVKEISTKSWKETVMIFNAVAYLAEALW
HHPDVELSFRRVKIKLKTHELNGITDRDFELAGHIEDLLRVKKVL

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