SitesBLAST

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)
28% identity, 72% coverage: 28:110/115 of query aligns to 28:110/118 of Q02I31

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Q02I31

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Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: Phosphothreonine

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)
33% identity, 77% coverage: 16:104/115 of query aligns to 13:93/104 of P61459

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P61459

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C82 (≠ V93) 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)
33% identity, 77% coverage: 16:104/115 of query aligns to 13:93/104 of P61457

query
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P61457

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T79 (= T90) to I: in HPABH4D; increased proteolytic degradation; reduced interaction with HNF1B; loss of HNF1B-coactivator activity; dbSNP:rs121913014
C82 (≠ V93) 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 (≠ T99) to Q: no impact on HNF1B interaction; no impact on HNF1B-coactivator activity; dbSNP:rs115117837

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)
97 E → K: in HPABH4D; increased proteolytic degradation; loss of HNF1B interaction; loss of HNF1B-coactivator activity; dbSNP:rs397518416
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)
33% identity, 77% coverage: 16:104/115 of query aligns to 8:88/99 of 1dcpA

query
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1dcpA

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active site: E53 (≠ H69), H57 (= H73), H58 (= H74), H75 (= H91), E76 (≠ D92), D84 (= D100)
binding 7,8-dihydrobiopterin: D56 (= D72), H57 (= H73), H58 (= H74), T74 (= T90), H75 (= H91)

1f93A Crystal structure of a complex between the dimerization domain of hnf-1 alpha and the coactivator dcoh (see paper)
33% identity, 77% coverage: 16:104/115 of query aligns to 12:92/103 of 1f93A

query
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1f93A

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active site: E57 (≠ H69), H61 (= H73), H62 (= H74), H79 (= H91), E80 (≠ D92), D88 (= D100)
binding : N43 (≠ F55), R44 (≠ E56), G47 (≠ A59), R51 (≠ A63), L54 (= L66)

Query Sequence

>WP_038217844.1 NCBI__GCF_000745855.1:WP_038217844.1
MSDSMLTIRDWKGVARKALKPSEVVAGLAKLEGWSLRGDGADVAIEKTYRFADYFETIAF
VNALALIAHREDHHPDLSVHYNRCVVRFSTHDVGGISVTDLDCARRADALLMPLR

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