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Conserved domains on  [gi|71037697|gb|AAZ18005|]
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pterin-4-alpha-carbinolamine dehydratase [Psychrobacter arcticus 273-4]

Protein Classification

4a-hydroxytetrahydrobiopterin dehydratase( domain architecture ID 10788442)

4a-hydroxytetrahydrobiopterin dehydratase catalyzes the conversion from (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin to (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin in tetrahydrobiopterin biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhhB COG2154
Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];
4-93 9.76e-42

Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];


:

Pssm-ID: 441757  Cd Length: 99  Bit Score: 131.87  E-value: 9.76e-42
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697  4 LSNQQVDLQLEELPGWQRDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVR 83
Cdd:COG2154  6 LTDEEIAAALAELPGWELEDGALERTFKFKDFAEALAFVNRVAELAEAEDHHPDISNRYNRVTVTLTTHDAGGLTENDFI 85

                       90
               ....*....|
gi 71037697 84 LAKRMEHIVQ 93
Cdd:COG2154 86 LAAKIDALAA 95
 
Name Accession Description Interval E-value
PhhB COG2154
Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];
4-93 9.76e-42

Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];


Pssm-ID: 441757  Cd Length: 99  Bit Score: 131.87  E-value: 9.76e-42
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697  4 LSNQQVDLQLEELPGWQRDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVR 83
Cdd:COG2154  6 LTDEEIAAALAELPGWELEDGALERTFKFKDFAEALAFVNRVAELAEAEDHHPDISNRYNRVTVTLTTHDAGGLTENDFI 85

                       90
               ....*....|
gi 71037697 84 LAKRMEHIVQ 93
Cdd:COG2154 86 LAAKIDALAA 95
PCD_DCoH_subfamily_b cd00914
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 18-91 1.89e-40

PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein). Two DCoH proteins have been identifed in humans: DCoH1 and DCoH2. Mutations in human DCoH1 cause hyperphenylalaninemia. Loss of enzymic activity of DCoH in humans is associated with the depigmentation disorder vitiligo. DCoH1 has been reported to be overexpessed in colon cancer carcinomas and in malignant melanomas.


Pssm-ID: 238456  Cd Length: 76  Bit Score: 128.11  E-value: 1.89e-40
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71037697 18 GW--QRDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVRLAKRMEHI 91
Cdd:cd00914  1 GWtlVDGRDAIHKSFKFKDFNEAFGFMTRVALEAEKMNHHPEWFNVYNKVDITLTTHDAGGLTERDIKLAKFIEKA 76
phhB PRK00823
pterin-4-alpha-carbinolamine dehydratase; Validated
 1-93 8.69e-38

pterin-4-alpha-carbinolamine dehydratase; Validated


Pssm-ID: 234845  Cd Length: 97  Bit Score: 121.87  E-value: 8.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697   1 MSSLSNQQVDLQLEELPGWQRDGN--AIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGIT 78
Cdd:PRK00823  3 AEKLSDEEIAELLPQLPGWTLVGDrdAIERTFKFKNFNEAFAFMNRVAEIAEEEDHHPDWFNVYNRVTVTLTTHDAGGLT 82

                        90
                ....*....|....*
gi 71037697  79 SHDVRLAKRMEHIVQ 93
Cdd:PRK00823 83 ENDFILAAKIDALAG 97
Pterin_4a pfam01329
Pterin 4 alpha carbinolamine dehydratase; Pterin 4 alpha carbinolamine dehydratase is also ...
 4-89 6.58e-37

Pterin 4 alpha carbinolamine dehydratase; Pterin 4 alpha carbinolamine dehydratase is also known as DCoH (dimerization cofactor of hepatocyte nuclear factor 1-alpha).


Pssm-ID: 460161  Cd Length: 88  Bit Score: 119.50  E-value: 6.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697    4 LSNQQVDLQLEELPGWQ-RDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDV 82
Cdd:pfam01329  1 LTEEEIEAALAELPGWKlGDGGALERTFKFKDFKEAIAFVNRVALLAEAEGHHPDITNVYNKVTVTLTTHDAGGLTENDF 80


                 ....*..
gi 71037697   83 RLAKRME 89
Cdd:pfam01329 81 ILAAKID 87
 
Name Accession Description Interval E-value
PhhB COG2154
Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];
4-93 9.76e-42

Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];


Pssm-ID: 441757  Cd Length: 99  Bit Score: 131.87  E-value: 9.76e-42
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697  4 LSNQQVDLQLEELPGWQRDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVR 83
Cdd:COG2154  6 LTDEEIAAALAELPGWELEDGALERTFKFKDFAEALAFVNRVAELAEAEDHHPDISNRYNRVTVTLTTHDAGGLTENDFI 85

                       90
               ....*....|
gi 71037697 84 LAKRMEHIVQ 93
Cdd:COG2154 86 LAAKIDALAA 95
PCD_DCoH_subfamily_b cd00914
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 18-91 1.89e-40

PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein). Two DCoH proteins have been identifed in humans: DCoH1 and DCoH2. Mutations in human DCoH1 cause hyperphenylalaninemia. Loss of enzymic activity of DCoH in humans is associated with the depigmentation disorder vitiligo. DCoH1 has been reported to be overexpessed in colon cancer carcinomas and in malignant melanomas.


Pssm-ID: 238456  Cd Length: 76  Bit Score: 128.11  E-value: 1.89e-40
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71037697 18 GW--QRDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVRLAKRMEHI 91
Cdd:cd00914  1 GWtlVDGRDAIHKSFKFKDFNEAFGFMTRVALEAEKMNHHPEWFNVYNKVDITLTTHDAGGLTERDIKLAKFIEKA 76
phhB PRK00823
pterin-4-alpha-carbinolamine dehydratase; Validated
 1-93 8.69e-38

pterin-4-alpha-carbinolamine dehydratase; Validated


Pssm-ID: 234845  Cd Length: 97  Bit Score: 121.87  E-value: 8.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697   1 MSSLSNQQVDLQLEELPGWQRDGN--AIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGIT 78
Cdd:PRK00823  3 AEKLSDEEIAELLPQLPGWTLVGDrdAIERTFKFKNFNEAFAFMNRVAEIAEEEDHHPDWFNVYNRVTVTLTTHDAGGLT 82

                        90
                ....*....|....*
gi 71037697  79 SHDVRLAKRMEHIVQ 93
Cdd:PRK00823 83 ENDFILAAKIDALAG 97
Pterin_4a pfam01329
Pterin 4 alpha carbinolamine dehydratase; Pterin 4 alpha carbinolamine dehydratase is also ...
 4-89 6.58e-37

Pterin 4 alpha carbinolamine dehydratase; Pterin 4 alpha carbinolamine dehydratase is also known as DCoH (dimerization cofactor of hepatocyte nuclear factor 1-alpha).


Pssm-ID: 460161  Cd Length: 88  Bit Score: 119.50  E-value: 6.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71037697    4 LSNQQVDLQLEELPGWQ-RDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDV 82
Cdd:pfam01329  1 LTEEEIEAALAELPGWKlGDGGALERTFKFKDFKEAIAFVNRVALLAEAEGHHPDITNVYNKVTVTLTTHDAGGLTENDF 80


                 ....*..
gi 71037697   83 RLAKRME 89
Cdd:pfam01329 81 ILAAKID 87
PCD_DCoH cd00488
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 18-91 3.02e-32

PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein). Two DCoH proteins have been identifed in humans: DCoH1 and DCoH2. Mutations in human DCoH1 cause hyperphenylalaninemia. Loss of enzymic activity of DCoH in humans is associated with the depigmentation disorder vitiligo. DCoH1 has been reported to be overexpessed in colon cancer carcinomas and in malignant melanomas.


Pssm-ID: 238272  Cd Length: 75  Bit Score: 107.22  E-value: 3.02e-32
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71037697 18 GWQR-DGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVRLAKRMEHI 91
Cdd:cd00488  1 GWELaDGDALERTFKFKDFKEAIAFVNRVAELAEALNHHPDISNVYNKVTVTLTTHDAGGLTENDFILAAKIDAL 75
PCD_DCoH_subfamily_a cd00913
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 18-91 5.72e-14

PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known as DCoH (dimerization cofactor of hepatocyte nuclear factor-1), is both a transcription activator and a metabolic enzyme. DCoH stimulates gene expression by associating with specific DNA binding proteins such as HNF-1alpha (hepatocyte nuclear factor-1) and Xenopus enhancer of rudimentary homologue (XERH). DCoH also catalyzes the dehydration of 4alpha- hydroxy- tetrahydrobiopterin (4alpha-OH-BH4) to quinoiddihydrobiopterin, a percursor of the phenylalanine hydroxylase cofactor BH4 (tetrahydrobiopterin). The DCoH homodimer has a saddle-shaped structure similar to that of TBP (TATA binding protein).


Pssm-ID: 238455  Cd Length: 76  Bit Score: 61.09  E-value: 5.72e-14
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71037697 18 GWQ--RDGNAIVKTYHFSDFVEAMSFMNQAAFHAEALEHHPEWSNAYNVVEVRLTTGDTGGITSHDVRLAKRMEHI 91
Cdd:cd00913  1 GWElaDDGLKLERTFRFKNFVEALEFVNAVGEIAEAEGHHPDLSLGWGRVRVTWWTHSIGGLSENDFIMAAKIDAL 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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