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Conserved domains on  [gi|1018443291|ref|NP_001309933|]
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pterin-4-alpha-carbinolamine dehydratase isoform 2 [Homo sapiens]

Protein Classification

4a-hydroxytetrahydrobiopterin dehydratase family protein( domain architecture ID 2568)

4a-hydroxytetrahydrobiopterin dehydratase family protein such as 4a-hydroxytetrahydrobiopterin dehydratase that 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; may be partial

CATH:  3.30.1360.20
EC:  4.2.1.96
Gene Ontology:  GO:0008124|GO:0006729
PubMed:  10727395|8590013
SCOP:  4001463

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PCD_DCoH super family cl00942
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 24-74 2.12e-35

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.


The actual alignment was detected with superfamily member cd00914:

Pssm-ID: 470002  Cd Length: 76  Bit Score: 115.40  E-value: 2.12e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1018443291  24 GWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVS 74
Cdd:cd00914     1 GWTLVDGRDAIHKSFKFKDFNEAFGFMTRVALEAEKMNHHPEWFNVYNKVD 51
 
Name Accession Description Interval E-value
PCD_DCoH_subfamily_b cd00914
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 24-74 2.12e-35

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: 115.40  E-value: 2.12e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1018443291  24 GWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVS 74
Cdd:cd00914     1 GWTLVDGRDAIHKSFKFKDFNEAFGFMTRVALEAEKMNHHPEWFNVYNKVD 51
phhB PRK00823
pterin-4-alpha-carbinolamine dehydratase; Validated
 3-73 1.49e-32

pterin-4-alpha-carbinolamine dehydratase; Validated


Pssm-ID: 234845  Cd Length: 97  Bit Score: 109.16  E-value: 1.49e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1018443291   3 GKAHRLSAEERDQLLPNLRavGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:PRK00823    1 MMAEKLSDEEIAELLPQLP--GWTLVGDRDAIERTFKFKNFNEAFAFMNRVAEIAEEEDHHPDWFNVYNRV 69
Pterin_4a pfam01329
Pterin 4 alpha carbinolamine dehydratase; Pterin 4 alpha carbinolamine dehydratase is also ...
 8-73 2.71e-26

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: 92.92  E-value: 2.71e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1018443291   8 LSAEERDQLLPNLraVGWnELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:pfam01329   1 LTEEEIEAALAEL--PGW-KLGDGGALERTFKFKDFKEAIAFVNRVALLAEAEGHHPDITNVYNKV 63
PhhB COG2154
Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];
4-73 2.40e-25

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


Pssm-ID: 441757  Cd Length: 99  Bit Score: 90.65  E-value: 2.40e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018443291   4 KAHRLSAEERDQLLPNLRavGWnELEGrDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:COG2154     2 AEPPLTDEEIAAALAELP--GW-ELED-GALERTFKFKDFAEALAFVNRVAELAEAEDHHPDISNRYNRV 67
 
Name Accession Description Interval E-value
PCD_DCoH_subfamily_b cd00914
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 24-74 2.12e-35

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: 115.40  E-value: 2.12e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1018443291  24 GWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVS 74
Cdd:cd00914     1 GWTLVDGRDAIHKSFKFKDFNEAFGFMTRVALEAEKMNHHPEWFNVYNKVD 51
phhB PRK00823
pterin-4-alpha-carbinolamine dehydratase; Validated
 3-73 1.49e-32

pterin-4-alpha-carbinolamine dehydratase; Validated


Pssm-ID: 234845  Cd Length: 97  Bit Score: 109.16  E-value: 1.49e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1018443291   3 GKAHRLSAEERDQLLPNLRavGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:PRK00823    1 MMAEKLSDEEIAELLPQLP--GWTLVGDRDAIERTFKFKNFNEAFAFMNRVAEIAEEEDHHPDWFNVYNRV 69
Pterin_4a pfam01329
Pterin 4 alpha carbinolamine dehydratase; Pterin 4 alpha carbinolamine dehydratase is also ...
 8-73 2.71e-26

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: 92.92  E-value: 2.71e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1018443291   8 LSAEERDQLLPNLraVGWnELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:pfam01329   1 LTEEEIEAALAEL--PGW-KLGDGGALERTFKFKDFKEAIAFVNRVALLAEAEGHHPDITNVYNKV 63
PhhB COG2154
Pterin-4a-carbinolamine dehydratase [Coenzyme transport and metabolism];
4-73 2.40e-25

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


Pssm-ID: 441757  Cd Length: 99  Bit Score: 90.65  E-value: 2.40e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018443291   4 KAHRLSAEERDQLLPNLRavGWnELEGrDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:COG2154     2 AEPPLTDEEIAAALAELP--GW-ELED-GALERTFKFKDFAEALAFVNRVAELAEAEDHHPDISNRYNRV 67
PCD_DCoH cd00488
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 24-73 1.73e-23

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: 85.26  E-value: 1.73e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1018443291  24 GWnELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:cd00488     1 GW-ELADGDALERTFKFKDFKEAIAFVNRVAELAEALNHHPDISNVYNKV 49
PCD_DCoH_subfamily_a cd00913
PCD_DCoH: The bifunctional protein pterin-4alpha-carbinolamine dehydratase (PCD), also known ...
 24-73 5.97e-06

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: 40.68  E-value: 5.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1018443291  24 GWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKV 73
Cdd:cd00913     1 GWELADDGLKLERTFRFKNFVEALEFVNAVGEIAEAEGHHPDLSLGWGRV 50
 
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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