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Q5R7K1 (PHS2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pterin-4-alpha-carbinolamine dehydratase 2

Short name=PHS 2
EC=4.2.1.96
Alternative name(s):
4-alpha-hydroxy-tetrahydropterin dehydratase 2
Gene names
Name:PCBD2
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length117 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 By similarity.

Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity By similarity.

Catalytic activity

(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O.

Subunit structure

Homotetramer. Interacts with DYRK1B By similarity.

Sequence similarities

Belongs to the pterin-4-alpha-carbinolamine dehydratase family.

Sequence caution

The sequence CAH92259.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTetrahydrobiopterin biosynthesis
   Molecular functionLyase
   PTMAcetylation
Gene Ontology (GO)
   Biological processtetrahydrobiopterin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function4-alpha-hydroxytetrahydrobiopterin dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 117›117Pterin-4-alpha-carbinolamine dehydratase 2
PRO_0000228719

Amino acid modifications

Modified residue1121N6-acetyllysine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q5R7K1 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: CB9C55AC2463713E

FASTA11713,142
        10         20         30         40         50         60 
LLAALRGQSL GLAAMSSGTH RLTPEERNQA ILDLKAAGWS ELSERDAIYK EFSFRNFNQA 

        70         80         90        100        110 
FGFMSRVALQ AEKMNHHPEW FNVYNKVQIT LTSHDCGELT KKDVKLAQFI EKAAASV 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860114 mRNA. Translation: CAH92259.1. Different initiation.
UniGenePab.816.

3D structure databases

ProteinModelPortalQ5R7K1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000018372; ENSPPYP00000017661; ENSPPYG00000015795.
ENSPPYT00000018373; ENSPPYP00000017662; ENSPPYG00000015795.

Phylogenomic databases

HOVERGENHBG000259.
InParanoidQ5R7K1.

Family and domain databases

InterProIPR001533. Trans/pterin_deHydtase.
[Graphical view]
Gene3DG3DSA:3.30.1360.20. Trans_pterinDh. 1 hit.
PANTHERPTHR12599. Trans_pterinDh. 1 hit.
PfamPF01329. Pterin_4a. 1 hit.
[Graphical view]
SUPFAMSSF55248. Trans_pterinDh. 1 hit.
ProtoNetSearch...

Entry information

Entry namePHS2_PONAB
AccessionPrimary (citable) accession number: Q5R7K1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: June 16, 2009
Last modified: September 21, 2011
This is version 31 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families