ID   PHS_XENLA               Reviewed;         104 AA.
AC   Q91901; Q5D030;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Pterin-4-alpha-carbinolamine dehydratase;
DE            Short=PHS;
DE            EC=4.2.1.96 {ECO:0000250|UniProtKB:P61459};
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase;
DE   AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1-alpha;
DE            Short=DCoH;
DE            Short=Dimerization cofactor of HNF1;
DE            Short=xDCoH;
DE   AltName: Full=Phenylalanine hydroxylase-stimulating protein;
DE   AltName: Full=Pterin carbinolamine dehydratase;
DE            Short=PCD;
GN   Name=pcbd; Synonyms=dcoh;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7743933; DOI=10.1242/dev.121.4.1217;
RA   Pogge von Strandmann E., Ryffel G.U.;
RT   "Developmental expression of the maternal protein XDCoH, the dimerization
RT   cofactor of the homeoprotein LFB1 (HNF1).";
RL   Development 121:1217-1226(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both
CC       prevent the formation of 7-pterins and accelerate the formation of
CC       quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates
CC       the dimerization of homeodomain protein HNF1A and enhances its
CC       transcriptional activity (By similarity). Also acts as a coactivator
CC       for HNF1B-dependent transcription (By similarity).
CC       {ECO:0000250|UniProtKB:P61457, ECO:0000250|UniProtKB:P61459}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC         (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC         Evidence={ECO:0000250|UniProtKB:P61459};
CC   -!- SUBUNIT: Homotetramer and homodimer. {ECO:0000250|UniProtKB:P61459}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61459}. Nucleus
CC       {ECO:0000250|UniProtKB:P61459}.
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; Z37525; CAA85762.1; -; mRNA.
DR   EMBL; BC068690; AAH68690.1; -; mRNA.
DR   PIR; I51697; I51697.
DR   AlphaFoldDB; Q91901; -.
DR   SMR; Q91901; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.20; -; 1.
DR   HAMAP; MF_00434; Pterin_4_alpha; 1.
DR   InterPro; IPR036428; PCD_sf.
DR   InterPro; IPR001533; Pterin_deHydtase.
DR   PANTHER; PTHR12599; PTHR12599; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; SSF55248; 1.
PE   3: Inferred from homology;
KW   Acetylation; Activator; Cytoplasm; Lyase; Nucleus; Reference proteome;
KW   Tetrahydrobiopterin biosynthesis; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..104
FT                   /note="Pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_0000063056"
FT   BINDING         61..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         78..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   104 AA;  11920 MW;  3A89AD700855352D CRC64;
     MAGKVHRLSG EEREQLLPNL RAVGWHELDG RDAICKEFHF KDFNRAFGFM TRVALQAEKL
     DHHPEWFNVY DKVHITLSTH DCGGLSERDI NLASFIEQIA ASLS