ID   PHS_BOVIN               Reviewed;         104 AA.
AC   Q3ZBD3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Pterin-4-alpha-carbinolamine dehydratase;
DE            Short=PHS;
DE            EC=4.2.1.96;
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase;
DE   AltName: Full=Phenylalanine hydroxylase-stimulating protein;
DE   AltName: Full=Pterin carbinolamine dehydratase;
DE            Short=PCD;
DE   AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1-alpha;
DE            Short=Dimerization cofactor of HNF1;
DE            Short=DCoH;
GN   Name=PCBD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to
CC       both prevent the formation of 7-pterins and accelerate the
CC       formation of quinonoid-BH2 (By similarity). Regulates the
CC       dimerization of homeodomain protein HNF-1-alpha and enhances its
CC       transcriptional activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-
CC       5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-
CC       dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
CC   -!- SUBUNIT: Homotetramer or homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Cytoplasmic and/or nuclear (By similarity).
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine
CC       dehydratase family.
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DR   EMBL; BC103434; AAI03435.1; ALT_INIT; mRNA.
DR   IPI; IPI00689238; -.
DR   UniGene; Bt.48735; -.
DR   SMR; Q3ZBD3; 41-143.
DR   Ensembl; ENSBTAG00000011866; Bos taurus.
DR   HOVERGEN; Q3ZBD3; -.
DR   BRENDA; 4.2.1.96; 251.
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 dehydrat...; IEA:EC.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001533; Trans/pterin_deHydtase.
DR   Gene3D; G3DSA:3.30.1360.20; Trans_pterinDh; 1.
DR   PANTHER; PTHR12599; Trans_pterinDh; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   ProDom; PD007262; Trans_pterinDh; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Lyase; Nucleus;
KW   Tetrahydrobiopterin biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    104       Pterin-4-alpha-carbinolamine dehydratase.
FT                                /FTId=PRO_0000315210.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   104 AA;  11986 MW;  997DF8C2417FFD56 CRC64;
     MAGKAHRLSA EERDQLLPNL RAVGWNELEG RDAIFKQFHF KDFNRAFGFM TRVALQAEKL
     DHHPEWFNVY NKVHITLSTH ECAGLSERDV NLASFIEQVA VSMT
//