ID   PHS2_CHICK              Reviewed;         103 AA.
AC   Q9DG45;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pterin-4-alpha-carbinolamine dehydratase 2;
DE            Short=PHS 2;
DE            EC=4.2.1.96;
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase 2;
DE   AltName: Full=DCoH-alpha;
DE   AltName: Full=DcoH-like protein DCoHm;
DE   AltName: Full=Hepatocyte nuclear factor 1a dimerization cofactor isoform;
GN   Name=PCBD2; Synonyms=DCOHM;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11237869; DOI=10.1042/0264-6021:3540645;
RA   Kim H., You S., Foster L.K., Farris J., Choi Y.-J., Foster D.N.;
RT   "Differential expression of chicken dimerization cofactor of hepatocyte
RT   nuclear factor-1 (DcoH) and its novel counterpart, DcoHalpha.";
RL   Biochem. J. 354:645-653(2001).
CC   -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both
CC       prevent the formation of 7-pterins and accelerate the formation of
CC       quinonoid-BH2 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha
CC       and enhances its transcriptional activity.
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   -!- TISSUE SPECIFICITY: Highest level found in the kidney, liver, heart and
CC       ovarian follicles.
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; AF190051; AAG17122.1; -; mRNA.
DR   RefSeq; NP_989534.1; NM_204203.2.
DR   AlphaFoldDB; Q9DG45; -.
DR   SMR; Q9DG45; -.
DR   STRING; 9031.ENSGALP00000010278; -.
DR   PRIDE; Q9DG45; -.
DR   GeneID; 374030; -.
DR   KEGG; gga:374030; -.
DR   CTD; 84105; -.
DR   VEuPathDB; HostDB:geneid_374030; -.
DR   eggNOG; KOG4073; Eukaryota.
DR   InParanoid; Q9DG45; -.
DR   OrthoDB; 1588292at2759; -.
DR   PhylomeDB; Q9DG45; -.
DR   PRO; PR:Q9DG45; -.
DR   Proteomes; UP000000539; Unplaced.
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   2: Evidence at transcript level;
KW   Lyase; Reference proteome; Tetrahydrobiopterin biosynthesis.
FT   CHAIN           1..103
FT                   /note="Pterin-4-alpha-carbinolamine dehydratase 2"
FT                   /id="PRO_0000063059"
SQ   SEQUENCE   103 AA;  11768 MW;  2C76DEABA2EA36F7 CRC64;
     MSSQSHWLTA EERTQVLLDL KASGWSESGE RDAIYKEFNF KNFNQAFGFM TRVALQAENM
     NHHPEWFNVY SKVQITLISH DCGGLTKRDV KLAQFIDKAA ASV