ID   PHS2_PONAB              Reviewed;         117 AA.
AC   Q5R7K1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   25-MAY-2022, entry version 63.
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   Flags: Fragment;
GN   Name=PCBD2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha
CC       and enhances its transcriptional activity. {ECO:0000250}.
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   -!- SUBUNIT: Homotetramer. Interacts with DYRK1B (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH92259.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR860114; CAH92259.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q5R7K1; -.
DR   SMR; Q5R7K1; -.
DR   STRING; 9601.ENSPPYP00000017661; -.
DR   eggNOG; KOG4073; Eukaryota.
DR   HOGENOM; CLU_081974_3_1_1; -.
DR   InParanoid; Q5R7K1; -.
DR   Proteomes; UP000001595; 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   Acetylation; Lyase; Reference proteome; Tetrahydrobiopterin biosynthesis.
FT   CHAIN           <1..117
FT                   /note="Pterin-4-alpha-carbinolamine dehydratase 2"
FT                   /id="PRO_0000228719"
FT   MOD_RES         101
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZL5"
FT   MOD_RES         101
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZL5"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZL5"
FT   MOD_RES         105
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZL5"
FT   MOD_RES         112
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZL5"
FT   MOD_RES         112
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZL5"
FT   NON_TER         1
SQ   SEQUENCE   117 AA;  13142 MW;  CB9C55AC2463713E CRC64;
     LLAALRGQSL GLAAMSSGTH RLTPEERNQA ILDLKAAGWS ELSERDAIYK EFSFRNFNQA
     FGFMSRVALQ AEKMNHHPEW FNVYNKVQIT LTSHDCGELT KKDVKLAQFI EKAAASV