ID   PHS2_CUPPJ              Reviewed;         100 AA.
AC   Q46VT8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   18-JUN-2025, entry version 91.
DE   RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_00434};
DE            Short=PHS 2 {ECO:0000255|HAMAP-Rule:MF_00434};
DE            EC=4.2.1.96 {ECO:0000255|HAMAP-Rule:MF_00434};
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_00434};
DE   AltName: Full=Pterin carbinolamine dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_00434};
DE            Short=PCD 2 {ECO:0000255|HAMAP-Rule:MF_00434};
GN   OrderedLocusNames=Reut_A3388;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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:0000255|HAMAP-Rule:MF_00434};
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00434}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ62746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000090; AAZ62746.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q46VT8; -.
DR   SMR; Q46VT8; -.
DR   STRING; 264198.Reut_A3388; -.
DR   KEGG; reu:Reut_A3388; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_3_2_4; -.
DR   OrthoDB; 9794987at2; -.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR   CDD; cd00914; PCD_DCoH_subfamily_b; 1.
DR   Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR   HAMAP; MF_00434; Pterin_4_alpha; 1.
DR   InterPro; IPR036428; PCD_sf.
DR   InterPro; IPR001533; Pterin_deHydtase.
DR   NCBIfam; NF002018; PRK00823.1-3; 1.
DR   NCBIfam; NF002020; PRK00823.1-5; 1.
DR   PANTHER; PTHR12599; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR   PANTHER; PTHR12599:SF0; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; PCD-like; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..100
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase 2"
FT                   /id="PRO_0000231470"
SQ   SEQUENCE   100 AA;  11368 MW;  5E750A0AC9613CFC CRC64;
     MTPLSPQARA TLLAELPGWT DVDNRDAIQK RFTFPDFNAA FAFMTRVAIQ AEKADHHPEW
     FNVYNRVDIT LSTHDANGLT QRDIDLAHFI ERAAASLRVE
//