ID   PHS_PSEPG               Reviewed;         118 AA.
AC   B0KRW3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000255|HAMAP-Rule:MF_00434};
DE            Short=PHS {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 {ECO:0000255|HAMAP-Rule:MF_00434};
DE   AltName: Full=Pterin carbinolamine dehydratase {ECO:0000255|HAMAP-Rule:MF_00434};
DE            Short=PCD {ECO:0000255|HAMAP-Rule:MF_00434};
GN   OrderedLocusNames=PputGB1_3996;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000926; ABY99886.1; -; Genomic_DNA.
DR   RefSeq; WP_012273573.1; NC_010322.1.
DR   AlphaFoldDB; B0KRW3; -.
DR   SMR; B0KRW3; -.
DR   STRING; 76869.PputGB1_3996; -.
DR   EnsemblBacteria; ABY99886; ABY99886; PputGB1_3996.
DR   KEGG; ppg:PputGB1_3996; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_2_2_6; -.
DR   OMA; FHHPGIL; -.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
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   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; SSF55248; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..118
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_1000080612"
SQ   SEQUENCE   118 AA;  13420 MW;  F6719E893F052220 CRC64;
     MNALNQAHCE ACRADAPKVT DEELAELIRE IPDWNIEVRD GHMELERVFL FKNFKHALAF
     TNAVGEIAEA EGHHPGLLTE WGKVTVTWWS HSIKGLHRND FIMCARTDKV AEVAEGRK