ID   PHS_PROMS               Reviewed;          96 AA.
AC   A2BPX4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=A9601_05471;
OS   Prochlorococcus marinus (strain AS9601).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=146891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS9601;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000551; ABM69835.1; -; Genomic_DNA.
DR   RefSeq; WP_011818001.1; NC_008816.1.
DR   AlphaFoldDB; A2BPX4; -.
DR   SMR; A2BPX4; -.
DR   STRING; 146891.A9601_05471; -.
DR   EnsemblBacteria; ABM69835; ABM69835; A9601_05471.
DR   KEGG; pmb:A9601_05471; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_3_2_3; -.
DR   OMA; WAEKWNH; -.
DR   OrthoDB; 1862336at2; -.
DR   Proteomes; UP000002590; 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   PANTHER; PTHR12599; PTHR12599; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; SSF55248; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..96
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_1000050434"
SQ   SEQUENCE   96 AA;  11254 MW;  6726B53F6E760C0D CRC64;
     MEPYILQDEE LNELVVKIPG WEIKSKQIQR EFNFANFIEA FAFMTKVALI CEKYNHHPNW
     ENVYAKVIIK LNTHDLGGIT NLDQTLASEI NKIFDQ