ID   PHS_BORBR               Reviewed;         113 AA.
AC   Q7WG14;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 82.
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=BB4106;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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=CAE34469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX640449; CAE34469.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q7WG14; -.
DR   SMR; Q7WG14; -.
DR   STRING; 257310.BB4106; -.
DR   EnsemblBacteria; CAE34469; CAE34469; BB4106.
DR   KEGG; bbr:BB4106; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_3_0_4; -.
DR   Proteomes; UP000001027; 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..113
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_0000063072"
SQ   SEQUENCE   113 AA;  12574 MW;  F8358B861AE4E932 CRC64;
     MSTEFPMRIG AEVALPALQG WNAAAGRDAI EKRYRFDNFN AAFGFMARVA MFAEKMDHHP
     EWRNVYNRVD VTLTTHDAGG VTELDVRMAQ FMDEAAGRLG ATGLPARADQ PRT