ID   PHS_SOLUE               Reviewed;          95 AA.
AC   Q01VX3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Acid_5239;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000473; ABJ86192.1; -; Genomic_DNA.
DR   RefSeq; WP_011686936.1; NC_008536.1.
DR   AlphaFoldDB; Q01VX3; -.
DR   SMR; Q01VX3; -.
DR   STRING; 234267.Acid_5239; -.
DR   EnsemblBacteria; ABJ86192; ABJ86192; Acid_5239.
DR   KEGG; sus:Acid_5239; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_3_2_0; -.
DR   OMA; WAEKWNH; -.
DR   OrthoDB; 1862336at2; -.
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..95
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_1000050465"
SQ   SEQUENCE   95 AA;  10572 MW;  07DF78A46CE3B837 CRC64;
     MTTKLSESEI QSALRERSAW TVVNGKLHRE YKFADFIHAF GFMTCAALSA EAMNHHPEWF
     NVYNRLTIDL TTHDAGGITA KDFQLAAKLD ALAAG