ID   PHS_VIBC3               Reviewed;         109 AA.
AC   A5F0J0; C3M6C1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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   Name=phhB; OrderedLocusNames=VC0395_0408, VC395_A0851;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ19317.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11684.1; -; Genomic_DNA.
DR   RefSeq; WP_000883445.1; NZ_JAACZH010000012.1.
DR   AlphaFoldDB; A5F0J0; -.
DR   SMR; A5F0J0; -.
DR   STRING; 345073.VC395_A0851; -.
DR   EnsemblBacteria; ABQ19317; ABQ19317; VC0395_0408.
DR   GeneID; 57742204; -.
DR   KEGG; vco:VC0395_0408; -.
DR   KEGG; vcr:VC395_A0851; -.
DR   PATRIC; fig|345073.21.peg.3581; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_2_2_6; -.
DR   OMA; FHHPGIL; -.
DR   Proteomes; UP000000249; Chromosome 1.
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..109
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_1000072317"
SQ   SEQUENCE   109 AA;  12443 MW;  A21369EF8453EDED CRC64;
     MLDELRCEAC SAGAIGLTSE EQQQLLSELD GWALIHRDGI AQLEKRYRFK NFKQAWAFSN
     QIAELAEQEF HHPAILLEWG NVTVTWWSHS IKGLHKNDFI CAAKCDALT