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PHS_CHLL3
ID   PHS_CHLL3               Reviewed;         114 AA.
AC   Q3B6N5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 83.
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=Plut_0106;
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB22996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000096; ABB22996.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041463965.1; NC_007512.1.
DR   AlphaFoldDB; Q3B6N5; -.
DR   SMR; Q3B6N5; -.
DR   STRING; 319225.Plut_0106; -.
DR   EnsemblBacteria; ABB22996; ABB22996; Plut_0106.
DR   KEGG; plt:Plut_0106; -.
DR   eggNOG; COG2154; Bacteria.
DR   HOGENOM; CLU_081974_2_2_10; -.
DR   OMA; FHHPGIL; -.
DR   OrthoDB; 1862336at2; -.
DR   Proteomes; UP000002709; 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..114
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_0000231459"
SQ   SEQUENCE   114 AA;  13043 MW;  618B94F99A283F5C CRC64;
     MGELNKTKCV SCSEGLPPLA ERESEELLKE IPEWVIVSED GVSRLVRTFT FENFREAMAF
     AGSVGELAES EQHHPKLVTE WGKVRVEWWT HAVHGLHMND FVMAARTDEL FQEL
 
 
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