ID PHS_RHOPT Reviewed; 100 AA.
AC B3Q9E4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 18-JUN-2025, 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=Rpal_0408;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) 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}.
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DR EMBL; CP001096; ACE98968.1; -; Genomic_DNA.
DR RefSeq; WP_012494130.1; NC_011004.1.
DR AlphaFoldDB; B3Q9E4; -.
DR SMR; B3Q9E4; -.
DR KEGG; rpt:Rpal_0408; -.
DR HOGENOM; CLU_081974_3_2_5; -.
DR OrthoDB; 9794987at2; -.
DR Proteomes; UP000001725; 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 CDD; cd00914; PCD_DCoH_subfamily_b; 1.
DR Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR HAMAP; MF_00434; Pterin_4_alpha; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR NCBIfam; NF002017; PRK00823.1-2; 1.
DR NCBIfam; NF002018; PRK00823.1-3; 1.
DR NCBIfam; NF002020; PRK00823.1-5; 1.
DR PANTHER; PTHR12599; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR PANTHER; PTHR12599:SF0; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; PCD-like; 1.
PE 3: Inferred from homology;
KW Lyase.
FT CHAIN 1..100
FT /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_1000192932"
SQ SEQUENCE 100 AA; 11295 MW; 122020DD000D8364 CRC64;
MNRLSASERQ AALRELPGWL ELEEREAIGR SYQFTDFSEA FGFMTRVALA AEKADHHPEW
RNVYRTVDVV LTTHDAGGVT ERDVKLAKAM DAIAERCGAR
//
