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Database: UniProt
Entry: A0A126RB20_9SPHN
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ID   A0A126RB20_9SPHN        Unreviewed;        96 AA.
AC   A0A126RB20;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE            Short=PHS {ECO:0000256|HAMAP-Rule:MF_00434};
DE            EC=4.2.1.96 {ECO:0000256|HAMAP-Rule:MF_00434};
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE   AltName: Full=Pterin carbinolamine dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE            Short=PCD {ECO:0000256|HAMAP-Rule:MF_00434};
GN   Name=phhB {ECO:0000313|EMBL:AMK18765.1};
GN   ORFNames=K663_11930 {ECO:0000313|EMBL:AMK18765.1};
OS   Sphingobium sp. MI1205.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=407020 {ECO:0000313|EMBL:AMK18765.1, ECO:0000313|Proteomes:UP000060707};
RN   [1] {ECO:0000313|Proteomes:UP000060707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI1205 {ECO:0000313|Proteomes:UP000060707};
RA   Tabata M.;
RT   "Genome sequence of gamma-HCH degrading bacterium Sphingobium sp. MI1205.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMK18765.1, ECO:0000313|Proteomes:UP000060707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI1205 {ECO:0000313|EMBL:AMK18765.1,
RC   ECO:0000313|Proteomes:UP000060707};
RX   PubMed=27056230;
RA   Tabata M., Ohhata S., Nikawadori Y., Sato T., Kishida K., Ohtsubo Y.,
RA   Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of a gamma-Hexachlorocyclohexane-Degrading
RT   Bacterium, Sphingobium sp. Strain MI1205.";
RL   Genome Announc. 4:0-0(2016).
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:0000256|ARBA:ARBA00001554, ECO:0000256|HAMAP-
CC         Rule:MF_00434};
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000256|ARBA:ARBA00006472, ECO:0000256|HAMAP-
CC       Rule:MF_00434}.
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DR   EMBL; CP005188; AMK18765.1; -; Genomic_DNA.
DR   RefSeq; WP_062117800.1; NZ_CP005188.1.
DR   AlphaFoldDB; A0A126RB20; -.
DR   STRING; 407020.K663_11930; -.
DR   KEGG; spmi:K663_11930; -.
DR   PATRIC; fig|407020.3.peg.2496; -.
DR   OrthoDB; 9794987at2; -.
DR   Proteomes; UP000060707; 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   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   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 {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00434}.
SQ   SEQUENCE   96 AA;  10754 MW;  731BBE7438FF6047 CRC64;
     MIGKLSGEER DRELADLPEW TAIAEPEGIR RRFVFADFNA AFGFMARVAL LAEQANHHPE
     WSNVYNRVDI TLTTHDAGGL SRRDIDMAKA IDALLA
//
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