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Database: UniProt
Entry: A0A229UIU7_9BACL
LinkDB: A0A229UIU7_9BACL
Original site: A0A229UIU7_9BACL 
ID   A0A229UIU7_9BACL        Unreviewed;        97 AA.
AC   A0A229UIU7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
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   ORFNames=CF651_27115 {ECO:0000313|EMBL:OXM83205.1};
OS   Paenibacillus rigui.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=554312 {ECO:0000313|EMBL:OXM83205.1, ECO:0000313|Proteomes:UP000215509};
RN   [1] {ECO:0000313|EMBL:OXM83205.1, ECO:0000313|Proteomes:UP000215509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16352 {ECO:0000313|EMBL:OXM83205.1,
RC   ECO:0000313|Proteomes:UP000215509};
RA   Mayilraj S.;
RT   "Genome sequencing and assembly of Paenibacillus rigui.";
RL   Submitted (JUL-2017) 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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXM83205.1}.
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DR   EMBL; NMQW01000050; OXM83205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229UIU7; -.
DR   OrthoDB; 9800108at2; -.
DR   Proteomes; UP000215509; Unassembled WGS sequence.
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; cd00488; PCD_DCoH; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215509}.
SQ   SEQUENCE   97 AA;  11258 MW;  78EE2698F74061DE CRC64;
     MSRVKLSEDE LASRLERVPG WGREEGKWLV RSYRFPSFPE AVAFVDRVAS VAEAFNHHPF
     IVIDYTLVKL RLTTWRAEGL TELDFETARR FDEVAEG
//
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