ID U3AFL1_9EURY Unreviewed; 91 AA.
AC U3AFL1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=MBEHAL_2333 {ECO:0000313|EMBL:GAD53573.1};
OS Halarchaeum acidiphilum MH1-52-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae.
OX NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD53573.1, ECO:0000313|Proteomes:UP000016986};
RN [1] {ECO:0000313|EMBL:GAD53573.1, ECO:0000313|Proteomes:UP000016986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD53573.1,
RC ECO:0000313|Proteomes:UP000016986};
RA Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL Submitted (SEP-2013) 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:GAD53573.1}.
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DR EMBL; BATA01000077; GAD53573.1; -; Genomic_DNA.
DR RefSeq; WP_021780662.1; NZ_BATA01000077.1.
DR AlphaFoldDB; U3AFL1; -.
DR eggNOG; arCOG02939; Archaea.
DR OrthoDB; 10495at2157; -.
DR Proteomes; UP000016986; 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}.
SQ SEQUENCE 91 AA; 10256 MW; 17B39C10CCD6A36D CRC64;
MAETLTDDEI EERLPPEWAH EGDEIVRTYE FDDYLEGVAF ASEIGELADE AFHHPTIVIE
YDAVDVRFTS HEAGGVTEQD LELAAECDAL R
//
