ID A0A1S1V7H0_9FIRM Unreviewed; 110 AA.
AC A0A1S1V7H0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=EUAN_15550 {ECO:0000313|EMBL:OHW62107.1};
OS Andreesenia angusta.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC Andreesenia.
OX NCBI_TaxID=39480 {ECO:0000313|EMBL:OHW62107.1, ECO:0000313|Proteomes:UP000180254};
RN [1] {ECO:0000313|EMBL:OHW62107.1, ECO:0000313|Proteomes:UP000180254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1989 {ECO:0000313|EMBL:OHW62107.1,
RC ECO:0000313|Proteomes:UP000180254};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Eubacterium angustum.";
RL Submitted (SEP-2016) 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:OHW62107.1}.
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DR EMBL; MKIE01000005; OHW62107.1; -; Genomic_DNA.
DR RefSeq; WP_071063352.1; NZ_MKIE01000005.1.
DR AlphaFoldDB; A0A1S1V7H0; -.
DR STRING; 39480.EUAN_15550; -.
DR OrthoDB; 9800108at2; -.
DR Proteomes; UP000180254; 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; cd00913; PCD_DCoH_subfamily_a; 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:UP000180254}.
SQ SEQUENCE 110 AA; 12713 MW; FC7EAA4D90838318 CRC64;
MKEELHKKRC EACTIGAEPL KPEEIAEYME SLDCGWEVVD NHHLERVFRF KNFVEALDYV
NRVGALAEEE QHHPDISLSW GKVVLTLFTH KIDGLSESDI VFAAKIDRMK
//
