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Database: UniProt
Entry: A0A0A6PCN2_9GAMM
LinkDB: A0A0A6PCN2_9GAMM
Original site: A0A0A6PCN2_9GAMM 
ID   A0A0A6PCN2_9GAMM        Unreviewed;       119 AA.
AC   A0A0A6PCN2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   03-MAY-2023, 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=PN36_08920 {ECO:0000313|EMBL:KHD07999.1};
OS   Candidatus Thiomargarita nelsonii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiomargarita.
OX   NCBI_TaxID=1003181 {ECO:0000313|EMBL:KHD07999.1, ECO:0000313|Proteomes:UP000030428};
RN   [1] {ECO:0000313|EMBL:KHD07999.1, ECO:0000313|Proteomes:UP000030428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hydrate Ridge {ECO:0000313|EMBL:KHD07999.1};
RX   PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA   Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA   Winkel M., Mussmann M., Bailey J.;
RT   "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT   nelsonii Reveals Genomic Plasticity.";
RL   Front. Microbiol. 7:603-603(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}.
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:KHD07999.1}.
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DR   EMBL; JSZA02000026; KHD07999.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6PCN2; -.
DR   Proteomes; UP000030428; 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:UP000030428}.
SQ   SEQUENCE   119 AA;  13570 MW;  173401F5E9AA29AD CRC64;
     MSELTQKRCK PCEGGIKPLT REEAQALLSQ LKDWQLNETA TEMSRPYKFK NYYETMAFVN
     AVAWIAHQED HHPDLEVAYN RCLVRYSTHA IGGMSENDFI CAAKIDALLA PPRNDSSHL
//
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