PHS_HAHCH
ID PHS_HAHCH Reviewed; 112 AA.
AC Q2SCE8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000255|HAMAP-Rule:MF_00434};
DE Short=PHS {ECO:0000255|HAMAP-Rule:MF_00434};
DE EC=4.2.1.96 {ECO:0000255|HAMAP-Rule:MF_00434};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000255|HAMAP-Rule:MF_00434};
DE AltName: Full=Pterin carbinolamine dehydratase {ECO:0000255|HAMAP-Rule:MF_00434};
DE Short=PCD {ECO:0000255|HAMAP-Rule:MF_00434};
GN OrderedLocusNames=HCH_04986;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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:0000255|HAMAP-Rule:MF_00434};
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000255|HAMAP-Rule:MF_00434}.
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DR EMBL; CP000155; ABC31676.1; -; Genomic_DNA.
DR RefSeq; WP_011398741.1; NC_007645.1.
DR AlphaFoldDB; Q2SCE8; -.
DR SMR; Q2SCE8; -.
DR STRING; 349521.HCH_04986; -.
DR PRIDE; Q2SCE8; -.
DR EnsemblBacteria; ABC31676; ABC31676; HCH_04986.
DR KEGG; hch:HCH_04986; -.
DR eggNOG; COG2154; Bacteria.
DR HOGENOM; CLU_081974_2_2_6; -.
DR OMA; FHHPGIL; -.
DR OrthoDB; 1862336at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1360.20; -; 1.
DR HAMAP; MF_00434; Pterin_4_alpha; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..112
FT /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_1000080609"
SQ SEQUENCE 112 AA; 12949 MW; E9BFB1ED79F25CA0 CRC64;
MSDTIPSCEA CRPDAEKVDP AKLEKYLSQV PEWRLEERNG VQMISRDYKF KNFALALEFT
NKVGAIAEEI NHHPELVTEW GKVRVTWWSH TIKGLHELDF AMAKRCEAVF NA