PHS_VIBC1
ID PHS_VIBC1 Reviewed; 112 AA.
AC A7N3S9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=VIBHAR_05422;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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: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; CP000790; ABU73327.1; -; Genomic_DNA.
DR RefSeq; WP_005433587.1; NC_022270.1.
DR AlphaFoldDB; A7N3S9; -.
DR SMR; A7N3S9; -.
DR EnsemblBacteria; ABU73327; ABU73327; VIBHAR_05422.
DR GeneID; 57824435; -.
DR GeneID; 67379375; -.
DR KEGG; vha:VIBHAR_05422; -.
DR PATRIC; fig|338187.25.peg.4819; -.
DR OMA; FHHPGIL; -.
DR OrthoDB; 1862336at2; -.
DR Proteomes; UP000008152; Chromosome II.
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.
FT CHAIN 1..112
FT /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_1000050469"
SQ SEQUENCE 112 AA; 13035 MW; D89C1293CF57C27B CRC64;
MLNEQKCEAC SIDAIALSKE EQQSLLLQLS DWQIIERDEI PQLEKVYKFK NFKQAWAFSN
KIAELAEDEF HHPSILLEWG KVTITWWSHS IKGLHKNDFI CASKCDALAI EE