PHS_PHEZH
ID PHS_PHEZH Reviewed; 97 AA.
AC B4RBN1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=PHZ_c0077;
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1;
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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; CP000747; ACG76491.1; -; Genomic_DNA.
DR RefSeq; WP_012520639.1; NC_011144.1.
DR AlphaFoldDB; B4RBN1; -.
DR SMR; B4RBN1; -.
DR STRING; 450851.PHZ_c0077; -.
DR EnsemblBacteria; ACG76491; ACG76491; PHZ_c0077.
DR KEGG; pzu:PHZ_c0077; -.
DR eggNOG; COG2154; Bacteria.
DR HOGENOM; CLU_081974_3_2_5; -.
DR OMA; WAEKWNH; -.
DR OrthoDB; 1862336at2; -.
DR Proteomes; UP000001868; 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 PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..97
FT /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_1000192926"
SQ SEQUENCE 97 AA; 10832 MW; 1601101C07C19415 CRC64;
MSRPKKIGAE AALARLPTWA KAEGGRDAIC KTFRFKDFNA AFGFMTRVAI RADQLDHHPE
WFNVYNRVEV TLATHDADGV TELDMTLAGF MDEISGN