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Database: UniProt
Entry: A0A077LAB0_9PSED
LinkDB: A0A077LAB0_9PSED
Original site: A0A077LAB0_9PSED 
ID   A0A077LAB0_9PSED        Unreviewed;       118 AA.
AC   A0A077LAB0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   Name=phhB {ECO:0000313|EMBL:BAP40877.1};
GN   ORFNames=PSCI_0175 {ECO:0000313|EMBL:BAP40877.1};
OS   Pseudomonas sp. StFLB209.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP40877.1, ECO:0000313|Proteomes:UP000031652};
RN   [1] {ECO:0000313|EMBL:BAP40877.1, ECO:0000313|Proteomes:UP000031652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StFLB209 {ECO:0000313|EMBL:BAP40877.1,
RC   ECO:0000313|Proteomes:UP000031652};
RX   PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA   Morohoshi T., Kato T., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT   sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL   Genome Announc. 2:e01037-e01014(2014).
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}.
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DR   EMBL; AP014637; BAP40877.1; -; Genomic_DNA.
DR   RefSeq; WP_045481579.1; NZ_AP014637.1.
DR   AlphaFoldDB; A0A077LAB0; -.
DR   STRING; 1028989.PSCI_0175; -.
DR   KEGG; pses:PSCI_0175; -.
DR   HOGENOM; CLU_081974_2_2_6; -.
DR   OrthoDB; 5294615at2; -.
DR   Proteomes; UP000031652; 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   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; PTHR42805; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR42805:SF1; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE-RELATED; 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:UP000031652}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  12975 MW;  FFE9DD8B7ED72ABB CRC64;
     MTALHERSCQ PCHGNASPVS DDDLKILLPQ LPGWRLETRD GVRQLEKTYD FKNFASALAF
     TNAIGALAEA EDHHPALLTE WGKVTVTWWT HAIGGLHAND FILAARTEGA AQQAEGRK
//
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