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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//