ID PHS_PSEAE Reviewed; 118 AA. AC P43335; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 128. DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase; DE Short=PHS; DE EC=4.2.1.96; DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase; DE AltName: Full=Pterin carbinolamine dehydratase; DE Short=PCD; GN Name=phhB; OrderedLocusNames=PA0871; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=8108417; DOI=10.1073/pnas.91.4.1366; RA Zhao G., Xia T., Song J., Roy R.A.; RT "Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine RT hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three- RT component gene cluster."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1366-1370(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both CC prevent the formation of 7-pterins and accelerate the formation of CC quinonoid-BH2. May also have a positive regulatory role in the CC expression of phhA. 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 -!- SUBUNIT: Homodimer. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase CC family. {ECO:0000305}. 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; M88627; AAA25937.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04260.1; -; Genomic_DNA. DR PIR; E83535; E83535. DR RefSeq; NP_249562.1; NC_002516.2. DR RefSeq; WP_003085898.1; NC_002516.2. DR AlphaFoldDB; P43335; -. DR SMR; P43335; -. DR STRING; 208964.PA0871; -. DR PaxDb; 208964-PA0871; -. DR GeneID; 880827; -. DR KEGG; pae:PA0871; -. DR PATRIC; fig|208964.12.peg.905; -. DR PseudoCAP; PA0871; -. DR HOGENOM; CLU_081974_2_2_6; -. DR InParanoid; P43335; -. DR OrthoDB; 5294615at2; -. DR PhylomeDB; P43335; -. DR BioCyc; PAER208964:G1FZ6-886-MONOMER; -. DR Proteomes; UP000002438; Chromosome. DR AbasyAtlas; P43335; -. 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; IPR050376; Pterin-4-alpha-carb_dehyd. DR InterPro; IPR001533; Pterin_deHydtase. DR NCBIfam; NF002016; PRK00823.1-1; 1. 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; Reference proteome; Tetrahydrobiopterin biosynthesis. FT CHAIN 1..118 FT /note="Pterin-4-alpha-carbinolamine dehydratase" FT /id="PRO_0000063065" SQ SEQUENCE 118 AA; 13333 MW; 02502CBC1F9ADF94 CRC64; MTALTQAHCE ACRADAPHVS DEELPVLLRQ IPDWNIEVRD GIMQLEKVYL FKNFKHALAF TNAVGEISEA EGHHPGLLTE WGKVTVTWWS HSIKGLHRND FIMAARTDEV AKTAEGRK //