PHS_PSEAE
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 03-AUG-2022, entry version 115.
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 / 1C /
RC 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 / 1C /
RC 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}.
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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; NZ_QZGE01000007.1.
DR AlphaFoldDB; P43335; -.
DR SMR; P43335; -.
DR STRING; 287.DR97_1072; -.
DR PaxDb; P43335; -.
DR PRIDE; P43335; -.
DR EnsemblBacteria; AAG04260; AAG04260; 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 OMA; FHHPGIL; -.
DR PhylomeDB; P43335; -.
DR BioCyc; PAER208964:G1FZ6-886-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
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; 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
