PHS_PSESM
ID PHS_PSESM Reviewed; 118 AA.
AC Q885L1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase;
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 Name=phhB; OrderedLocusNames=PSPTO_1821;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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 (By similarity). {ECO:0000250}.
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; AE016853; AAO55340.1; -; Genomic_DNA.
DR RefSeq; NP_791645.1; NC_004578.1.
DR RefSeq; WP_005616592.1; NC_004578.1.
DR AlphaFoldDB; Q885L1; -.
DR SMR; Q885L1; -.
DR STRING; 223283.PSPTO_1821; -.
DR EnsemblBacteria; AAO55340; AAO55340; PSPTO_1821.
DR GeneID; 1183462; -.
DR KEGG; pst:PSPTO_1821; -.
DR PATRIC; fig|223283.9.peg.1851; -.
DR eggNOG; COG2154; Bacteria.
DR HOGENOM; CLU_081974_2_2_6; -.
DR OMA; FHHPGIL; -.
DR OrthoDB; 1862336at2; -.
DR PhylomeDB; Q885L1; -.
DR Proteomes; UP000002515; 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_0000063067"
SQ SEQUENCE 118 AA; 13176 MW; FD5CF845B10FE25A CRC64;
MSTLNQAHCE ACSAGAPQVS EAELPELLRQ IPDWNIEVRD SVMQLEKVFL FKNFKFALAF
TNAVGEIAEA EGHHPGLLTE WGKVTVTWWS HSIKGLHRND FIMAARTDEV AAKAEGRK
