PHS_PSEAB
ID PHS_PSEAB Reviewed; 118 AA.
AC Q02I31;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000255|HAMAP-Rule:MF_00434};
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 OrderedLocusNames=PA14_53000;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE, AND
RP PHOSPHORYLATION AT THR-2.
RC STRAIN=UCBPP-PA14;
RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL Anal. Bioanal. Chem. 406:6297-6309(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: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; CP000438; ABJ10031.1; -; Genomic_DNA.
DR RefSeq; WP_003085898.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02I31; -.
DR SMR; Q02I31; -.
DR iPTMnet; Q02I31; -.
DR PRIDE; Q02I31; -.
DR EnsemblBacteria; ABJ10031; ABJ10031; PA14_53000.
DR KEGG; pau:PA14_53000; -.
DR HOGENOM; CLU_081974_2_2_6; -.
DR OMA; FHHPGIL; -.
DR BioCyc; PAER208963:G1G74-4461-MON; -.
DR Proteomes; UP000000653; 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 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 1: Evidence at protein level;
KW Lyase; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25096199"
FT CHAIN 2..118
FT /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_1000050436"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25096199"
SQ SEQUENCE 118 AA; 13333 MW; 02502CBC1F9ADF94 CRC64;
MTALTQAHCE ACRADAPHVS DEELPVLLRQ IPDWNIEVRD GIMQLEKVYL FKNFKHALAF
TNAVGEISEA EGHHPGLLTE WGKVTVTWWS HSIKGLHRND FIMAARTDEV AKTAEGRK
