PHS_BRUME
ID PHS_BRUME Reviewed; 97 AA.
AC P65722; Q8YEL4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Name=phhB; OrderedLocusNames=BMEI1864;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL53045.1; -; Genomic_DNA.
DR PIR; AB3485; AB3485.
DR RefSeq; WP_002965330.1; NZ_GG703778.1.
DR PDB; 3JST; X-ray; 2.10 A; A/B=1-97.
DR PDBsum; 3JST; -.
DR AlphaFoldDB; P65722; -.
DR SMR; P65722; -.
DR STRING; 224914.BMEI1864; -.
DR EnsemblBacteria; AAL53045; AAL53045; BMEI1864.
DR GeneID; 45123580; -.
DR GeneID; 55589881; -.
DR KEGG; bme:BMEI1864; -.
DR PATRIC; fig|224914.52.peg.1713; -.
DR eggNOG; COG2154; Bacteria.
DR OMA; WAEKWNH; -.
DR EvolutionaryTrace; P65722; -.
DR Proteomes; UP000000419; Chromosome I.
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 PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase.
FT CHAIN 1..97
FT /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_0000063076"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:3JST"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3JST"
FT HELIX 39..56
FT /evidence="ECO:0007829|PDB:3JST"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3JST"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3JST"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:3JST"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:3JST"
SQ SEQUENCE 97 AA; 11054 MW; 3176828807D408F3 CRC64;
MARNRLTESE MNEALRALDG WQKVDGREAI TRSFKFKDFS TAFGFMAQAA LYAEKLDHHP
EWFNAYNRVD VTLATHSENG VTELDIKMAR KMNAIAG
