(data stored in ACNUC7421 zone)

SWISSPROT: D8NKP1_RALSL

ID   D8NKP1_RALSL            Unreviewed;       100 AA.
AC   D8NKP1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   16-JAN-2019, entry version 40.
DE   RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE            Short=PHS {ECO:0000256|HAMAP-Rule:MF_00434};
DE            EC=4.2.1.96 {ECO:0000256|HAMAP-Rule:MF_00434};
DE   AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE   AltName: Full=Pterin carbinolamine dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE            Short=PCD {ECO:0000256|HAMAP-Rule:MF_00434};
GN   Name=phhB {ECO:0000313|EMBL:CBJ41425.1};
GN   ORFNames=RCFBP_10109 {ECO:0000313|EMBL:CBJ41425.1};
OS   Ralstonia solanacearum CFBP2957.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=859656 {ECO:0000313|EMBL:CBJ41425.1, ECO:0000313|Proteomes:UP000008677};
RN   [1] {ECO:0000313|EMBL:CBJ41425.1, ECO:0000313|Proteomes:UP000008677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ41425.1};
RX   PubMed=20550686; DOI=10.1186/1471-2164-11-379;
RA   Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA   Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA   Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT   "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT   species complex reveal significant evolutionary divergence.";
RL   BMC Genomics 11:379-379(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin
CC         = (6R)-L-erythro-6,7-dihydrobiopterin + H2O;
CC         Xref=Rhea:RHEA:11920, ChEBI:CHEBI:15377, ChEBI:CHEBI:15642,
CC         ChEBI:CHEBI:43120; EC=4.2.1.96; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00434, ECO:0000256|SAAS:SAAS01115827};
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine
CC       dehydratase family. {ECO:0000256|HAMAP-Rule:MF_00434,
CC       ECO:0000256|SAAS:SAAS00686664}.
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DR   EMBL; FP885897; CBJ41425.1; -; Genomic_DNA.
DR   EnsemblBacteria; CBJ41425; CBJ41425; RCFBP_10109.
DR   KEGG; rsc:RCFBP_10109; -.
DR   HOGENOM; HOG000007680; -.
DR   KO; K01724; -.
DR   Proteomes; UP000008677; 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   PANTHER; PTHR12599; PTHR12599; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; SSF55248; 1.
PE   3: Inferred from homology;
DR   PRODOM; D8NKP1.
DR   SWISS-2DPAGE; D8NKP1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008677};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00434, ECO:0000256|SAAS:SAAS00686667,
KW   ECO:0000313|EMBL:CBJ41425.1}.
SQ   SEQUENCE   100 AA;  11519 MW;  5ED2A07FFEACA4E9 CRC64;
     MPTLNDEQRK ALFAELQGWS TQSDRDAIHK RFTFTDFNAA FGFMTRVALK AEQMNHHPEW
     FNVWNRVDIT LSTHDANGLT HRDADLARFI EQAAKLTGAK
//

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