(data stored in ACNUC28527 zone)

SWISSPROT: D0KMT2_SACS9

ID   D0KMT2_SACS9            Unreviewed;        97 AA.
AC   D0KMT2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   11-DEC-2019, entry version 44.
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   OrderedLocusNames=Ssol_0006 {ECO:0000313|EMBL:ACX90312.1};
OS   Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=555311 {ECO:0000313|EMBL:ACX90312.1, ECO:0000313|Proteomes:UP000001493};
RN   [1] {ECO:0000313|EMBL:ACX90312.1, ECO:0000313|Proteomes:UP000001493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98/2 {ECO:0000313|EMBL:ACX90312.1,
RC   ECO:0000313|Proteomes:UP000001493};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Mead D.;
RT   "Complete sequence of Sulfolobus solfataricus 98/2.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00434};
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00434}.
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DR   EMBL; CP001800; ACX90312.1; -; Genomic_DNA.
DR   RefSeq; WP_009992110.1; NZ_ACUK01000288.1.
DR   SMR; D0KMT2; -.
DR   EnsemblBacteria; ACX90312; ACX90312; Ssol_0006.
DR   GeneID; 38466625; -.
DR   KEGG; sol:Ssol_0006; -.
DR   HOGENOM; HOG000007680; -.
DR   KO; K01724; -.
DR   OMA; AVGWNEV; -.
DR   OrthoDB; 120013at2157; -.
DR   BioCyc; SSOL555311:G1GGG-6-MONOMER; -.
DR   Proteomes; UP000001493; 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; D0KMT2.
DR   SWISS-2DPAGE; D0KMT2.
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00434}.
SQ   SEQUENCE   97 AA;  11191 MW;  B0C87D24BDFF7B42 CRC64;
     MSGISSKELE ELKINGWIVL ENGKKIKKEF RFKDFKQSVD FLKDIQPSAD ALDHHPDVCV
     YYNRVVVELT THDVGGLTDL DYKLAIKLDE LYKMKTS
//

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