(data stored in ACNUC7421 zone)

SWISSPROT: GCH4_PSEHT

ID   GCH4_PSEHT              Reviewed;         302 AA.
AC   Q3ILJ5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   30-AUG-2017, entry version 72.
DE   RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   OrderedLocusNames=PSHAa0549;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6-
CC       (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI85637.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR954246; CAI85637.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011327250.1; NC_007481.1.
DR   STRING; 326442.PSHAa0549; -.
DR   EnsemblBacteria; CAI85637; CAI85637; PSHAa0549.
DR   KEGG; pha:PSHAa0549; -.
DR   PATRIC; fig|326442.8.peg.518; -.
DR   eggNOG; ENOG4105DZA; Bacteria.
DR   eggNOG; COG1469; LUCA.
DR   HOGENOM; HOG000247517; -.
DR   KO; K09007; -.
DR   OrthoDB; POG091H0MIO; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-EC.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   PANTHER; PTHR36445:SF2; PTHR36445:SF2; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILJ5.
DR   SWISS-2DPAGE; Q3ILJ5.
KW   Complete proteome; Hydrolase; Reference proteome.
FT   CHAIN         1    302       GTP cyclohydrolase FolE2.
FT                                /FTId=PRO_0000289506.
FT   SITE        151    151       May be catalytically important.
FT                                {ECO:0000255|HAMAP-Rule:MF_01527}.
SQ   SEQUENCE   302 AA;  33539 MW;  FEDB0E3EC8D88873 CRC64;
     MPDIANTAPA LQTGTLDWVG MGEIELPFIF ESHGITPVTV NAKARAFVNL HKEDAKGIHM
     SRLFLALDTL STEQQVNPQT LAQALDFFIS SHEGLSDKAL IEFKFELPLR RKSLLSDKAG
     WKSYPVILTS TIEQGVINYE LSVDVTYSST CPCSAALARQ LIQNAFAEKF SQETLSQKEA
     LEWLGTTQGI VATPHSQRSI ANVKVKLDSN ITQFDVVNLI NTIEDELKTP VQAAVKREDE
     QEFARLNGQN LMFCEDAARK IKALLETQQY SDYWLQINHY ESLHAHDALA IAVKGVAGGY
     RA
//

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