(data stored in ACNUC7421 zone)

SWISSPROT: GCH1_PSEHT

ID   GCH1_PSEHT              Reviewed;         184 AA.
AC   Q3IF89;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 80.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000255|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000255|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000255|HAMAP-Rule:MF_00223};
GN   OrderedLocusNames=PSHAa0073;
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   -!- 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_00223}.
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_00223}.
CC   -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of
CC       five dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
DR   EMBL; CR954246; CAI85182.1; -; Genomic_DNA.
DR   RefSeq; WP_011326800.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF89; -.
DR   STRING; 326442.PSHAa0073; -.
DR   EnsemblBacteria; CAI85182; CAI85182; PSHAa0073.
DR   KEGG; pha:PSHAa0073; -.
DR   PATRIC; fig|326442.8.peg.72; -.
DR   eggNOG; ENOG4105EUJ; Bacteria.
DR   eggNOG; COG0302; LUCA.
DR   HOGENOM; HOG000221222; -.
DR   KO; K01495; -.
DR   OMA; PFMGKVH; -.
DR   OrthoDB; POG091H01SE; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00223; FolE; 1.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   PANTHER; PTHR11109; PTHR11109; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IF89.
DR   SWISS-2DPAGE; Q3IF89.
KW   Complete proteome; GTP-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Reference proteome; Zinc.
FT   CHAIN         1    184       GTP cyclohydrolase 1.
FT                                /FTId=PRO_1000043718.
FT   METAL        75     75       Zinc. {ECO:0000255|HAMAP-Rule:MF_00223}.
FT   METAL        78     78       Zinc. {ECO:0000255|HAMAP-Rule:MF_00223}.
FT   METAL       146    146       Zinc. {ECO:0000255|HAMAP-Rule:MF_00223}.
SQ   SEQUENCE   184 AA;  20794 MW;  1EA5F48C7D3B05A1 CRC64;
     MHNELKQGYE NIITAVGEDP NREGLLDTPK RAAKAMEYLT QGYRQTLEEI TNNAVFTSDA
     DDMVLVQDIE LYSMCEHHLL PFTGRCHIAY IPNGKVLGLS KFARIVDMFA RRFQIQEQLT
     HQIAKAVEEV TGATGVGVIV EAKHMCMMMR GVEKQNSSMR TSVMLGNFRA DPKTRNEFLQ
     LIKG
//

If you have problems or comments...

PBIL Back to PBIL home page