(data stored in SCRATCH zone)

SWISSPROT: Q3IJ00_PSEHT

ID   Q3IJ00_PSEHT            Unreviewed;       207 AA.
AC   Q3IJ00;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 81.
DE   SubName: Full=GTP cyclohydrolase II {ECO:0000313|EMBL:CAI85618.1};
DE            EC=3.5.4.25 {ECO:0000313|EMBL:CAI85618.1};
GN   Name=ribA {ECO:0000313|EMBL:CAI85618.1};
GN   OrderedLocusNames=PSHAa0529 {ECO:0000313|EMBL:CAI85618.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85618.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85618.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., 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 + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC       {ECO:0000256|SAAS:SAAS00711743}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP.
CC       {ECO:0000256|SAAS:SAAS00711745}.
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DR   EMBL; CR954246; CAI85618.1; -; Genomic_DNA.
DR   RefSeq; WP_011327231.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ00; -.
DR   STRING; 326442.PSHAa0529; -.
DR   EnsemblBacteria; CAI85618; CAI85618; PSHAa0529.
DR   GeneID; 32567585; -.
DR   KEGG; pha:PSHAa0529; -.
DR   eggNOG; ENOG4107T1C; Bacteria.
DR   eggNOG; COG0807; LUCA.
DR   HOGENOM; HOG000115442; -.
DR   KO; K01497; -.
DR   OMA; ERTGHLI; -.
DR   OrthoDB; POG091H0120; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; SSF142695; 1.
PE   4: Predicted;
DR   PRODOM; Q3IJ00.
DR   SWISS-2DPAGE; Q3IJ00.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   GTP-binding {ECO:0000256|SAAS:SAAS00711691};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00711696,
KW   ECO:0000313|EMBL:CAI85618.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00711702};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00711707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Riboflavin biosynthesis {ECO:0000256|SAAS:SAAS00711711}.
FT   DOMAIN       20    171       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
SQ   SEQUENCE   207 AA;  22977 MW;  60B706EA596E99A8 CRC64;
     MAQVRARVQL NVGKNSDIPA EIISFTDLKD GKEHIAMVFN NADTEQDVPL IRMHSECLTG
     DVFYSSRCDC GEQLNECIEM MHEQGGILLY LRQEGRGIGL YNKIDAYVLQ SQGMNTYEAN
     NHLGFADDLR DFSDAVLMLN ALNLPHVKLM TNNPKKLNAL RDAGITVDSV VGTHAHIKAG
     VAGNKAYLET KIKHGAHMLD IKKIKKP
//

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