(data stored in SCRATCH zone)

SWISSPROT: A4F6S1_SACEN

ID   A4F6S1_SACEN            Unreviewed;       213 AA.
AC   A4F6S1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 88.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000256|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000256|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000256|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000256|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000256|HAMAP-Rule:MF_00223,
GN   ECO:0000313|EMBL:CAL99745.1};
GN   OrderedLocusNames=SACE_0397 {ECO:0000313|EMBL:CAL99745.1};
GN   ORFNames=A8924_0793 {ECO:0000313|EMBL:PFG93548.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99745.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99745.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99745.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93548.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93548.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC         H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00223,
CC         ECO:0000256|SAAS:SAAS01118752};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00021202}.
CC   -!- SUBUNIT: Homopolymer. {ECO:0000256|HAMAP-Rule:MF_00223}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00673743}.
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DR   EMBL; AM420293; CAL99745.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93548.1; -; Genomic_DNA.
DR   RefSeq; WP_009946437.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0397; -.
DR   EnsemblBacteria; CAL99745; CAL99745; SACE_0397.
DR   KEGG; sen:SACE_0397; -.
DR   eggNOG; ENOG4105EUJ; Bacteria.
DR   eggNOG; COG0302; LUCA.
DR   HOGENOM; HOG000221222; -.
DR   KO; K01495; -.
DR   OMA; IVVVECE; -.
DR   OrthoDB; 1632367at2; -.
DR   BioCyc; SERY405948:SACE_RS01950-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6S1.
DR   SWISS-2DPAGE; A4F6S1.
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00021177,
KW   ECO:0000313|EMBL:CAL99745.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00223,
KW   ECO:0000256|SAAS:SAAS00021169};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00223,
KW   ECO:0000256|SAAS:SAAS00021243};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00021207}.
FT   DOMAIN          33..210
FT                   /note="GTP_cyclohydroI"
FT                   /evidence="ECO:0000259|Pfam:PF01227"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           101
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT   METAL           104
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT   METAL           174
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
SQ   SEQUENCE   213 AA;  23561 MW;  49EA75058253FAAC CRC64;
     MTSTVGEPVG PEEDSGPGRS AFHNPVFDQE RAEAAIRELL LAAGEDPDRE GLRETPARVA
     RAYRELFAGL YTDPDQVLDR TFDEAHEELV LVREIPMYSQ CEHHLLPFHG VAHVGYIPNE
     KGRVTGLSKL ARLVDLYAKR PQVQERLTSQ VADALMRRLE PRGVIVVIEA EHLCMGMRGI
     RKAGSMTTTS AVRGIFRSSA SSRSEALSLI RGT
//

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