(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBT1_SEGRD

ID   D6ZBT1_SEGRD            Unreviewed;       197 AA.
AC   D6ZBT1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 53.
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   OrderedLocusNames=Srot_0421 {ECO:0000313|EMBL:ADG96908.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96908.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96908.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate +
CC         formate + H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58462; EC=3.5.4.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00223, ECO:0000256|SAAS:SAAS01118752};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00223,
CC       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; CP001958; ADG96908.1; -; Genomic_DNA.
DR   RefSeq; WP_013137364.1; NC_014168.1.
DR   STRING; 640132.Srot_0421; -.
DR   EnsemblBacteria; ADG96908; ADG96908; Srot_0421.
DR   KEGG; srt:Srot_0421; -.
DR   eggNOG; ENOG4105EUJ; Bacteria.
DR   eggNOG; COG0302; LUCA.
DR   HOGENOM; HOG000221222; -.
DR   KO; K01495; -.
DR   OMA; IVVVECE; -.
DR   OrthoDB; 1632367at2; -.
DR   BioCyc; SROT640132:G1GLH-422-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002247; Chromosome.
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-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; D6ZBT1.
DR   SWISS-2DPAGE; D6ZBT1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00223,
KW   ECO:0000256|SAAS:SAAS00021177, ECO:0000313|EMBL:ADG96908.1};
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:UP000002247};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00021207}.
FT   DOMAIN       17    192       GTP_cyclohydroI. {ECO:0000259|Pfam:
FT                                PF01227}.
FT   METAL        85     85       Zinc. {ECO:0000256|HAMAP-Rule:MF_00223}.
FT   METAL        88     88       Zinc. {ECO:0000256|HAMAP-Rule:MF_00223}.
FT   METAL       158    158       Zinc. {ECO:0000256|HAMAP-Rule:MF_00223}.
SQ   SEQUENCE   197 AA;  21722 MW;  DEBBD5FA87B0854E CRC64;
     MESFEQTKSA FDDNRAEAAV RELLIAVGED PDRPGLSRTP ARVAKLYREL FSGLEQNPED
     VLGESFAADH DELVLVKDIR VQSVCEHHLL SFHGNAHVGY IPGVGGSVVG FSALSRLVDL
     YARRPQIQER LTSQVADALM EHLRPRGVIV VVEAEHLCMQ VRADRQQSAR VTTSAVRGLL
     RTNPSSRAEA LGFILRA
//

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