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Q1LT77

- GCH1_BAUCH

UniProt

Q1LT77 - GCH1_BAUCH

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Protein

GTP cyclohydrolase 1

Gene

folE

Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101ZincUniRule annotation
Metal bindingi113 – 1131ZincUniRule annotation
Metal bindingi181 – 1811ZincUniRule annotation

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. one-carbon metabolic process Source: UniProtKB-HAMAP
  3. tetrahydrofolate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBCIC374463:GI6Q-394-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1UniRule annotation (EC:3.5.4.16UniRule annotation)
Alternative name(s):
GTP cyclohydrolase IUniRule annotation
Short name:
GTP-CH-IUniRule annotation
Gene namesi
Name:folEUniRule annotation
Ordered Locus Names:BCI_0394
OrganismiBaumannia cicadellinicola subsp. Homalodisca coagulata
Taxonomic identifieri374463 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia
ProteomesiUP000002427: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220GTP cyclohydrolase 1PRO_1000043667Add
BLAST

Interactioni

Subunit structurei

Toroid-shaped homodecamer, composed of two pentamers of five dimers.By similarity

Protein-protein interaction databases

STRINGi374463.BCI_0394.

Structurei

3D structure databases

ProteinModelPortaliQ1LT77.
SMRiQ1LT77. Positions 4-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase I family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0302.
HOGENOMiHOG000221222.
KOiK01495.
OMAiVQFFSSR.
OrthoDBiEOG6XHC8G.

Family and domain databases

HAMAPiMF_00223. FolE.
InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00063. folE. 1 hit.
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1LT77-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVILTKEASM VRQALLANGL EPFLRGEERL GIEARKRRIA AHMKKIMTLL
60 70 80 90 100
NLDLADDSLA KTPYRIAYMY IEEIFPGLDY ANFPQITLIS NKMKADEMVT
110 120 130 140 150
VRNITLTSTC EHHFLMIDGK ATVSYIPKSN VIGLSKINRI VRFFAQRPQV
160 170 180 190 200
QERLTQQILL ALQTILGTNN VAVSIYAVHY CVKARGICDS TSTTTTTSLG
210 220
GIFKSSQNTR QEFLRTINQT
Length:220
Mass (Da):24,802
Last modified:May 30, 2006 - v1
Checksum:i8A7E971B06DAB2D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF13956.1.
RefSeqiWP_011520570.1. NC_007984.1.
YP_588837.1. NC_007984.1.

Genome annotation databases

EnsemblBacteriaiABF13956; ABF13956; BCI_0394.
GeneIDi4056702.
KEGGibci:BCI_0394.
PATRICi21074295. VBIBauCic75062_0376.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF13956.1 .
RefSeqi WP_011520570.1. NC_007984.1.
YP_588837.1. NC_007984.1.

3D structure databases

ProteinModelPortali Q1LT77.
SMRi Q1LT77. Positions 4-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374463.BCI_0394.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF13956 ; ABF13956 ; BCI_0394 .
GeneIDi 4056702.
KEGGi bci:BCI_0394.
PATRICi 21074295. VBIBauCic75062_0376.

Phylogenomic databases

eggNOGi COG0302.
HOGENOMi HOG000221222.
KOi K01495.
OMAi VQFFSSR.
OrthoDBi EOG6XHC8G.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci BCIC374463:GI6Q-394-MONOMER.

Family and domain databases

HAMAPi MF_00223. FolE.
InterProi IPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view ]
PANTHERi PTHR11109. PTHR11109. 1 hit.
Pfami PF01227. GTP_cyclohydroI. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00063. folE. 1 hit.
PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
    Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
    PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiGCH1_BAUCH
AccessioniPrimary (citable) accession number: Q1LT77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: October 1, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3