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Protein

GTP cyclohydrolase FolE2

Gene

folE2

Organism
Pelobacter propionicus (strain DSM 2379)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate.UniRule annotation

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
Sitei144 – 1441May be catalytically importantUniRule annotation

GO - Molecular functioni

  1. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciPPRO338966:GHL0-3332-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2UniRule annotation (EC:3.5.4.16UniRule annotation)
Gene namesi
Name:folE2UniRule annotation
Ordered Locus Names:Ppro_3275
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257GTP cyclohydrolase FolE2PRO_0000292755Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi338966.Ppro_3275.

Structurei

3D structure databases

ProteinModelPortaliA1AU47.
SMRiA1AU47. Positions 12-255.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase IV family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OrthoDBiEOG6X6RBH.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1AU47-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPDMQKRPDH RRIPISKVGV KDISYPIVVM DKNRSLQHTV ARVNMYVDLP
60 70 80 90 100
HQFKGTHMSR FVEILNRHRE QIALDKLETI LEEMKARLGS ASAHLEIQFP
110 120 130 140 150
YFIDKRAPVS GARSLMEYSC EFSASLTDTL DFVLGVRVPL TSLCPCSREL
160 170 180 190 200
AIHGAHNQRS IMTVRVRYRD FIWIEDLVEL IEQCGSSPLY SLLKRVDEKY
210 220 230 240 250
VTEQAYENPR FVEDMVREAY SRLAGMENIT WFSVETENFE SIHNHSAYAA

VELDRRG
Length:257
Mass (Da):29,794
Last modified:June 26, 2007 - v2
Checksum:i30774B6753A75E64
GO

Sequence cautioni

The sequence ABL00868.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00868.1. Different initiation.
RefSeqiYP_902925.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABL00868; ABL00868; Ppro_3275.
GeneIDi4572269.
KEGGippd:Ppro_3275.
PATRICi22899689. VBIPelPro64470_3431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00868.1. Different initiation.
RefSeqiYP_902925.1. NC_008609.1.

3D structure databases

ProteinModelPortaliA1AU47.
SMRiA1AU47. Positions 12-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338966.Ppro_3275.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL00868; ABL00868; Ppro_3275.
GeneIDi4572269.
KEGGippd:Ppro_3275.
PATRICi22899689. VBIPelPro64470_3431.

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OrthoDBiEOG6X6RBH.

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.
BioCyciPPRO338966:GHL0-3332-MONOMER.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiGCH4_PELPD
AccessioniPrimary (citable) accession number: A1AU47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: January 7, 2015
This is version 43 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.