Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GTP cyclohydrolase-2

Gene

ribA

Organism
Shewanella baltica (strain OS155 / ATCC BAA-1091)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.UniRule annotation

Catalytic activityi

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Zinc; catalyticUniRule annotation
Metal bindingi65 – 651Zinc; catalyticUniRule annotation
Metal bindingi67 – 671Zinc; catalyticUniRule annotation
Binding sitei70 – 701GTPUniRule annotation
Binding sitei114 – 1141GTPUniRule annotation
Active sitei126 – 1261Proton acceptorUniRule annotation
Active sitei128 – 1281NucleophileUniRule annotation
Binding sitei149 – 1491GTPUniRule annotation
Binding sitei154 – 1541GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 535GTPUniRule annotation
Nucleotide bindingi92 – 943GTPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. riboflavin biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Riboflavin biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciSBAL325240:GCTA-1697-MONOMER.
UniPathwayiUPA00275; UER00400.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase-2UniRule annotation (EC:3.5.4.25UniRule annotation)
Alternative name(s):
GTP cyclohydrolase IIUniRule annotation
Gene namesi
Name:ribAUniRule annotation
Ordered Locus Names:Sbal_1668
OrganismiShewanella baltica (strain OS155 / ATCC BAA-1091)
Taxonomic identifieri325240 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001557: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204GTP cyclohydrolase-2PRO_1000040579Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi325240.Sbal_1668.

Structurei

3D structure databases

ProteinModelPortaliA3D367.
SMRiA3D367. Positions 1-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase II family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0807.
HOGENOMiHOG000115442.
KOiK01497.
OMAiQGFILYL.
OrthoDBiEOG679TK8.

Family and domain databases

HAMAPiMF_00179. RibA.
InterProiIPR000926. GTP_CycHdrlaseII_RibA.
[Graphical view]
PfamiPF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00505. ribA. 1 hit.

Sequencei

Sequence statusi: Complete.

A3D367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIKYVATSK LPTPWGVFAM HGFEDTESGK EHVALTFGTL SADEPVLGRI
60 70 80 90 100
HSECLTGDAL FSLRCDCGFQ LQAAMQNIAE TGSGFILYLR QEGRGIGLLN
110 120 130 140 150
KIRAYELQDK GANTVEANEQ LGFEADMRKY DMIKPILEQI GVKHVRLMTN
160 170 180 190 200
NPRKVKAMKE FGIEVVERVP LQVGKNRYNE AYLKTKSTEL GHMMSEYHFM

DENK
Length:204
Mass (Da):22,997
Last modified:March 20, 2007 - v1
Checksum:i81F61281BD8FAA24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000563 Genomic DNA. Translation: ABN61180.1.
RefSeqiWP_011846503.1. NC_009052.1.
YP_001050049.1. NC_009052.1.

Genome annotation databases

EnsemblBacteriaiABN61180; ABN61180; Sbal_1668.
GeneIDi4844764.
KEGGisbl:Sbal_1668.
PATRICi37182199. VBISheBal55297_1948.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000563 Genomic DNA. Translation: ABN61180.1.
RefSeqiWP_011846503.1. NC_009052.1.
YP_001050049.1. NC_009052.1.

3D structure databases

ProteinModelPortaliA3D367.
SMRiA3D367. Positions 1-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi325240.Sbal_1668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN61180; ABN61180; Sbal_1668.
GeneIDi4844764.
KEGGisbl:Sbal_1668.
PATRICi37182199. VBISheBal55297_1948.

Phylogenomic databases

eggNOGiCOG0807.
HOGENOMiHOG000115442.
KOiK01497.
OMAiQGFILYL.
OrthoDBiEOG679TK8.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00400.
BioCyciSBAL325240:GCTA-1697-MONOMER.

Family and domain databases

HAMAPiMF_00179. RibA.
InterProiIPR000926. GTP_CycHdrlaseII_RibA.
[Graphical view]
PfamiPF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00505. ribA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OS155 / ATCC BAA-1091.

Entry informationi

Entry nameiRIBA_SHEB5
AccessioniPrimary (citable) accession number: A3D367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: March 4, 2015
This is version 48 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

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.