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P94398 (GCH4_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase FolE2

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase 1B
Gene names
Name:folE2
Synonyms:yciA
Ordered Locus Names:BSU03340
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts GTP to 7,8-dihydroneopterin triphosphate. Ref.5

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. Ref.5

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_01527_B

Induction

Repressed by zinc, via zur. Ref.4

Sequence similarities

Belongs to the GTP cyclohydrolase IV family.

Caution

Was originally (Ref.4) thought to be a zinc uptake system.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7,8-dihydroneopterin 3'-triphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionGTP cyclohydrolase I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304GTP cyclohydrolase FolE2 HAMAP-Rule MF_01527_B
PRO_0000147701

Sites

Site1831May be catalytically important By similarity

Experimental info

Sequence conflict202 – 2098SIWADIHP → KHLGRIFTR in BAA08968. Ref.1
Sequence conflict2221L → P in BAA08968. Ref.1
Sequence conflict290 – 2956DAYAKL → RCLCEV in BAA08968. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P94398 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 90A28F90FE9BDAB3

FASTA30434,564
        10         20         30         40         50         60 
MNQHTLLPKK TERLQYFGSV SPIKGEKPVE KEKMKDLQNI RKDYFFDIQH VGVANVSHPV 

        70         80         90        100        110        120 
TITSAMMPAE QTTAANFTMT CNLPRNQKGI NMSRLTELLQ VYHQNGWILS FSSLQQFTKE 

       130        140        150        160        170        180 
LAENMDTSSA TVEVRFPWFF ERKSPKLEKA GLMHADIFMS VTYRKDQPFK QRAGISAKVT 

       190        200        210        220        230        240 
TLCPCSKEIS EYSAHNQRGT VSIWADIHPA ASLPSDVKAD LLHAAESNAS ARLHPVLKRP 

       250        260        270        280        290        300 
DEKAVTETAY ENPRFVEDLA RLIAADLFEL EWVSAFEIEC RNEESIHLHD AYAKLCFSKE 


VDKI 

« Hide

References

« Hide 'large scale' references
[1]"The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
Yamane K., Kumano M., Kurita K.
Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 202-209; 222 AND 290-295.
[4]"Functional analysis of the Bacillus subtilis Zur regulon."
Gaballa A., Wang T., Ye R.W., Helmann J.D.
J. Bacteriol. 184:6508-6514(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: 168.
[5]"Discovery of a new prokaryotic type I GTP cyclohydrolase family."
El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., Iwata-Reuyl D., de Crecy-Lagard V.
J. Biol. Chem. 281:37586-37593(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50453 Genomic DNA. Translation: BAA08968.1.
AL009126 Genomic DNA. Translation: CAB12128.2.
PIRH69759.
RefSeqNP_388216.2. NC_000964.3.

3D structure databases

ProteinModelPortalP94398.
SMRP94398. Positions 44-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP94398. 1 interaction.
MINTMINT-8366745.
STRING224308.BSU03340.

Protein family/group databases

TCDB9.B.10.1.1. the putative tripartite zn(2+) transporter (tzt) family.

Proteomic databases

PaxDbP94398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12128; CAB12128; BSU03340.
GeneID938325.
KEGGbsu:BSU03340.
PATRIC18972227. VBIBacSub10457_0342.

Organism-specific databases

GenoListBSU03340. [Micado]

Phylogenomic databases

eggNOGCOG1469.
HOGENOMHOG000280679.
KOK09007.
OrthoDBEOG6X6RBH.
PhylomeDBP94398.

Enzyme and pathway databases

BioCycBSUB:BSU03340-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_01527_B. GTP_cyclohydrol_B.
InterProIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamPF02649. GCHY-1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00294. TIGR00294. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCH4_BACSU
AccessionPrimary (citable) accession number: P94398
Secondary accession number(s): Q797Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList