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P19465 (GCH1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 1
EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
Gene names
Name:folE
Synonyms:mtrA
Ordered Locus Names:BSU22780
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_00223

Enzyme regulation

K+ ions moderately increases the Vmax, whereas UTP and Ca2+ and Mg2+ ions drastically increase the Km for GTP. HAMAP-Rule MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_00223

Subunit structure

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

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119386

Sites

Metal binding781Zinc By similarity
Metal binding811Zinc By similarity
Metal binding1501Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P19465 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: E912535CC67A5551

FASTA19021,219
        10         20         30         40         50         60 
MKEVNKEQIE QAVRQILEAI GEDPNREGLL DTPKRVAKMY AEVFSGLNED PKEHFQTIFG 

        70         80         90        100        110        120 
ENHEELVLVK DIAFHSMCEH HLVPFYGKAH VAYIPRGGKV TGLSKLARAV EAVAKRPQLQ 

       130        140        150        160        170        180 
ERITSTIAES IVETLDPHGV MVVVEAEHMC MTMRGVRKPG AKTVTSAVRG VFKDDAAARA 

       190 
EVLEHIKRQD

« Hide

References

« Hide 'large scale' references
[1]"The mtr locus is a two-gene operon required for transcription attenuation in the trp operon of Bacillus subtilis."
Gollnick P., Ishino S., Kuroda M.I., Henner D.J., Yanofsky C.
Proc. Natl. Acad. Sci. U.S.A. 87:8726-8730(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]"Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu."
Micka B., Groch N., Heinemann U., Marahiel M.A.
J. Bacteriol. 173:3191-3198(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
Strain: 168 / JH642.
[4]"The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis."
Babitzke P., Gollnick P., Yanofsky C.
J. Bacteriol. 174:2059-2064(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Enzymic characterization of Bacillus subtilis GTP cyclohydrolase I. Evidence for a chemical dephosphorylation of dihydroneopterin triphosphate."
de Saizieu A., Vankan P., van Loon A.P.
Biochem. J. 306:371-377(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M37320 Genomic DNA. Translation: AAA22615.1.
M80245 Genomic DNA. Translation: AAA20852.1.
AL009126 Genomic DNA. Translation: CAB14194.1.
X52418 Genomic DNA. No translation available.
PIRA38256.
RefSeqNP_390159.1. NC_000964.3.

3D structure databases

ProteinModelPortalP19465.
SMRP19465. Positions 2-188.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU22780.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14194; CAB14194; BSU22780.
GeneID938994.
KEGGbsu:BSU22780.
PATRIC18976367. VBIBacSub10457_2374.

Organism-specific databases

GenoListBSU22780. [Micado]

Phylogenomic databases

HOGENOMHOG000221222.
KOK01495.
OMALIRHQPA.
ProtClustDBPRK09347.

Enzyme and pathway databases

BioCycBSUB:BSU22780-MONOMER.
MetaCyc:BSU22780-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
IPR018234. GTP_CycHdrlase_I_CS.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCH1_BACSU
AccessionPrimary (citable) accession number: P19465
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents