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P19465

- GCH1_BACSU

UniProt

P19465 - GCH1_BACSU

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Protein

GTP cyclohydrolase 1

Gene
folE, mtrA, BSU22780
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

K+ ions moderately increases the Vmax, whereas UTP and Ca2+ and Mg2+ ions drastically increase the Km for GTP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi78 – 781Zinc By similarity
Metal bindingi81 – 811Zinc By similarity
Metal bindingi150 – 1501Zinc By similarity

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

BioCyciBSUB:BSU22780-MONOMER.
MetaCyc:BSU22780-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1 (EC:3.5.4.16)
Alternative name(s):
GTP cyclohydrolase I
Short name:
GTP-CH-I
Gene namesi
Name:folE
Synonyms:mtrA
Ordered Locus Names:BSU22780
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU22780. [Micado]

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190GTP cyclohydrolase 1UniRule annotationPRO_0000119386Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi224308.BSU22780.

Structurei

3D structure databases

ProteinModelPortaliP19465.
SMRiP19465. Positions 2-188.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000221222.
KOiK01495.
OMAiYEQIEYA.
OrthoDBiEOG6XHC8G.
PhylomeDBiP19465.

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.

P19465-1 [UniParc]FASTAAdd to Basket

« Hide

MKEVNKEQIE QAVRQILEAI GEDPNREGLL DTPKRVAKMY AEVFSGLNED    50
PKEHFQTIFG ENHEELVLVK DIAFHSMCEH HLVPFYGKAH VAYIPRGGKV 100
TGLSKLARAV EAVAKRPQLQ ERITSTIAES IVETLDPHGV MVVVEAEHMC 150
MTMRGVRKPG AKTVTSAVRG VFKDDAAARA EVLEHIKRQD 190
Length:190
Mass (Da):21,219
Last modified:February 1, 1991 - v1
Checksum:iE912535CC67A5551
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37320 Genomic DNA. Translation: AAA22615.1.
M80245 Genomic DNA. Translation: AAA20852.1.
AL009126 Genomic DNA. Translation: CAB14194.1.
X52418 Genomic DNA. No translation available.
PIRiA38256.
RefSeqiNP_390159.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14194; CAB14194; BSU22780.
GeneIDi938994.
KEGGibsu:BSU22780.
PATRICi18976367. VBIBacSub10457_2374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37320 Genomic DNA. Translation: AAA22615.1 .
M80245 Genomic DNA. Translation: AAA20852.1 .
AL009126 Genomic DNA. Translation: CAB14194.1 .
X52418 Genomic DNA. No translation available.
PIRi A38256.
RefSeqi NP_390159.1. NC_000964.3.

3D structure databases

ProteinModelPortali P19465.
SMRi P19465. Positions 2-188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU22780.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14194 ; CAB14194 ; BSU22780 .
GeneIDi 938994.
KEGGi bsu:BSU22780.
PATRICi 18976367. VBIBacSub10457_2374.

Organism-specific databases

GenoListi BSU22780. [Micado ]

Phylogenomic databases

HOGENOMi HOG000221222.
KOi K01495.
OMAi YEQIEYA.
OrthoDBi EOG6XHC8G.
PhylomeDBi P19465.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci BSUB:BSU22780-MONOMER.
MetaCyc:BSU22780-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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGCH1_BACSU
AccessioniPrimary (citable) accession number: P19465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 110 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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