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P94398

- GCH4_BACSU

UniProt

P94398 - GCH4_BACSU

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Protein
GTP cyclohydrolase FolE2
Gene
folE2, yciA, BSU03340
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate.1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei183 – 1831May be catalytically important By similarity

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

BioCyciBSUB:BSU03340-MONOMER.
UniPathwayiUPA00848; UER00151.

Protein family/group databases

TCDBi9.B.10.1.1. the putative tripartite zn(2+) transporter (tzt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2 (EC:3.5.4.16)
Alternative name(s):
GTP cyclohydrolase 1B
Gene namesi
Name:folE2
Synonyms:yciA
Ordered Locus Names:BSU03340
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU03340. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304GTP cyclohydrolase FolE2UniRule annotation
PRO_0000147701Add
BLAST

Proteomic databases

PaxDbiP94398.

Expressioni

Inductioni

Repressed by zinc, via zur.1 Publication

Interactioni

Protein-protein interaction databases

IntActiP94398. 1 interaction.
MINTiMINT-8366745.
STRINGi224308.BSU03340.

Structurei

3D structure databases

ProteinModelPortaliP94398.
SMRiP94398. Positions 44-298.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OrthoDBiEOG6X6RBH.
PhylomeDBiP94398.

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]
TIGRFAMsiTIGR00294. TIGR00294. 1 hit.

Sequencei

Sequence statusi: Complete.

P94398-1 [UniParc]FASTAAdd to Basket

« Hide

MNQHTLLPKK TERLQYFGSV SPIKGEKPVE KEKMKDLQNI RKDYFFDIQH    50
VGVANVSHPV TITSAMMPAE QTTAANFTMT CNLPRNQKGI NMSRLTELLQ 100
VYHQNGWILS FSSLQQFTKE LAENMDTSSA TVEVRFPWFF ERKSPKLEKA 150
GLMHADIFMS VTYRKDQPFK QRAGISAKVT TLCPCSKEIS EYSAHNQRGT 200
VSIWADIHPA ASLPSDVKAD LLHAAESNAS ARLHPVLKRP DEKAVTETAY 250
ENPRFVEDLA RLIAADLFEL EWVSAFEIEC RNEESIHLHD AYAKLCFSKE 300
VDKI 304
Length:304
Mass (Da):34,564
Last modified:June 16, 2009 - v2
Checksum:i90A28F90FE9BDAB3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2098SIWADIHP → KHLGRIFTR in BAA08968. 1 Publication
Sequence conflicti222 – 2221L → P in BAA08968. 1 Publication
Sequence conflicti290 – 2956DAYAKL → RCLCEV in BAA08968. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50453 Genomic DNA. Translation: BAA08968.1.
AL009126 Genomic DNA. Translation: CAB12128.2.
PIRiH69759.
RefSeqiNP_388216.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12128; CAB12128; BSU03340.
GeneIDi938325.
KEGGibsu:BSU03340.
PATRICi18972227. VBIBacSub10457_0342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50453 Genomic DNA. Translation: BAA08968.1 .
AL009126 Genomic DNA. Translation: CAB12128.2 .
PIRi H69759.
RefSeqi NP_388216.2. NC_000964.3.

3D structure databases

ProteinModelPortali P94398.
SMRi P94398. Positions 44-298.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P94398. 1 interaction.
MINTi MINT-8366745.
STRINGi 224308.BSU03340.

Protein family/group databases

TCDBi 9.B.10.1.1. the putative tripartite zn(2+) transporter (tzt) family.

Proteomic databases

PaxDbi P94398.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12128 ; CAB12128 ; BSU03340 .
GeneIDi 938325.
KEGGi bsu:BSU03340.
PATRICi 18972227. VBIBacSub10457_0342.

Organism-specific databases

GenoListi BSU03340. [Micado ]

Phylogenomic databases

eggNOGi COG1469.
HOGENOMi HOG000280679.
KOi K09007.
OrthoDBi EOG6X6RBH.
PhylomeDBi P94398.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci BSUB:BSU03340-MONOMER.

Family and domain databases

HAMAPi MF_01527_B. GTP_cyclohydrol_B.
InterProi IPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view ]
Pfami PF02649. GCHY-1. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00294. TIGR00294. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiGCH4_BACSU
AccessioniPrimary (citable) accession number: P94398
Secondary accession number(s): Q797Q1
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally (1 Publication) thought to be a zinc uptake system.

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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