P94398 (GCH4_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	GTP cyclohydrolase I activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	GTP cyclohydrolase folE2 HAMAP-Rule MF_01527_B		PRO_0000147701
Sites
	Site	183	1	May be catalytically important By similarity
Experimental info
	Sequence conflict	202 – 209	8	SIWADIHP → KHLGRIFTR in BAA08968. Ref.1
	Sequence conflict	222	1	L → P in BAA08968. Ref.1
	Sequence conflict	290 – 295	6	DAYAKL → RCLCEV in BAA08968. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P94398 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 90A28F90FE9BDAB3	FASTA	304	34,564
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	H69759.
RefSeq	NP_388216.2. NC_000964.3.
3D structure databases
ProteinModelPortal	P94398.
SMR	P94398. Positions 44-298.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-8366745.
STRING	224308.BSU03340.
Protein family/group databases
TCDB	9.B.10.1.1. putative tripartite Zn2+ transporter (TZT) family.
Proteomic databases
PaxDb	P94398.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB12128; CAB12128; BSU03340.
GeneID	938325.
KEGG	bsu:BSU03340.
PATRIC	18972227. VBIBacSub10457_0342.
Organism-specific databases
GenoList	BSU03340. [Micado]
Phylogenomic databases
eggNOG	COG1469.
HOGENOM	HOG000280679.
KO	K09007.
ProtClustDB	PRK13674.
Enzyme and pathway databases
BioCyc	BSUB:BSU03340-MONOMER.
UniPathway	UPA00848; UER00151.
Family and domain databases
Gene3D	3.10.270.10. 1 hit.
HAMAP	MF_01527_B. GTP_cyclohydrol_B.
InterPro	IPR022838. GTP_cyclohydrolase_FolE2. IPR003801. GTP_cyclohydrolase_FolE2/MptA. IPR002042. Uricase. [Graphical view]
Pfam	PF02649. GCHY-1. 1 hit. [Graphical view]
TIGRFAMs	TIGR00294. TIGR00294. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GCH4_BACSU

Accession

Primary (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:	May 29, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program