P19465 (GCH1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP MF_00223
Enzyme regulation	K+ ions moderately increases the Vmax, whereas UTP and Ca2+ and Mg2+ ions drastically increase the Km for GTP. HAMAP MF_00223
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP 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.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	GTP cyclohydrolase 1 HAMAP MF_00223		PRO_0000119386
Sites
	Metal binding	78	1	Zinc By similarity
	Metal binding	81	1	Zinc By similarity
	Metal binding	150	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19465 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: E912535CC67A5551	FASTA	190	21,219
	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

References

	« Hide 'large scale' referencesShow '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: 2123343] [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: 9384377] [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: 1902464] [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: 1551827] [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: 7887891] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

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.
PIR	A38256.
RefSeq	NP_390159.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P19465.
SMR	P19465. Positions 2-188.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003639; EBBACP00000003639; EBBACG00000003632.
GeneID	938994.
GenomeReviews	Gene locus BSU22780 in contig AL009126_GR.
KEGG	bsu:BSU22780.
NMPDR	fig|224308.1.peg.2282.
PATRIC	18976367. VBIBacSub10457_2374.
Organism-specific databases
GenoList	BSU22780. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002882.
HOGENOM	HBG370191.
OMA	LPFMGRA.
PhylomeDB	P19465.
ProtClustDB	PRK09347.
Enzyme and pathway databases
BioCyc	BSUB:BSU22780-MONOMER. MetaCyc:BSU22780-MONOMER.
Family and domain databases
HAMAP	MF_00223. FolE. [Tree]
InterPro	IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view]
KO	K01495.
PANTHER	PTHR11109. GTP_cyclohydro_I. 1 hit.
Pfam	PF01227. GTP_cyclohydroI. 1 hit. [Graphical view]
TIGRFAMs	TIGR00063. FolE. 1 hit.
PROSITE	PS00859. GTP_CYCLOHYDROL_1_1. 1 hit. PS00860. GTP_CYCLOHYDROL_1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCH1_BACSU

Accession

Primary (citable) accession number: P19465

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program