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Q81SW2 (GCH1_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:BA_1532, GBAA_1532, BAS1421
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. 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 – 189189GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119382

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q81SW2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0A8B0379657B322B

FASTA18921,020
        10         20         30         40         50         60 
MAKVNLEQIE HAVRLILEAI GDDPNREGVL DTPKRVAKMY AEVFSGMHED PKEHLHKVFG 

        70         80         90        100        110        120 
EDHEELVLVK DIPFYSMCEH HLVPFYGVAH VAYIPQGGKV TGLSKLARTV DTIARRPQLQ 

       130        140        150        160        170        180 
ERITSTVANS IMEVLEPHGV MVVVEAEHMC MTMRGVKKPG AKTVTTAVRG VLENDAAARS 


EILSFIKTK 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP25469.1.
AE017334 Genomic DNA. Translation: AAT30630.1.
AE017225 Genomic DNA. Translation: AAT53741.1.
RefSeqNP_843983.1. NC_003997.3.
YP_018155.1. NC_007530.2.
YP_027690.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81SW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198094.BA_1532.

Protocols and materials databases

DNASU1086534.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP25469; AAP25469; BA_1532.
AAT30630; AAT30630; GBAA_1532.
AAT53741; AAT53741; BAS1421.
GeneID1086534.
2817519.
2849638.
KEGGban:BA_1532.
bar:GBAA_1532.
bat:BAS1421.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OMAKRTYDEE.
OrthoDBEOG6XHC8G.

Enzyme and pathway databases

BioCycANTHRA:MTRA-MONOMER.
BANT260799:GJAJ-1495-MONOMER.
BANT261594:GJ7F-1557-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[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_BACAN
AccessionPrimary (citable) accession number: Q81SW2
Secondary accession number(s): Q6I141, Q6KUZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways