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P48596 (GCH1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Protein punch
Gene names
Name:Pu
ORF Names:CG9441
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Isoform B is required for eye pigment production, Isoform C may be required for normal embryonic development and segment pattern formation. Ref.1

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.

Tissue specificity

Isoform B is expressed almost exclusively in adult heads. Ref.1

Developmental stage

Isoform C is expressed in embryos, larvae and adults. Ref.1

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence caution

The sequence AAC04308.1 differs from that shown. Reason: Frameshift at positions 27, 75, 266 and 271.

The sequence AAC04309.1 differs from that shown. Reason: Frameshift at positions 27, 75, 266 and 271.

The sequence AAD44334.1 differs from that shown. Reason: Frameshift at positions 27, 75, 266 and 271.

The sequence AAR20857.2 differs from that shown. Reason: Frameshift at position 53.

Ontologies

Keywords
   Biological processTetrahydrobiopterin biosynthesis
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7,8-dihydroneopterin 3'-triphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

compound eye pigmentation

Inferred from mutant phenotype PubMed 3136053. Source: FlyBase

cuticle pigmentation

Inferred from mutant phenotype PubMed 3115849. Source: FlyBase

embryonic pattern specification

Inferred from mutant phenotype PubMed 3115849. Source: FlyBase

larval chitin-based cuticle development

Inferred from mutant phenotype PubMed 3115849. Source: FlyBase

preblastoderm mitotic cell cycle

Inferred from mutant phenotype PubMed 7706401. Source: FlyBase

pteridine biosynthetic process

Inferred from mutant phenotype PubMed 7706401. Source: FlyBase

regulation of GTP cyclohydrolase I activity

Inferred from direct assay PubMed 16966327. Source: FlyBase

regulation of epithelial cell migration, open tracheal system

Inferred from mutant phenotype PubMed 17585895. Source: FlyBase

tetrahydrobiopterin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 7706401. Source: FlyBase

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP cyclohydrolase I activity

Inferred from direct assay PubMed 16966327PubMed 3080426PubMed 3136053. Source: FlyBase

GTP cyclohydrolase I regulator activity

Inferred from direct assay PubMed 16966327. Source: FlyBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P48596-1)

Also known as: C;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P48596-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: MSFTRQLSEM...PLTPRTSTTP → MKPQTSEQNG...LNLELASNGS
Isoform C (identifier: P48596-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-117: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119482

Sites

Metal binding2141Zinc By similarity
Metal binding2171Zinc By similarity
Metal binding2851Zinc By similarity

Natural variations

Alternative sequence1 – 117117MSFTR…TSTTP → MKPQTSEQNGSGQNGEGAAD AVAVATIPTGEASAASATSG TDLTVSKNSQQLKLEMLNLE LASNGS in isoform B.
VSP_001616
Alternative sequence102 – 11716Missing in isoform C.
VSP_001615
Natural variant581A → T in strain: Raleigh Inbred 6, Raleigh Inbred 9, Raleigh Inbred 11, Raleigh Inbred 27 and Raleigh Inbred 33. Ref.3
Natural variant611A → P in strain: Raleigh Inbred 6, Raleigh Inbred 9, Raleigh Inbred 11, Raleigh Inbred 27 and Raleigh Inbred 33. Ref.3
Natural variant771A → V in strain: Raleigh Inbred 11. Ref.3
Natural variant841N → S in strain: Raleigh Inbred 6, Raleigh Inbred 9, Raleigh Inbred 11 and Raleigh Inbred 33. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A (C) [UniParc].

Last modified January 27, 2003. Version 3.
Checksum: 712A0045F2C12D6A

FASTA32435,541
        10         20         30         40         50         60 
MSFTRQLSEM SASELNDAID DTNFPQAHIL SRGRNNSVCS TSSTSGTSSL ADRQQNQAEE 

        70         80         90        100        110        120 
ATAIAGTPVE EVAPAPALVP LAGNQRPRLI LKTNGSSPDS DGTQPKTPLT PRTSTTPGHE 

       130        140        150        160        170        180 
KCTFHHDLEL DHKPPTREAL LPDMARSYRL LLGGLGENPD RQGLIKTPER AAKAMLYFTK 

       190        200        210        220        230        240 
GYDQSLEDVL NGAVFDEDHD EMVVVKDIEM FSMCEHHLVP FYGKVSIGYL PCNKILGLSK 

       250        260        270        280        290        300 
LARIVEIFSR RLQVQERLTK QIAVAVTQAV QPAGVAVVVE GVHMCMVMRG VQKINSKTVT 

       310        320 
STMLGVFRDD PKTREEFLNL VNSK 

« Hide

Isoform B [UniParc].

Checksum: 99B3DA99E8D4B2C2
Show »

FASTA27329,812
Isoform C [UniParc].

Checksum: A142F66EDE6D3969
Show »

FASTA30833,877

References

« Hide 'large scale' references
[1]"Multiple mRNAs from the Punch locus of Drosophila melanogaster encode isoforms of GTP cyclohydrolase I with distinct N-terminal domains."
McLean J.R., Krishnakumar S., O'Donnell J.M.
J. Biol. Chem. 268:27191-27197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Head.
[2]"Differential regulation of Drosophila GTP cyclohydrolase I isoforms and their interaction with tyrosine hydroxylase."
Xu D., Neckameyer W., O'Donnell J.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Embryo.
[3]"Punch affects life history traits in Drosophila melanogaster."
Geiger-Thornsberry G.L., Harbison S.T., Lyman R.F., Mackay T.F.C.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-58; PRO-61; VAL-77 AND SER-84.
Strain: Raleigh Inbred 1, Raleigh Inbred 11, Raleigh Inbred 24, Raleigh Inbred 27, Raleigh Inbred 30, Raleigh Inbred 33, Raleigh Inbred 6 and Raleigh Inbred 9.
[4]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01118 mRNA. Translation: AAC04308.1. Frameshift.
U01119 mRNA. Translation: AAC04309.1. Frameshift.
AF159422 mRNA. Translation: AAD44334.1. Frameshift.
AY382619 Genomic DNA. Translation: AAR20848.1.
AY382620 Genomic DNA. Translation: AAR20850.1.
AY382622 Genomic DNA. Translation: AAR20852.1.
AY382623 Genomic DNA. Translation: AAR20854.1.
AY382624 Genomic DNA. Translation: AAR20855.1.
AY382625 Genomic DNA. Translation: AAR20857.2. Frameshift.
AY382626 Genomic DNA. Translation: AAR20859.1.
AY382628 Genomic DNA. Translation: AAR20862.1.
AE013599 Genomic DNA. Translation: AAF46690.1.
AE013599 Genomic DNA. Translation: AAF46692.1.
AE013599 Genomic DNA. Translation: AAM70858.1.
AY051890 mRNA. Translation: AAK93314.1.
PIRA49302.
B49302.
RefSeqNP_523801.2. NM_079077.4. [P48596-3]
NP_726037.1. NM_166430.3. [P48596-2]
NP_726038.1. NM_166431.4. [P48596-1]
UniGeneDm.7417.

3D structure databases

ProteinModelPortalP48596.
SMRP48596. Positions 138-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid63049. 3 interactions.
DIPDIP-24104N.
MINTMINT-937025.

Proteomic databases

PaxDbP48596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071580; FBpp0071507; FBgn0003162. [P48596-1]
GeneID37415.
KEGGdme:Dmel_CG9441.

Organism-specific databases

CTD37415.
FlyBaseFBgn0003162. Pu.

Phylogenomic databases

eggNOGCOG0302.
GeneTreeENSGT00390000013481.
InParanoidP48596.
KOK01495.
OMANTRTEIE.
OrthoDBEOG77DJ6T.
PhylomeDBP48596.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-18450.
UniPathwayUPA00848; UER00151.

Gene expression databases

BgeeP48596.

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...

Other

ChiTaRSPu. drosophila.
GenomeRNAi37415.
NextBio803517.
PROP48596.

Entry information

Entry nameGCH1_DROME
AccessionPrimary (citable) accession number: P48596
Secondary accession number(s): Q6TY66 expand/collapse secondary AC list , Q6TY71, Q6TY73, Q6TY74, Q6TY78, Q960S4, Q9W2J9, Q9W2K1, Q9Y0C8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 27, 2003
Last modified: July 9, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase