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P51599 (GCH1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 90. 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:gch-1
ORF Names:104H10.80, NCU07774
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid. HAMAP-Rule MF_00223

Catalytic activity

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

Enzyme regulation

GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity By similarity. 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 – 313313GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119486

Sites

Metal binding2021Zinc By similarity
Metal binding2051Zinc By similarity
Metal binding2731Zinc By similarity

Experimental info

Sequence conflict186 – 1883GHN → DHD in CAA89828. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P51599 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: C8535C0A7FF84114

FASTA31334,471
        10         20         30         40         50         60 
MAQETTRDGS DSPSGSVSPP IANGTNNKKD KKSSKKRAHS SGERRSSVSK PARDPSDKPE 

        70         80         90        100        110        120 
ESPSKKKKRK TTSSTAAAAV PSTITEEVSP STSVTRSPSP VIDFDGLSRP SRGTRERLEE 

       130        140        150        160        170        180 
TEAQKQERLD KMKGAVRTLL ECIGEDPDRE GLLATPERYA KAMLFLTKGY QENVRDIVNG 

       190        200        210        220        230        240 
AIFQEGHNEM VIVKDIEVFS MCEHHLVPFT GKMHIGYIPS NAVIGISKLP RIAELFARRL 

       250        260        270        280        290        300 
QIQERLTKEV ANAIMEILKP QGVAVVMESS HLCMVMRGVQ KTTSSTITSC VLGCFESREK 

       310 
TRLEFLSLIG VNR 

« Hide

References

« Hide 'large scale' references
[1]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers."
Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.
Biochem. Biophys. Res. Commun. 212:705-711(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 185-278.
Strain: BD AL-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513410 Genomic DNA. Translation: CAC28574.1.
CM002240 Genomic DNA. Translation: EAA29459.3.
Z49758 mRNA. Translation: CAA89828.1.
RefSeqXP_958695.2. XM_953602.2.

3D structure databases

ProteinModelPortalP51599.
SMRP51599. Positions 124-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU07774.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000007952; EFNCRP00000007941; EFNCRG00000007940.
GeneID3874842.
KEGGncr:NCU07774.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
KOK01495.
OrthoDBEOG7QRR5W.

Enzyme and pathway databases

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_NEUCR
AccessionPrimary (citable) accession number: P51599
Secondary accession number(s): Q7RV90, Q9C2R6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 30, 2003
Last modified: March 19, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways