GTP cyclohydrolase 1 - Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

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P51599 (GCH1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

ORF Names:

104H10.80, NCU07774

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.
Catalytic activity	GTP + H₂O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
Enzyme regulation	GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity By similarity.
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
Subunit structure	Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.
Sequence similarities	Belongs to the GTP cyclohydrolase I family.
Sequence caution	The sequence EAA29459.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Folate biosynthesis
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway folic acid biosynthetic 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 – 313

313

GTP cyclohydrolase 1

PRO_0000119486

Sites

Metal binding

202

Zinc By similarity

Metal binding

205

Zinc By similarity

Metal binding

273

Zinc By similarity

Experimental info

Sequence conflict

186 – 188

GHN → DHD in CAA89828. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P51599 [UniParc].

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

313

34,471

        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' referencesShow '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. 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. AABX02000046 Genomic DNA. Translation: EAA29459.2. Different initiation. Z49758 mRNA. Translation: CAA89828.1.
RefSeq	XP_958695.2. XM_953602.2.
3D structure databases
ProteinModelPortal	P51599.
SMR	P51599. Positions 124-310.
ModBase	Search...
Protein-protein interaction databases
STRING	5141.NCU07774.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000007952; EFNCRP00000007941; EFNCRG00000007940.
GeneID	3874842.
KEGG	ncr:NCU07774.
Phylogenomic databases
eggNOG	COG0302.
HOGENOM	HOG000221222.
KO	K01495.
OrthoDB	EOG4643MV.
Enzyme and pathway databases
UniPathway	UPA00848; UER00151.
Family and domain databases
InterPro	IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view]
PANTHER	PTHR11109. PTHR11109. 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_NEUCR

Accession

Primary (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:	April 3, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents