[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Seshadri R., Samuel J.E., Myers G., Kim M., Huot H., Durkin A.S., Dodson R.J., Daugherty S.C., Li J., Harkins D.; Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: GTP + H₂O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
PATHWAY: Cofactor biosynthesis; dihydroneopterin triphosphate biosynthesis; 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate from GTP: step 1/1 .
SUBUNIT: Homopolymer (By similarity).
SIMILARITY: Belongs to the GTP cyclohydrolase I family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000733; ABS76861.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001424247.2; -.

3D structure databases

ModBase

A9KFF3.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0003934;	Molecular function: GTP cyclohydrolase I activity (inferred from electronic annotation from HAMAP).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019438;	Biological process: aromatic compound biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from HAMAP).
GO:0046654;	Biological process: tetrahydrofolate biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00223; -; 1.
PBIL [Tree]

InterPro

IPR001474; GTP_CycOHase_I.
Graphical view of domain structure.

PANTHER

PTHR11109; GTP_cyclohydro_I; 1.

ProDom

PD003330; GTP_cyclohydroI; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00063; folE; 1.

PROSITE

PS00859; GTP_CYCLOHYDROL_1_1; 1.
PS00860; GTP_CYCLOHYDROL_1_2; 1.

Genome annotation databases

GeneID

5457661; -.

GenomeReviews

CP000733_GR; CBUD_0863.

KEGG

cbd:CBUD_0863; -.

CMR

A9KFF3; CBUD_0863.

Other

ProtoNet

A9KFF3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; Metal-binding; One-carbon metabolism; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 184`	`184`	`GTP cyclohydrolase 1.`	`PRO_1000078138`
`METAL`	`75 75`		`Zinc (By similarity).`
`METAL`	`78 78`		`Zinc (By similarity).`
`METAL`	`146 146`		`Zinc (By similarity).`

Sequence information

Length: 184 AA [This is the length of the unprocessed precursor]

Molecular weight: 20777 Da [This is the MW of the unprocessed precursor]

CRC64: C69EA3EA9C15ABA4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNTIADHVK AILIALGEDP NREGLRDTPK RYEKALEHLT KGYHEKLPSV VKKAVFQSGM 

        70         80         90        100        110        120 
DEMVILKDIE LYSLCEHHLL PFIGRCHVAY LPSGKIIGIS KLARIVDMFA KRLQVQENLT 

       130        140        150        160        170        180 
KQIAEAILTA TEAKGVGVII EAKHLCMMMR GVEKQNSEMT TSVMLGTFRK DDRTRSEFLS 


LIRK

A9KFF3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools