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UniProtKB/Swiss-Prot entry Q8NM84


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GCH1_CORGL
Primary accession number Q8NM84
Secondary accession numbers None
Integrated into Swiss-Prot on October 10, 2002
Sequence was last modified on October 10, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name GTP cyclohydrolase 1
Synonyms EC 3.5.4.16
GTP cyclohydrolase I
GTP-CH-I
Gene name
Name: folE
OrderedLocusNames: Cgl2695, cg2983
From
Corynebacterium glutamicum (Brevibacterium flavum) [TaxID: 1718] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
Nakagawa S.;
"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan]
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.";
J. Biotechnol. 104:5-25(2003).
Comments
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
BA000036; BAC00089.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927156; CAF20718.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_601891.1; -.
YP_226934.1; -.
3D structure databases
HSSP P22288; 1IS8. [HSSP ENTRY / PDB]
ModBase Q8NM84.
Enzyme and pathway databases
BioCyc CGLU196627-1:CG2983-MON; -.
Ontologies
GO
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.
Pfam PF01227; GTP_cyclohydroI; 1.
Pfam graphical view of domain structure.
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.
ProtoNet Q8NM84.
Genome annotation databases
GeneID 1020642; -.
3344752; -.
GenomeReviews BX927147_GR; cg2983.
BA000036_GR; Cgl2695.
KEGG cgb:cg2983; -.
cgl:NCgl2602; -.
Phylogenomic databases
HOGENOM Q8NM84; -.
Genome annotation databases
CMR Q8NM84; Cgl2695.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; One-carbon metabolism; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   196  196     GTP cyclohydrolase 1. PRO_0000119401
METAL   84    84        Zinc (By similarity). 
METAL   87    87        Zinc (By similarity). 
METAL   157   157        Zinc (By similarity). 
Sequence information
Length: 196 AA [This is the length of the unprocessed precursor] Molecular weight: 21472 Da [This is the MW of the unprocessed precursor] CRC64: 7D88EE795426D7E7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDNHAAVREF DEERATAAIR ELLIAVGEDP DREGLLETPA RVARAYKETF AGLHEDPTTV 

        70         80         90        100        110        120 
LEKTFSEGHE ELVLVREIPI YSMCEHHLVP FFGVAHIGYI PGKSGKVTGL SKLARLADMF 

       130        140        150        160        170        180 
AKRPQVQERL TSQIADALVE KLDAQAVAVV IEAEHLCMAM RGIRKPGAVT TTSAVRGGFK 

       190 
NNAASRAEVF SLIRGH 

Q8NM84 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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