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UniProtKB/Swiss-Prot entry Q7NYZ2


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

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Entry information
Entry name GCH1_CHRVO
Primary accession number Q7NYZ2
Secondary accession numbers None
Integrated into Swiss-Prot on January 16, 2004
Sequence was last modified on December 15, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 45)
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: CV_1130
From
Chromobacterium violaceum [TaxID: 536] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Chromobacterium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131;
DOI=10.1073/pnas.1832124100; PubMed=14500782 [NCBI, ExPASy, EBI, Israel, Japan]
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability.";
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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
AE016825; AAQ58805.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_900800.1; -.
3D structure databases
ModBase Q7NYZ2.
Enzyme and pathway databases
BioCyc CVIO243365:CV_1130-MON; -.
Ontologies
GO
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: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 IPR002110; ANK.
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.
PRINTS PR01415; ANKYRIN.
ProDom PD003330; GTP_cyclohydroI; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00859; GTP_CYCLOHYDROL_1_1; 1.
PS00860; GTP_CYCLOHYDROL_1_2; FALSE_NEG.
BLOCKS Q7NYZ2.
ProtoNet Q7NYZ2.
Genome annotation databases
GeneID 2550409; -.
GenomeReviews AE016825_GR; CV_1130.
KEGG cvi:CV_1130; -.
NMPDR fig|243365.1.peg.1130; -.
Phylogenomic databases
HOGENOM Q7NYZ2; -.
Genome annotation databases
CMR Q7NYZ2; CV_1130.
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   206  206     GTP cyclohydrolase 1. PRO_0000119397
METAL   97    97        Zinc (By similarity). 
METAL   100   100        Zinc (By similarity). 
METAL   168   168        Zinc (By similarity). 
Sequence information
Length: 206 AA [This is the length of the unprocessed precursor] Molecular weight: 23162 Da [This is the MW of the unprocessed precursor] CRC64: 800443D34D495DBD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSFTDDHDHA ACQRPLERVR PFDAAAFERA VADMLTASGI AIDPIHTGKT AQRVRELWQK 

        70         80         90        100        110        120 
RLLDGYDTVP AEALGSGFAD ERRDMVVIRS LAVHGMCPHH LLPFRGVAHV AYLPGGRLHG 

       130        140        150        160        170        180 
FGRIARMVDA ISHRYTYQEW ITHEIARTLV EHGEARGAAC LIEAEQLCLL MGENRRGDER 

       190        200 
VITQCYAGDF ETDAEARNQF LRAIER 

Q7NYZ2 in FASTA format

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