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UniProtKB/Swiss-Prot entry Q39Z32


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

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Entry information
Entry name FOLD1_GEOMG
Primary accession number Q39Z32
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 22)
Name and origin of the protein
Protein name Bifunctional protein folD 1
Synonyms None
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene name
Name: folD1
OrderedLocusNames: Gmet_0247
From
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [TaxID: 269799] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; Geobacteraceae; Geobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Geobacter metallireducens GS-15.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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
CP000148; ABB30492.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_383217.1; -.
3D structure databases
ModBase Q39Z32.
Enzyme and pathway databases
BioCyc GMET269799:GMET_0247-MON; -.
Ontologies
GO
GO:0004477; Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004488; Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01576; -; 1.
PBIL [Tree]
InterPro IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; FALSE_NEG.
BLOCKS Q39Z32.
Genome annotation databases
GeneID 3739710; -.
GenomeReviews CP000148_GR; Gmet_0247.
KEGG gme:Gmet_0247; -.
NMPDR fig|269799.3.peg.277; -.
Phylogenomic databases
HOGENOM Q39Z32; -.
Genome annotation databases
CMR Q39Z32; Gmet_0247.
Other
ProtoNet Q39Z32.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   290  290     Bifunctional protein folD 1. PRO_0000268358
Sequence information
Length: 290 AA [This is the length of the unprocessed precursor] Molecular weight: 31744 Da [This is the MW of the unprocessed precursor] CRC64: 2D245E593E767DE7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLLDGKKCA ESLVADIARK VAGYEESGLR KPHMTVILVG EHAPSESYVK SKIKSCGNAG 

        70         80         90        100        110        120 
FEGTLLRFPD TITEAELLEK IRGINADPTT DGLIVQLPLP RHINQQHIIN AIAPEKDIDG 

       130        140        150        160        170        180 
FHPTNFGRMT LGQKAFRPAT AYGICKLLQF YEIPVWGKHC VVIGRSNIVG KPISIMLSND 

       190        200        210        220        230        240 
FDIGNATVTL THIETPRELL LDETRRADIV IVAVGIPGFV TEDMVKEGVV VIDVGINRLE 

       250        260        270        280        290 
DGKIVGDVDF ENVKKKCSWI TPVPGGVGRM TVAALMINTL MAYQNNFDLV 

Q39Z32 in FASTA format

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

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