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UniProtKB/Swiss-Prot entry B0KLM9

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

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Entry information
Entry name FOLD2_PSEPG
Primary accession number B0KLM9
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on March 18, 2008 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 6)
Name and origin of the protein
Protein name Bifunctional protein folD 2
Synonyms None
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene name
Name: folD2
OrderedLocusNames: PputGB1_2105
From
Pseudomonas putida (strain GB-1) [TaxID: 76869] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
"Complete sequence of Pseudomonas putida GB-1.";
Submitted (JAN-2008) 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
CP000926; ABY98006.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001668342.1; -.
3D structure databases
ModBase B0KLM9.
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).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086; Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006164; Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
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; FALSE_NEG.
PS00767; THF_DHG_CYH_2; 1.
BLOCKS B0KLM9.
ProtoNet B0KLM9.
Genome annotation databases
GeneID 5869894; -.
GenomeReviews CP000926_GR; PputGB1_2105.
KEGG ppg:PputGB1_2105; -.
CMR B0KLM9; PputGB1_2105.
Other
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   303  303     Bifunctional protein folD 2. PRO_0000340591
Sequence information
Length: 303 AA [This is the length of the unprocessed precursor] Molecular weight: 32148 Da [This is the MW of the unprocessed precursor] CRC64: 250DDB49D2466032 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNALTSLKLI DGKATAARVL AEVREQVQEL RQGGVQPGLV VVLVGADAAS QVYVRNKVLR 

        70         80         90        100        110        120 
AEEVGIRSQE HRLPADTTQA HLLTLIDRLN RDPEVNGILV QLPLPAHIDE HCVLQAINPL 

       130        140        150        160        170        180 
KDVDGFHSEN VGGLAQGRDV LTPCTPSGCM RLLRDACGEL RGKHAVVVGR SNIVGKPMAA 

       190        200        210        220        230        240 
LLLQADCTVT VVHSRSRDLP ALCRQADILV AAVGKPRLIG ADCLKPGAVV IDVGINRINE 

       250        260        270        280        290        300 
DGQNHLVGDV DFAAALPQVA GITPVPGGVG PMTIAYLMKN TLLALDLQQQ AAHQERTACL 


SPC
B0KLM9 in FASTA format

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