ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8NR14


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name K6PF_CORGL
Primary accession number Q8NR14
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on October 19, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name 6-phosphofructokinase
Synonyms Phosphofructokinase
EC 2.7.1.11
Phosphohexokinase
Gene name
Name: pfkA
OrderedLocusNames: Cgl1250, cg1409
From
Corynebacterium glutamicum (Brevibacterium flavum) [TaxID: 1718] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 1: Evidence at protein level;
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; BAB98643.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927151; CAF19953.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_600473.1; -.
YP_225539.1; -.
3D structure databases
HSSP P00512; 3PFK. [HSSP ENTRY / PDB]
ModBase Q8NR14.
Enzyme and pathway databases
BioCyc CGLU196627-1:CG1409-MON; -.
2D gel databases
World-2DPAGE 0001:Q8NR14; -.
Ontologies
GO
GO:0005945; Cellular component: 6-phosphofructokinase complex (inferred from electronic annotation from InterPro).
GO:0003872; Molecular function: 6-phosphofructokinase activity (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006002; Biological process: fructose 6-phosphate metabolic process (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00339; -; 1.
PBIL [Tree]
InterPro IPR012003; ATP_PFK_prok.
IPR012829; PFK.
IPR015912; Phosphofructokinase_CS.
IPR000023; Ppfruckinase.
Graphical view of domain structure.
PANTHER PTHR13697; Ppfruckinase; 1.
Pfam PF00365; PFK; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000532; ATP_PFK_prok; 1.
PRINTS PR00476; PHFRCTKINASE.
ProDom PD000707; Ppfruckinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02483; PFK_mixed; 1.
PROSITE PS00433; PHOSPHOFRUCTOKINASE; 1.
ProtoNet Q8NR14.
Genome annotation databases
GeneID 1019232; -.
3344017; -.
GenomeReviews BX927147_GR; cg1409.
BA000036_GR; Cgl1250.
KEGG cgb:cg1409; -.
cgl:NCgl1202; -.
Phylogenomic databases
HOGENOM Q8NR14; -.
Genome annotation databases
CMR Q8NR14; Cgl1250.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   346  346     6-phosphofructokinase. PRO_0000111948
NP_BIND   23    27  5     ATP (By similarity). 
NP_BIND   158   162  5     ATP (By similarity). 
NP_BIND   175   191  17     ATP (By similarity). 
ACT_SITE   131   131        Proton acceptor (By similarity). 
METAL   189   189        Magnesium; via carbonyl oxygen (By similarity). 
BINDING   166   166        Substrate (By similarity). 
BINDING   270   270        Substrate (By similarity). 
BINDING   276   276        Substrate (By similarity). 
BINDING   279   279        Substrate (By similarity). 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 37464 Da [This is the MW of the unprocessed precursor] CRC64: 96713869752962B0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEDMRIATLT SGGDCPGLNA VIRGIVRTAS NEFGSTVVGY QDGWEGLLGD RRVQLYDDED 

        70         80         90        100        110        120 
IDRILLRGGT ILGTGRLHPD KFKAGIDQIK ANLEDAGIDA LIPIGGEGTL KGAKWLSDNG 

       130        140        150        160        170        180 
IPVVGVPKTI DNDVNGTDFT FGFDTAVAVA TDAVDRLHTT AESHNRVMIV EVMGRHVGWI 

       190        200        210        220        230        240 
ALHAGMAGGA HYTVIPEVPF DIAEICKAME RRFQMGEKYG IIVVAEGALP REGTMELREG 

       250        260        270        280        290        300 
HIDQFGHKTF TGIGQQIADE IHVRLGHDVR TTVLGHIQRG GTPTAFDRVL ATRYGVRAAR 

       310        320        330        340 
ACHEGSFDKV VALKGESIEM ITFEEAVGTL KEVPFERWVT AQAMFG 

Q8NR14 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!