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 Q8A624

[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 K6PF2_BACTN
Primary accession number Q8A624
Secondary accession numbers None
Integrated into Swiss-Prot on June 16, 2003
Sequence was last modified on June 16, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
Name and origin of the protein
Protein name 6-phosphofructokinase 2
Synonyms EC 2.7.1.11
Phosphofructokinase 2
Phosphohexokinase 2
Gene name
Name: pfkA2
OrderedLocusNames: BT_2062
From
Bacteroides thetaiotaomicron [TaxID: 818] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(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
AE015928; AAO77169.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_810975.1; -.
3D structure databases
HSSP P00512; 3PFK. [HSSP ENTRY / PDB]
ModBase Q8A624.
Enzyme and pathway databases
BioCyc BTHE226186:BT_2062-MON; -.
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.
IPR012828; PFKA_ATP.
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 TIGR02482; PFKA_ATP; 1.
PROSITE PS00433; PHOSPHOFRUCTOKINASE; 1.
Genome annotation databases
GeneID 1071883; -.
GenomeReviews AE015928_GR; BT_2062.
KEGG bth:BT_2062; -.
NMPDR fig|226186.1.peg.2062; -.
Phylogenomic databases
HOGENOM Q8A624; -.
Genome annotation databases
CMR Q8A624; BT_2062.
Other
ProtoNet Q8A624.
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   326  326     6-phosphofructokinase 2. PRO_0000111938
NP_BIND   24    28  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). 
METAL   191   191        Magnesium (By similarity). 
BINDING   166   166        Substrate (By similarity). 
BINDING   250   250        Substrate (By similarity). 
BINDING   256   256        Substrate (By similarity). 
BINDING   259   259        Substrate (By similarity). 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 35257 Da [This is the MW of the unprocessed precursor] CRC64: EEF46D4915E7A082 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGTVKCIGIL TSGGDAPGMN AAIRAVTRAA IYNGLQVKGI YRGYKGLVTG EIKEFKSQNV 

        70         80         90        100        110        120 
SNIIQLGGTI LKTARCKEFT TPEGRQLAYD NMKREGIDAL VIIGGDGSLT GARIFAQEFD 

       130        140        150        160        170        180 
VPCIGLPGTI DNDLYGTDTT IGYDTALNTI LDAVDKIRDT ATSHERLFFV EVMGRDAGFL 

       190        200        210        220        230        240 
ALNGAIASGA EAAIIPEFST EVDQLEEFIK NGFRKSKNSS IVLVAESELT GGAMHYAERV 

       250        260        270        280        290        300 
KNEYPQYDVR VTILGHLQRG GSPTAHDRIL ASRLGAAAID AIMEDQRNVM IGIEHDEIVY 

       310        320 
VPFSKAIKND KPVKRDLVNV LKELSI
Q8A624 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 ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!