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Database: UniProt/TrEMBL
Entry: Q0AXS5_SYNWW
LinkDB: Q0AXS5_SYNWW
Original site: Q0AXS5_SYNWW 
ID   Q0AXS5_SYNWW            Unreviewed;       365 AA.
AC   Q0AXS5;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   19-FEB-2014, entry version 57.
DE   RecName: Full=6-phosphofructokinase;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
GN   Name=pfkA; OrderedLocusNames=Swol_1170;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family.
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DR   EMBL; CP000448; ABI68479.1; -; Genomic_DNA.
DR   RefSeq; YP_753850.1; NC_008346.1.
DR   ProteinModelPortal; Q0AXS5; -.
DR   STRING; 335541.Swol_1170; -.
DR   EnsemblBacteria; ABI68479; ABI68479; Swol_1170.
DR   GeneID; 4283745; -.
DR   KEGG; swo:Swol_1170; -.
DR   PATRIC; 23857165; VBISynWol51738_1242.
DR   eggNOG; COG0205; -.
DR   HOGENOM; HOG000248869; -.
DR   KO; K00850; -.
DR   OMA; IPEIPYK; -.
DR   OrthoDB; EOG644ZRM; -.
DR   BioCyc; SWOL335541:GHL1-1203-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IEA:GOC.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00339; Phosphofructokinase; 1.
DR   InterPro; IPR012003; ATP_PFK_prok.
DR   InterPro; IPR012829; PFK.
DR   InterPro; IPR022953; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT   NP_BIND      24     28       ATP (By similarity).
FT   NP_BIND     168    172       ATP (By similarity).
FT   NP_BIND     185    201       ATP (By similarity).
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
FT   METAL       199    199       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       201    201       Magnesium (By similarity).
FT   BINDING     176    176       Substrate (By similarity).
FT   BINDING     281    281       Substrate (By similarity).
FT   BINDING     287    287       Substrate (By similarity).
FT   BINDING     290    290       Substrate (By similarity).
SQ   SEQUENCE   365 AA;  39123 MW;  37E1B3E18CAD9047 CRC64;
     MKEIRHIGIL TGGGDCPGLN AVIRAISKTA INYGVEVIGF IDGFKGLVEN RYIQLDLRAV
     SGISHTGGTI LGTSNRDNPF QFFTISEGTP QHSDESDRAV ANMEHLGLDG LVVIGGDGSL
     NIADRFAEKG VPIVGVPKTI DNDLSATDVT FGFNTAVNTA SEALDRLHTT AESHHRVMVL
     EVMGRYAGWI ALHAGISGGA DVILIPEIPY NMDAVISKIT QRYRQGKNFS IIVVAEGAIP
     EDGEMVIRNL VATSHDPIRL GGIGQKVAED IGNRLQNIEV RVTVLGHLQR GGSPIPYDRI
     LSTRYGVAAV DAFMAGQFGT MVSLRGDMIA AVPIKEAIKE IRRVKPESDL VRAARAVGIS
     FGDKY
//
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