ID Q1CYM6_MYXXD Unreviewed; 345 AA.
AC Q1CYM6;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 01-MAY-2013, entry version 56.
DE RecName: Full=6-phosphofructokinase;
DE Short=Phosphofructokinase;
DE EC=2.7.1.11;
DE AltName: Full=Phosphohexokinase;
GN Name=pfkA; OrderedLocusNames=MXAN_6373;
OS Myxococcus xanthus (strain DK 1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK 1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF87778.1; -; Genomic_DNA.
DR RefSeq; YP_634497.1; NC_008095.1.
DR ProteinModelPortal; Q1CYM6; -.
DR STRING; 246197.MXAN_6373; -.
DR EnsemblBacteria; ABF87778; ABF87778; MXAN_6373.
DR GeneID; 4101446; -.
DR KEGG; mxa:MXAN_6373; -.
DR PATRIC; 22655241; VBIMyxXan43560_6264.
DR eggNOG; COG0205; -.
DR HOGENOM; HOG000248869; -.
DR KO; K00850; -.
DR OMA; NGTQKTA; -.
DR BioCyc; MXAN246197:GIWU-6322-MONOMER; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA: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:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolysis; IEA: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; Ppfruckinase; 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 20 24 ATP (By similarity).
FT NP_BIND 153 157 ATP (By similarity).
FT NP_BIND 170 186 ATP (By similarity).
FT ACT_SITE 126 126 Proton acceptor (By similarity).
FT METAL 184 184 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 186 186 Magnesium (By similarity).
FT BINDING 161 161 Substrate (By similarity).
FT BINDING 269 269 Substrate (By similarity).
FT BINDING 275 275 Substrate (By similarity).
FT BINDING 278 278 Substrate (By similarity).
SQ SEQUENCE 345 AA; 37044 MW; 8109152D02E586F8 CRC64;
MKVAVLTGGG DCPGLNAVIR AVVRRANAHG FEMMGLRDGW KGLLEDNHFR LTRETTSGIL
HRGGTILGTS RVNPFKVENG LERVKRAIER NGIHAVIAIG GEGTLSAATR MSQEGLRIVG
VPKTIDNDIN ATDFTFGFDT AVAIATEAID RLHSTAESHK RVIVCEVMGR HVGWIATYAG
IAGGADVILV PEIPADLAKV AEHIQRRHAG GRTFSIVVVA EGTRIKLSAD QQEQLVTSGA
LDEAGRPRLG GVGTILAHEI ERRTGFETRV SVLGHIQRGG APTAHDRVLA TRYGVHACDM
VARGEFGKMA ALRGNDIISV DLADATRELK RVPQEFFEVA QVFFG
//
