ID K6PF_MYCBO Reviewed; 343 AA.
AC P65691; O53257;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 61.
DE RecName: Full=6-phosphofructokinase;
DE Short=Phosphofructokinase;
DE EC=2.7.1.11;
DE AltName: Full=Phosphohexokinase;
GN Name=pfkA; OrderedLocusNames=Mb3035c;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
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; BX248344; CAD96722.1; -; Genomic_DNA.
DR RefSeq; NP_856680.1; NC_002945.3.
DR ProteinModelPortal; P65691; -.
DR SMR; P65691; 2-335.
DR STRING; 233413.Mb3035c; -.
DR EnsemblBacteria; CAD96722; CAD96722; Mb3035c.
DR GeneID; 1093228; -.
DR KEGG; mbo:Mb3035c; -.
DR PATRIC; 18008410; VBIMycBov88188_3335.
DR eggNOG; COG0205; -.
DR HOGENOM; HOG000248869; -.
DR KO; K00850; -.
DR OMA; YEVIGYK; -.
DR ProtClustDB; PRK03202; -.
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 Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1 343 6-phosphofructokinase.
FT /FTId=PRO_0000111969.
FT NP_BIND 20 24 ATP (By similarity).
FT NP_BIND 155 159 ATP (By similarity).
FT NP_BIND 172 188 ATP (By similarity).
FT ACT_SITE 128 128 Proton acceptor (By similarity).
FT METAL 186 186 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 163 163 Substrate (By similarity).
FT BINDING 267 267 Substrate (By similarity).
FT BINDING 273 273 Substrate (By similarity).
FT BINDING 276 276 Substrate (By similarity).
SQ SEQUENCE 343 AA; 36880 MW; 826E5FF16A6ECABA CRC64;
MRIGVLTGGG DCPGLNAVIR AVVRTCHARY GSSVVGFQNG FRGLLENRRV QLHNDDRNDR
LLAKGGTMLG TARVHPDKLR AGLPQIMQTL DDNGIDVLIP IGGEGTLTAA SWLSEENVPV
VGVPKTIDND IDCTDVTFGH DTALTVATEA IDRLHSTAES HERVMLVEVM GRHAGWIALN
AGLASGAHMT LIPEQPFDIE EVCRLVKGRF QRGDSHFICV VAEGAKPAPG TIMLREGGLD
EFGHERFTGV AAQLAVEVEK RINKDVRVTV LGHIQRGGTP TAYDRVLATR FGVNAADAAH
AGEYGQMVTL RGQDIGRVPL ADAVRKLKLV PQSRYDDAAA FFG
//
