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Probable ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase)

 A0A1R4AAN6_BABMR        Unreviewed;      1311 AA.
A0A1R4AAN6;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
25-OCT-2017, entry version 5.
RecName: Full=Probable ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185};
Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185};
EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03185};
AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03185};
ORFNames=BMR1_02g02830 {ECO:0000313|EMBL:SJK86047.1};
Babesia microti (strain RI).
Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
Babesiidae; Babesia.
NCBI_TaxID=1133968 {ECO:0000313|EMBL:SJK86047.1, ECO:0000313|Proteomes:UP000002899};
[1] {ECO:0000313|EMBL:SJK86047.1, ECO:0000313|Proteomes:UP000002899}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RI {ECO:0000313|EMBL:SJK86047.1,
ECO:0000313|Proteomes:UP000002899};
PubMed=22833609; DOI=10.1093/nar/gks700;
Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
Ben Mamoun C.;
"Sequencing of the smallest Apicomplexan genome from the human
pathogen Babesia microti.";
Nucleic Acids Res. 40:9102-9114(2012).
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
to fructose 1,6-bisphosphate by ATP, the first committing step of
glycolysis. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03185};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta
(catalytic) chains. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
-----------------------------------------------------------------------
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EMBL; FO082872; SJK86047.1; -; Genomic_DNA.
UniPathway; UPA00109; UER00182.
Proteomes; UP000002899; Chromosome II.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR011183; PfpB_PPi_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 2.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 2.
TIGRFAMs; TIGR02477; PFKA_PPi; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Complete proteome {ECO:0000313|Proteomes:UP000002899};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
Kinase {ECO:0000256|HAMAP-Rule:MF_03185, ECO:0000313|EMBL:SJK86047.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03185};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Reference proteome {ECO:0000313|Proteomes:UP000002899};
Transferase {ECO:0000256|HAMAP-Rule:MF_03185,
ECO:0000313|EMBL:SJK86047.1}.
DOMAIN 164 430 PFK. {ECO:0000259|Pfam:PF00365}.
DOMAIN 778 1014 PFK. {ECO:0000259|Pfam:PF00365}.
NP_BIND 236 237 ATP. {ECO:0000256|HAMAP-Rule:MF_03185}.
NP_BIND 265 268 ATP. {ECO:0000256|HAMAP-Rule:MF_03185}.
REGION 294 296 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 341 343 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 505 508 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
ACT_SITE 296 296 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03185}.
METAL 266 266 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03185}.
BINDING 172 172 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03185}.
BINDING 402 402 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03185}.
SITE 267 267 Important for substrate specificity;
cannot use PPi as phosphoryl donor.
{ECO:0000256|HAMAP-Rule:MF_03185}.
SEQUENCE 1311 AA; 147112 MW; 9F6318A0CD6931DB CRC64;
MASKEEKKPK GLRRVMSVYS RDNQHWLNSV DENKYENYDR SSNLMVDTNM LRRKETLLLS
TEPATILPGV KAICKGDLGL KLSDEWLYRN SSTMQINRRN VDLDLPPLLK GKCHVLKEYD
STGECENPDE LKEIGKVLSN IIDKKMVLVE PFAVDIPGEM RRIKIGLILS GGPAPGGHCV
ISGAFDYLKI RNPDSKLIGF IGGIDGFLNN KYEDISSEKI DNYRNMGGFD MLWSGRGRIK
NDKDLETAAK IATDLELDGL IIIGGDGSNS NAALLANYFE KLPRKICVVG VPKTIDGDVK
SENIEQSFGF DTASRTYSEL IGNLCVDATS TRYTWHFVRV MGRSASHLAL ECAMQTHPNI
LLVGEEIQEN GTSLEEIVHQ ITDLMIQRMK LGKNFGVILI SEGLIEFIPE VKILIQELNE
IVNRGQEFDV NLLNKSRKTW EFLPYMIQEQ LLLDREASGY IMVAKIATER LLLMLVESYI
ASEKTDDLKR LNSLKLQFMP HYFGYEGRCA VPSDFDATYC YSLGYNASLL ISHDRNGYMS
VIRNLAKHYE EWVPMGLPFV SIMHMVDAPA GSDLPKFPAI KRVLVDLNSK MFKAISKARI
TWALSENYRS PGPLQLKLSN LNATCLEKFS DVPNSIKQTT SLTFDSSSLS NKLVHVSDNL
DYMSERKDDV NELISQQRCF SLLNDLDLVC KESTNGTCYS PLQNMRLNYK PNIPPLCKNP
NLTMTRNISN GNTIPTDTYT YRQILLNYPH LTSKTSFEIY NVSAIDTPNN SLPKASKVGI
VCLSKQYPGI MNVIWGVRER LKNCELYAFQ GTAGLINGVY SIIKDEDLKL FRNQGGLGII
YRSRFKSIYP LSDRIAAANT CIKLGLHSLV IMGDSGAISQ ATLFAEYLLS NNIDINIIGV
PVTGSNCLAS FGCDNNPIEA CVGFDTNAKL YAGLVGNVLT DAASIPKYWH FVKILGRLPS
LEVLEVALQT HPNVVIIAEE YGAANKTLFD VVRDIADAVC QRAEIGKNFG TVLIPDHLIF
HLPSMKTLID ELRSLYEKID PGDNLVNHIS KLSSWNKALF ESFPEYIRKV LYTFDPSEIL
LENMEIEILL ANMVKEELNL RKKKGLYKGN YLSVTHYFGY QGRCSLPTNF DSNLGFAYGH
IAGVAVESNV TGVCVGIQGL CTQKVEQWEM FAVPFVRLLR ISPDRPEIFS LNDHPRKGEL
PLVLCSMVNL SGKSFRALKE ARGRWVYEDL FCNPGPIQYG EYKVSHNLLL QLEHAEYWNM
LALATKLTDK LKKTYRFGVS EDFLRHVLAS LSSLLLVANN PGKLISILDD I


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