ID A0A087HIX1_ARAAL Unreviewed; 617 AA. AC A0A087HIX1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_03185}; DE Short=PFP {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185}; GN Name=PFP-ALPHA {ECO:0000256|HAMAP-Rule:MF_03185}; GN ORFNames=AALP_AA2G207700 {ECO:0000313|EMBL:KFK42073.1}; OS Arabis alpina (Alpine rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Arabideae; OC Arabis. OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42073.1, ECO:0000313|Proteomes:UP000029120}; RN [1] {ECO:0000313|EMBL:KFK42073.1, ECO:0000313|Proteomes:UP000029120} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120}; RC TISSUE=Leaf {ECO:0000313|EMBL:KFK42073.1}; RA Willing E.-M.; RT "The reference genome of Arabis alpina."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6- CC phosphate 1-phosphotransferase. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- ENZYME REGULATION: Allosterically activated by fructose 2,6- CC bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta CC (catalytic) chains. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. PPi-dependent PFK group II subfamily. Clade "Long" sub- CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM002870; KFK42073.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000029120; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR011183; PfpB_PPi_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR TIGRFAMs; TIGR02477; PFKA_PPi; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03185}; KW Complete proteome {ECO:0000313|Proteomes:UP000029120}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03185}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03185}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185}; KW Reference proteome {ECO:0000313|Proteomes:UP000029120}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03185}. FT DOMAIN 88 449 PFK. {ECO:0000259|Pfam:PF00365}. SQ SEQUENCE 617 AA; 67435 MW; 70EB47E66A9999ED CRC64; MDSDFGIPRE LSPLQQLRSQ YQPLLPPCLQ GTTVRVELGD GTTGAKAGDA HIIARAFPHT LGQPLAHFLR ANAKVVDAQI ITEHPAIRVG IVFSGRQAPG GHNVIWGLYE ALKVHNAKNT LLGFLGGSEG LFAQKTVEIT DDVLQTYKNQ GGFDLLGRTK DQIRTTEQVN AALKACTDLK LDGLVIIGGV TSNTDAGHLA EFFAETKCPT KVVGVPVTIN GDLKNQFVEA NVGFDTICKV NSQLISNVCT DALSAEKYYY FIRLMGRKHS HVALECTLQS HPNMVILGEE VAASKLTIFD IAKQICDAVQ ARAEQDKNHG VILIPEGLVE SIPELFALLK EIHGLLKEGV DADKISTKLS PWSFALFEFL PPFMKKQLLL HPESDDSAQL SQIETEKLLA YLVETEMNKR MKVGTYKGKK FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHILAAGL NGYMATVTNL KSPVNKWKCG AAPITAMMTV KRWSQNAGST SIGRPVIHPA TVDLKGKAYD LLRQNAQKFL MEDMYRNPGP LQYDGPGADA KAVSLCVEDQ DYMGRIKKLQ EYLDQVRTIV KPGCSQDVLK AALSVMASVT DVLSTISSSS TSGQQFA //