ID A0A180G3S9_PUCT1 Unreviewed; 832 AA.
AC A0A180G3S9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE AltName: Full=Phosphohexokinase {ECO:0000256|PIRNR:PIRNR000533};
GN ORFNames=PTTG_09695 {ECO:0000313|EMBL:OAV87260.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV87260.1};
RN [1] {ECO:0000313|EMBL:OAV87260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV87260.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV87260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV87260.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000432,
CC ECO:0000256|PIRNR:PIRNR000533};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|PIRNR:PIRNR000533}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E"
CC sub-subfamily. {ECO:0000256|PIRNR:PIRNR000533}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV87260.1}.
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DR EMBL; ADAS02000503; OAV87260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180G3S9; -.
DR STRING; 630390.A0A180G3S9; -.
DR VEuPathDB; FungiDB:PTTG_09695; -.
DR OrthoDB; 374214at2759; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.450; -; 3.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 2.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000533};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|PIRNR:PIRNR000533};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000533};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000533};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000533}.
FT DOMAIN 3..364
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 447..736
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 745..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 90477 MW; D6E1EBB55AEB5E5C CRC64;
MTRIAVLTSG GDSAGMNAAV RSVVRTAISN SCEVYVVREG YEGLVRGNEA HAPKPDTLAV
PTSARRPGMP KTSDRPLSTN FISTYFGADA LKDGEADSEL RGQHIVRVGW DDVGPFLSEG
GTLIGTQRSQ SFRLLEGRRK AALNLITHGI NALVVCGGDG SLTGADKLRA EWPEHVNALL
ASNEISAEQA NTYSHLIIVG LVGSIDNDMA LTDVTIGAPT ALHRICESID NISSTASSHS
RAFVVEVMGR NCGWLALMAG MSSGADYVFI PEKPPAYDDW EHELCEALRR HREMGKRKSI
VIVAEGAIDK NLQPIKADYI ATILTERLKL DTRVTTLGHT QRGGKPCAYD RILATLQGIE
AVKAVLELAQ TPGGESPLIG LRENQIIRVP LMKAVQTTQE LAKAIANKDF KHAMSLRDTV
YQTSFDAFAA TTRLDERIKL PESQRMRIGI IHIGAPAGGM NAATRTAVRY CHTRGHTPLA
IFNSWTGLMD GHVEELGWLR VDQWTTRGGS ELGTNRTLPS AENIEEIVGR LKMFRIDGLL
LIGGFEVLKS LKFLDEVKSQ HAALDIPMVH LPATISNNVP LTEWSLGSDT SINVLVEACD
AIRQSASASR SRVFVVETQG GECGYIAMLG ALATGAAVVH TPEHPVGLEQ ITKDVQFLKR
RFEADRKGRS LGRLLIRSDK ASKTYTNEFV MRILNEEGRG LFDARQVSLG HTLQGAIPSP
RDRTRAVGLS IQCVGFLERH SKKKTPAEGC ASEQPPAVMR NTSVPTLDPR GTGDEQMWGT
IVITGSLVRI ANLDEIVANA DFANRRGRNA WWLELKNVVE MMAGKKQDEL GA
//
