ID D6RMA9_COPC7 Unreviewed; 839 AA.
AC D6RMA9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=CC1G_14425 {ECO:0000313|EMBL:EFI27934.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EFI27934.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EFI27934.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EFI27934.1}.
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DR EMBL; AACS02000004; EFI27934.1; -; Genomic_DNA.
DR RefSeq; XP_002911428.1; XM_002911382.1.
DR AlphaFoldDB; D6RMA9; -.
DR STRING; 240176.D6RMA9; -.
DR GeneID; 9379887; -.
DR KEGG; cci:CC1G_14425; -.
DR VEuPathDB; FungiDB:CC1G_14425; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; D6RMA9; -.
DR OMA; EWQDQMC; -.
DR OrthoDB; 374214at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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; 3.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 2.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 3.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000533}.
FT DOMAIN 2..54
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 115..365
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 461..749
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 91170 MW; 3801A341B1DC7BE5 CRC64;
MRIAILTSGG DSAGMNAVVR AVVKTGILKG CEMYVVREGY EGLVRGNNEH AEQQAKNVAA
ETEAEVEREV KATYEAPHGQ PAVNLLHNLR FGDGELLKDG TCEFVGGRTL KGRYIVRVGW
DDVRGWFSQG GTLIGTARSM TFKTVEGREA AAHNLIREGI DALVVCGGDG SLTGADVFRR
EWPSLIAALK EKGLVSEDQA KKHAHLKIVG LVGSIDNDMS MTDLTIGAPT ALQRICEAID
NINSTAYSHS RAFVIEVMGR DCGWLAALAG VAGGADFIFI PERPPTAMPW EDDMCAQIHR
HREVGKRTTI VLVAEGAHDS DLNPIKPEYV KDILTERLGL DTRVTTLGHT QRGGRPCALD
RILATHPPGS RSNRCLVAIH GRHPFIHDRF AREQDRASTS NGGGRTGKPF PDPPTRAVKA
KDYEKALELR GSEFKEILDG FFATSMLAEE SAKLPKEKRM RIGIIHMGAP AGGMNAATRA
AVRYCIRQGH TALAIHNGFR GLLDGNIDQL SWLGVDAWTP RGGSELGTNR ALPSTDIGGV
AAKFQEYNLQ GLLIIGGFEG FTALLQLEEG RKHYPAFHIP MVHLPATISN NVPVTEYSIG
SDTSLNALVD ACDAIKQSAS ASRDRVFVVE TQGGKCGYIA TMGALAVGAS LVYTPEEGIT
LDMLRRDVRF LKTRYSLDPP GKSEGRLVIR NEASSSVYTT TMITKMLQEE GGSLFDARSA
SLGHTLQGGI PSPIDRVRAA RLSLKCMVFL EQHHNRLLGQ KHRQAPPESA SVITVQTSSV
KMVPVQEMVK HADMVNRRGK TAWWFGVKHL EEQLAGKPQF LGLHKSPEYQ ASVSGYAKM
//
