ID A0A4S8MYR9_DENBC Unreviewed; 532 AA.
AC A0A4S8MYR9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=K435DRAFT_709763 {ECO:0000313|EMBL:THV07674.1};
OS Dendrothele bispora (strain CBS 962.96).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricales incertae sedis; Dendrothele.
OX NCBI_TaxID=1314807 {ECO:0000313|EMBL:THV07674.1, ECO:0000313|Proteomes:UP000297245};
RN [1] {ECO:0000313|EMBL:THV07674.1, ECO:0000313|Proteomes:UP000297245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 962.96 {ECO:0000313|EMBL:THV07674.1,
RC ECO:0000313|Proteomes:UP000297245};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|ARBA:ARBA00001174,
CC ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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; ML179037; THV07674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S8MYR9; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000297245; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:THV07674.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000297245};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 33..359
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 394..515
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 532 AA; 58253 MW; 6491A4300D56ECB7 CRC64;
MFATDGIHSQ LEWSSTLSTI KAPVPTEETK FHRKTSIIAT IGPKVNTAEK LAELRRAGVN
VVRMNFSHGS YEYHQSVIDN TRKMVAQDPE GRPVAIALDT KGPEIRTGLM RDGMDIAVQA
GHEFTVSTDP KFQETCDDKV LWMDYANLPK VTAPGKLIYV DDGILSLLVL SIDGNNIRVR
TLNNGTLSSR KGVNLPKTDV DLPALSEKDK KDLQFGVKNN VDMIFASFIR RAQDVKDIKT
VLGPDGASIK IIVKIENEQG VANFDEILKE ADGVMVARGD LGIEIPASQV FLAQKMMIAK
CNIVGKPVIV ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGSYPVQSVL
MMAETCLLAE YAICYPPLYD ELRAVQPRPT ETTETVAIAA VAAASEQEAS AILVLSTSGN
TARLISKYRP RVPIIAVTRN EQTARQIHLH RGCYPFWYPE PRGIQSHQWQ TDVDNRIRFG
LRSALKLNII SPGSTVIAVQ GWKGGLGHTN TLRILSVPTD PADFELQELG SV
//
