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Database: UniProt
Entry: A0A444F4Y1_ENSVE
LinkDB: A0A444F4Y1_ENSVE
Original site: A0A444F4Y1_ENSVE 
ID   A0A444F4Y1_ENSVE        Unreviewed;       422 AA.
AC   A0A444F4Y1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=GW17_00018357 {ECO:0000313|EMBL:RWW17701.1};
OS   Ensete ventricosum (Abyssinian banana) (Musa ensete).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Ensete.
OX   NCBI_TaxID=4639 {ECO:0000313|EMBL:RWW17701.1, ECO:0000313|Proteomes:UP000288739};
RN   [1] {ECO:0000313|EMBL:RWW17701.1, ECO:0000313|Proteomes:UP000288739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Bedadit {ECO:0000313|Proteomes:UP000288739};
RC   TISSUE=Leaf {ECO:0000313|EMBL:RWW17701.1};
RX   PubMed=29896517; DOI=10.1016/j.dib.2018.03.026;
RA   Yemataw Z., Muzemil S., Ambachew D., Tripathi L., Tesfaye K., Chala A.,
RA   Farbos A., O'Neill P., Moore K., Grant M., Studholme D.J.;
RT   "Genome sequence data from 17 accessions of Ensete ventricosum, a staple
RT   food crop for millions in Ethiopia.";
RL   Data Brief 18:285-293(2018).
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   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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:RWW17701.1}.
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DR   EMBL; JTFG03001785; RWW17701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444F4Y1; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000288739; 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   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
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   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   PANTHER; PTHR11817:SF5; PYRUVATE KINASE-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288739};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          89..233
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          294..373
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  45605 MW;  B41002358FA754A3 CRC64;
     MAEDEDRVHS GAGFEVRGDD RAAPKSGHER GPLQLLPRLR RVPSGDAAQP EGRHGGNRHP
     MRRHARHQGP SSFTITSFFT SCCCLKRPDG KPIQLKKGQE LIVSTDYGIR GDENMISMSY
     NKLADDLKPD GVILCADGTI MLTVLACDSS SGLVRCRCEN SALLGERKNV NLPGVVVDLP
     TLTEKDKEDI LRWGKGSDVV EARKLLGDHA KSIMLMSKVE NQEGVANFDD ILANAVLDGN
     DCVMLSGETA AGVHPDLAVE TTTKICLEAE SYLDYGAVFK QLMAAAPATT SPLESLASSA
     VLTARSARAA LIIVLTRGGT TAKLVAKYRP QVPILSVVVP EITTDSFDWF CSDEAPARHG
     LIVRGLIPLL SGGMTKTRHS ETRKKRSSSP CSTRKLRASA NRAMLTKTTH CTARELLRSS
     SF
//
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