ID A0A5A7UTK2_CUCME Unreviewed; 589 AA.
AC A0A5A7UTK2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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=E5676_scaffold216G001510 {ECO:0000313|EMBL:TYK30163.1},
GN E6C27_scaffold280G003470 {ECO:0000313|EMBL:KAA0057466.1};
OS Cucumis melo var. makuwa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=1194695 {ECO:0000313|EMBL:KAA0057466.1, ECO:0000313|Proteomes:UP000321393};
RN [1] {ECO:0000313|EMBL:KAA0057466.1, ECO:0000313|Proteomes:UP000321947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chang Bougi {ECO:0000313|Proteomes:UP000321947};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAA0057466.1};
RA Kwon S.-Y.;
RT "Draft genome sequences of two oriental melons (Cucumis melo L. var
RT makuwa).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
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:KAA0057466.1}.
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DR EMBL; SSTE01007195; KAA0057466.1; -; Genomic_DNA.
DR EMBL; SSTD01000775; TYK30163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A7UTK2; -.
DR STRING; 1194695.A0A5A7UTK2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000321393; Unassembled WGS sequence.
DR Proteomes; UP000321947; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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:SF14; PLASTIDIAL PYRUVATE KINASE 1, CHLOROPLASTIC; 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:KAA0057466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000321393};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 110..441
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 480..580
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 589 AA; 64500 MW; 846B478F42B231FE CRC64;
MTQSLQLFTS SAISLPKHSI SKPFSSTAAF RFPFSFSKSS IRASSSDLNP LSSSSTSQVL
VSENGSSSGG GVVSSSATRE FVSVASDSTS IDVDAVTEAE LKENGFRSTR RTKLVCTIGP
ASCGFEQLEA LAVGGMNVAR INMCHGTRDW HRTVIERVRR LNDEKGYAVA IMMDTEGSEI
HMGDLGGASS AKAEDGEIWT FSVRAFDSTL PERTINVNYE GFAEDVRVGD DLLVDGGMVR
FEVIEKIGPD VKCLCTDPGL LLPRANLTFW RDGHLVRERN AMLPTISSKD WLDIDFGIAE
GVDFLAISFV KSAEVIKHLK SYIAARSRGS DISIIAKIES LDSLKNLEEI ILASDGAMVA
RGDLGAQIPL EQVPSVQQKV VQLCRQLNKP VIVASQLLES MIEYPTPTRA EVADVSEAVR
QRSDALMLSG ESAMGQYPDK ALAVLRSVSL RIEKWWRDEK RHEPMELPEV GSSFSDSILE
EICNSAAKMA NNLEVDAIFV YTTSGHMASL LSRCRPDCPI FAFTSTTSVR RRLNLQWGLI
PFRLSFSDDM ENNLNKTFLL LKARNLIKSG DLVIAVSDML QSIQVMNVP
//
