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Database: UniProt
Entry: A0A371HJ76_MUCPR
LinkDB: A0A371HJ76_MUCPR
Original site: A0A371HJ76_MUCPR 
ID   A0A371HJ76_MUCPR        Unreviewed;       527 AA.
AC   A0A371HJ76;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=CR513_13636 {ECO:0000313|EMBL:RDY02856.1};
OS   Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX   NCBI_TaxID=157652 {ECO:0000313|EMBL:RDY02856.1, ECO:0000313|Proteomes:UP000257109};
RN   [1] {ECO:0000313|EMBL:RDY02856.1, ECO:0000313|Proteomes:UP000257109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC   TISSUE=Seed {ECO:0000313|EMBL:RDY02856.1};
RA   Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT   "Draft genome of Mucuna pruriens seed.";
RL   Submitted (MAY-2018) 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:RDY02856.1}.
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DR   EMBL; QJKJ01002447; RDY02856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371HJ76; -.
DR   STRING; 157652.A0A371HJ76; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000257109; 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; 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; PYRUVATE KINASE; 1.
DR   PANTHER; PTHR11817:SF4; 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.
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:RDY02856.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          30..360
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          395..514
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   527 AA;  57700 MW;  065FC2B6B11DED68 CRC64;
     MPSGHLLLEE PIRMVSILEP SKPSVFPAMT KIVGTLGPQS RDVHTICSCL FSGMSVARFD
     FSWHDPEYHQ ETLENLKVAI KNTKTLCAVM LDTVGAEMQV VNKSEKAISL KADGQVVLTP
     DHGQEATSEI LPINFNGLAK AMKTGDTIFI GQYLFTGSET TSVWLEVSEV KGEDVVCLIK
     NSATLAGPLF TLHASQIHID LPTLTEKDKE VISTWGVKNK IDFLSLSYTR HAEDVRQARE
     FLSKLGDLSQ TQIFAKIENV EGLTHFDEIL QEADGIILSR GNLGIDLPPE KVFLFQKSAL
     HKCNMAGKPA VLTRVVDSMT DNLRPTRAEA TDVANAVLDG SDAILLGAET LRGLYPCQTI
     YTVGKICSEA EKVFNQGLYF KRTVKYVGEP MTHLESIASS AVRAAIKVKA TIIICFTSSG
     RAARLIAKYR PTMPVLSVVI PRLTTNQLKW SFTGAFEARQ SLIVRGLFPL LADPRHPAES
     TSATNESILK VALDHGKSLG IIKSHDRVVV CQKLGDASVI KIIELED
//
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