ID I1QW56_ORYGL Unreviewed; 569 AA.
AC I1QW56;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
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};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA10G0143900.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA10G0143900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR STRING; 4538.I1QW56; -.
DR EnsemblPlants; ORGLA10G0143900.1; ORGLA10G0143900.1; ORGLA10G0143900.
DR Gramene; ORGLA10G0143900.1; ORGLA10G0143900.1; ORGLA10G0143900.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_2_1; -.
DR OMA; TAYKGHM; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000007306; 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; 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:SF63; PLASTIDIAL PYRUVATE KINASE 3, 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 88..409
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 457..547
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 15..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 61475 MW; BC666F0EB0D43161 CRC64;
MAAAAAEIVG SAAARMAAPA VXPAPPAAAA AAPPQPRRAV AARSLRTSTS DRVAADLALG
SNGSLSAQSI AENTADATSQ VVSANSRRKT KIVCTIGPST NTREMIWKLA ETGMNVARMN
MSHGDHQSHQ KVIDLVKEYN AKNTDGNVIA IMLDTKGPEV RSGDVPEPIM LEEGQEFNFT
IKRGVSTKDT VSVNYDDFIN DVEVGDILLV DGGMMSLAVK SKTADTVKCE VVDGGELKSR
RHLNVRGKSA TLPSITEKDW EDIKFGVENG VDFYAVSFVK DAKVIHELKD YLKSANADIH
VIPKIESADS IPNLQSIIAA SDGAMVARGD LGAELPIEEV PLLQEEIVRT CRSMQKPVIV
ATNMLESMID HPTPTRAEVS DIAIAVREGS DAIMLSGETA HGKFPLKAVK VMHTVAQRTE
SSLYNPTTSP SLVAHPQALL NEEFSQSQLS KMFGSHATMM ANTLCTPIIV FTRTGSMAVL
LSHYRPSSTI FAFTNEERVK QRLALYQGVV PIYMKFSDDA EETFSRAISS LLSAQFVKEG
DYVTLVQSGV KSIWREESTH HIQVRKVQG
//