ID A0A2R5HGW2_9LACT Unreviewed; 501 AA.
AC A0A2R5HGW2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pykF {ECO:0000313|EMBL:GBG97244.1};
GN ORFNames=NtB2_01382 {ECO:0000313|EMBL:GBG97244.1};
OS Lactococcus termiticola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2169526 {ECO:0000313|EMBL:GBG97244.1, ECO:0000313|Proteomes:UP000245021};
RN [1] {ECO:0000313|EMBL:GBG97244.1, ECO:0000313|Proteomes:UP000245021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NtB2 {ECO:0000313|EMBL:GBG97244.1,
RC ECO:0000313|Proteomes:UP000245021};
RA Noda S., Aihara C., Yuki M., Ohkuma M.;
RT "Draft Genome Sequence of Lactococcus sp. Strain NtB2 (JCM 32569), Isolated
RT from the Gut of the Higher Termite Nasutitermes takasagoensis.";
RL Genome Announc. 6:e00445-18(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|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 -!- 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:GBG97244.1}.
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DR EMBL; BFFO01000008; GBG97244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5HGW2; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000245021; 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; 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:SF132; PYRUVATE KINASE 1; 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:GBG97244.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245021};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 3..354
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 386..497
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 501 AA; 54762 MW; CDA00316DC3AB62C CRC64;
MQKRVKIVST LGPAVETRGG KKFGEDGYWS QPLDVETSAQ TIASLIKAGA NVFRFNFSHG
DYDEHAARMA CVRRAEEIAG QKVGFLLDTK GPEIRTELFA NDDIKQESYK TGDTFRIATK
QGEKSTKEVI ALNVAGGLDI FDDVEIGQRI LVDDGKLGLT ITGKDATTRE FLVVAENDEI
IAKQKGVNIP NTKIPFPTLA ERDEADIRFG LQQGLNFIAI SFVRTADDVH AVRRILEETG
NSHVQLFPKI ENQQGIDNID SIIEAADGIM IARGDMGIEV PFEMVPVYQK MIITKCAEAG
KAVITATNML ESMTEHPRAT RSEISDVFNA VIDGTDATML SGESANGKYP LQAVETMAKV
DTNAQTMLQQ YGRLRFRDYD RSSVTEVVAS AVRDATRSMD IALVIALTDS GSTARVISKY
RPNADILAVT FSDKVQRSLM INWGVIPVLR DKPSTTDDMF DIAEEAALES GLVKSGDNVV
IVAGVPVGSG RTNTMRIRTI K
//
