ID A7RER9_NEMVE Unreviewed; 556 AA.
AC A7RER9;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 97.
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=NEMVEDRAFT_v1g157664 {ECO:0000313|EMBL:EDO49963.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO49963.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO49963.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; DS469507; EDO49963.1; -; Genomic_DNA.
DR RefSeq; XP_001642026.1; XM_001641976.1.
DR AlphaFoldDB; A7RER9; -.
DR STRING; 45351.A7RER9; -.
DR EnsemblMetazoa; EDO49963; EDO49963; NEMVEDRAFT_v1g157664.
DR GeneID; 5522266; -.
DR KEGG; nve:5522266; -.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; A7RER9; -.
DR OMA; RVHHIGE; -.
DR OrthoDB; 312683at2759; -.
DR PhylomeDB; A7RER9; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00288; Pyruvate_Kinase; 1.
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:SF3; AT14039P-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 46..370
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 407..523
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 534..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 61584 MW; 9EECEF0F2D165ED0 CRC64;
MSAKGAREEY LHDVLNRHKQ WISSRARSNL EFRSELDIDK HPLTIRNSGV VCTIGPASRS
VEIVAQLIEN GMNIARLNFS HGTHEYHRET IMNIRRAALL EWPHAVGIAL DTKGPEIRTG
LLKAGEIKLE KGQKLKVSTD KAMYDQGHTE CIFVDYENIV KVVQIGGTVY VDDGLISLKV
LEKGDNFLIT EVLNDALLGS KKGVNLPNCA VDLPAVSEQD KKDIAFAVEM EVDMIFASFI
RKPEDIAEIR KLLEKHAKNI KIVAKIENHE GVRRFNEILE VADGIMVARG DLGIEIPAEK
VFLAQKMMIA RCNMKGVPVI CATQMLESMV QNPRPTRAET SDVANAILDG ADCVMLSGET
AKGLYPVQAV AMMHRISREA EAAIFHKQSF DELRHNLEGY ADTHISTAIA AVAASFTAGA
DAIICLTHTG RTAAVVARFR PRCPIVVVTR DPRVARQMHL WRGCFPIVYD QEPLDNVLEE
HDQRLDFALG MGKKMGFLTI GSTFVFVSGW KSGAAHTNTL RILTLTQEKI HIARSLSESA
DPTGKTHNEE QEDIDG
//
