ID A0A267GKQ7_9PLAT Unreviewed; 623 AA.
AC A0A267GKQ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BOX15_Mlig028607g1 {ECO:0000313|EMBL:PAA86613.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA86613.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA86613.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA86613.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA86613.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- 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:PAA86613.1}.
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DR EMBL; NIVC01000271; PAA86613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GKQ7; -.
DR STRING; 282301.A0A267GKQ7; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000215902; 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: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.
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:UP000215902};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 67..403
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 451..563
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 589..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 68464 MW; A490795626B853F2 CRC64;
MQQDDSSHAF QFGGVQLTLP TPTLSKVSST MPGYYRMNTQ SRIMHSRETQ LTHLCRLDID
NLPIYPRVTS IMCTLGPSCE TPEMIRRMIV RGMNIARINL TLGSYKYCSQ LIKAVRAEEA
KLNSESMDSY MVAVAVDITA PTLRTGQVGG AVNGSFKVSE GEFVTITVDE AYKDDCTAEH
LYIDTAYWRK SFHAINVGDR IDIDDGTVML IAREKASLTG SIRCLVEQGG ILLSSRVVRL
PRMAEYRHAV AEKYKQDLLF AVENQVDIVC CGFAESGLAI TQIRKVLGPF SLNTKVLARI
ESSDGLKNLA DILSVADGVF VDRGELGRNL PIEKVFLAQK SVIAHANAAK KPAVVAAQML
DSMRHKPRAT RAEVSDVANA VLDGADVLAL GVETAKGAFP LETLQVMVQV CQEAESAYYH
GRKFVDLKRI EAVRLAAMGP NDEQIETFTS ATAAVSAAMT NGAAAIIVVT TTGKTAFAVA
SYRPPCPILT VTRQMSVARQ CHLYRGLRPV YFSEEKCDDW SEDMDRRITH TLQFAVRSKF
VKPGERVVIC TGWHAGQTNT VRLVVVPAEE FMSSPLHIVR SSQVFNVSSK QQQPREVAPN
QPNLLPPNQP APAWGENPTV TFD
//
