ID A0A5D6VZA8_9FIRM Unreviewed; 475 AA.
AC A0A5D6VZA8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=pyk {ECO:0000313|EMBL:TYZ20956.1};
GN ORFNames=FZ040_11115 {ECO:0000313|EMBL:TYZ20956.1};
OS Selenomonas sp. mPRGC5.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=2593411 {ECO:0000313|EMBL:TYZ20956.1, ECO:0000313|Proteomes:UP000323646};
RN [1] {ECO:0000313|EMBL:TYZ20956.1, ECO:0000313|Proteomes:UP000323646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mPRGC5 {ECO:0000313|Proteomes:UP000323646};
RA Poothong S., Nuengjamnong C., Tanasupawat S.;
RT "Selenomonas sp. mPRGC5 and Selenomonas sp. mPRGC8 isolated from ruminal
RT fluid of dairy goat (Capra hircus).";
RL Submitted (AUG-2019) 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|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:TYZ20956.1}.
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DR EMBL; VTOY01000011; TYZ20956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D6VZA8; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000323646; 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, ECO:0000313|EMBL:TYZ20956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000323646};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:TYZ20956.1}.
FT DOMAIN 3..323
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 357..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 475 AA; 52021 MW; 65FF33F949689017 CRC64;
MLKKTKIICT QGPSTEKPGV IDALIENGMN LARFNFSHGD HEEHLNRINM VREAAKKAGK
VISLVLDTKG PEMRLGEFKD GKVMLEKGNK FTLTYEDIPG DETHVSVNHK GLYTEVKPGD
TLLLSDGLVA LKVDEIKGKD IVTTIQNSGK MSTRKRVAAP GVSLGLPPIS EQDEKDIIFG
CEQDMDFVAA SFIQRPADVL AIRKLIEEHN GHMEIIPKIE NLEGVKNFDE ILAVSDGIMV
ARGDLGVEVP AEDVPLIQKE IIRKCNKAGK PVIVATQMLD SMERNPRPTR AEVSDVGNAI
LDGTDAIMLS GETASGDYPV EAVATMNRIA CRIESALEYK DLFMERGFEH LQSRTRAVAH
ATVQMAYELD APAIITPTES GYTTKVVSKY RPKAAIVAYT PSEKVVRQLN LRWGVYPILG
TEWNDVDEML SNATSAAVKN EYVKRGDTTI VTSGIKVDSS AAVGKNTNSI RVYAI
//
