ID D7AQ85_THEM3 Unreviewed; 583 AA.
AC D7AQ85;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=Tmath_1619 {ECO:0000313|EMBL:ADH61326.1};
OS Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS 53645 / CIP 108742 / A3).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH61326.1, ECO:0000313|Proteomes:UP000002064};
RN [1] {ECO:0000313|EMBL:ADH61326.1, ECO:0000313|Proteomes:UP000002064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11426 / CIP 108742 / A3
RC {ECO:0000313|Proteomes:UP000002064};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT mathranii str. A3.";
RL Submitted (MAY-2010) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00006237}.
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DR EMBL; CP002032; ADH61326.1; -; Genomic_DNA.
DR RefSeq; WP_013150582.1; NC_014209.1.
DR AlphaFoldDB; D7AQ85; -.
DR STRING; 583358.Tmath_1619; -.
DR KEGG; tmt:Tmath_1619; -.
DR HOGENOM; CLU_015439_0_2_9; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002064; Chromosome.
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; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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; PF00391; PEP-utilizers; 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; SSF52009; Phosphohistidine 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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:ADH61326.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 501..573
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 583 AA; 62885 MW; 3303AB6434D7FE33 CRC64;
MRRTKIVCTI GPASEDYNIL RKLIEKGMNV ARLNFSHGDF AEHGARIDNI KKIRQELGLP
VAILLDTKGP EIRTGKFKNG EVQLKEGQTF VITTRDVLGD ETICSVSYKG LPQDVERGSR
ILVDDGLISL KVTDVKGEDI VCIVENSGPV KDHKGVNVPG VKLNLPALTQ KDIDDIEFGI
QKGIDMIAAS FVRKASDVLA IRRLLEENKA EHILIIAKIE NREGVENIDE IIKVSDGIMV
ARGDLGVEIP LEEIPIVQKM IIQKCNKAGK PVITATQMLD SMMRNPRPTR AEVTDVANAI
LDGTDAIMLS GETAQGKYPI EAFETMAKIA EKTEAYVGYK DIIDRNIDTN VSITNAISHA
TCTTARDIGA AAIITCTKSG YTARMVSRYR PQAPIIATTP SENVARKLSI VWGVYPLVTE
EVSTTDEMID VAIQSALTAG FIRNGDIVVI SAGIPVAMAG TTNMLKVHIV GDVLLRGIGI
GSKATTGAVC VINDISKDKD KFREGDIIVA AKTERDFMPL IEKASAIITE EGGLTSHAAI
VGLNLGIPVI VGCEGATSKL KDGMTVTVDT VRGFVYKGTV NIK
//
