ID C4GCK0_9FIRM Unreviewed; 480 AA.
AC C4GCK0;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
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:EEP27700.1};
GN ORFNames=GCWU000342_01694 {ECO:0000313|EMBL:EEP27700.1};
OS Shuttleworthia satelles DSM 14600.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Shuttleworthia.
OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP27700.1, ECO:0000313|Proteomes:UP000003494};
RN [1] {ECO:0000313|EMBL:EEP27700.1, ECO:0000313|Proteomes:UP000003494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP27700.1,
RC ECO:0000313|Proteomes:UP000003494};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP27700.1}.
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DR EMBL; ACIP02000004; EEP27700.1; -; Genomic_DNA.
DR RefSeq; WP_006906689.1; NZ_GG665867.1.
DR AlphaFoldDB; C4GCK0; -.
DR STRING; 626523.GCWU000342_01694; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_9; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000003494; 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; 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, ECO:0000313|EMBL:EEP27700.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003494};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EEP27700.1}.
FT DOMAIN 5..326
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 365..477
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 480 AA; 52746 MW; 4696B51B03BE3477 CRC64;
MDYKRKTKII CTMGPSTDRD GVMEELVRAG MNVARFNFSH GDHEEQLGRL VKLREIRHRL
HLPVAALLDT KGPEIRLRDF RDRKVMLEDG QTFTLTTRQV EGTNEIVTVS YRDLPKDVEV
GSHILIDDGL VELEVTGLTD TDITCRVLNG GPVSNRKGVN VPNVDLTMDY LSEQDRSDLI
FGCQEGFDFI AASFTRTAED ILEIKKILHE HGGDNIKIIA KIESNQGVSN IDAIIDACDG
IMVARGDMGV EIPLEDVPIL QKEIIKKTLF KGKLVVTATQ MLDSMITHPR PTRAEAGDVA
NAVFDGTSAV MLSGETAAGN YPVQAVKTMA RICVRTEQDI NYKARLKERG VSAIEAKEED
GVALSIAHTA CTLAADIDAV AIINVTKSGH SCTQISKFRP ANPIIACCTD KQVMRQMNLY
WGVTPVMIET ESDIDRLLDD AVEAAVRANL MEKDQLAVVT AGLPLAVEGK TNLLKVHQAR
//
