ID A0A1H9IDC8_9BACI Unreviewed; 584 AA.
AC A0A1H9IDC8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=SAMN05216362_12425 {ECO:0000313|EMBL:SEQ72593.1};
OS Piscibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Piscibacillus.
OX NCBI_TaxID=571933 {ECO:0000313|EMBL:SEQ72593.1, ECO:0000313|Proteomes:UP000199427};
RN [1] {ECO:0000313|EMBL:SEQ72593.1, ECO:0000313|Proteomes:UP000199427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21633 {ECO:0000313|EMBL:SEQ72593.1,
RC ECO:0000313|Proteomes:UP000199427};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOES01000024; SEQ72593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9IDC8; -.
DR STRING; 571933.SAMN05216362_12425; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000199427; 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; 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:SEQ72593.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199427};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 2..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..469
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 502..574
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 584 AA; 63071 MW; 3D879B04E88853A4 CRC64;
MNKTKIVCTI GPASESVETL KELIDAGMNV ARLNFSHGDH EEQRQRIENI RQAANEKGKS
IAILLDTKGP EIRTGLFENG EVELEKGSTV TLTMEEVKGN QNRFTITYKG LIDDIEVGKQ
ILLDDGLIAL EVTDVNHDQQ EIVTKVLNTG VIKDRKGVNV PNVRVNLPGI TEKDANDILF
GIEQNVDFIA ASFVRRPSDV LEIRELLENN NADHIKIIPK IENREGVENL DQIINVSDGI
MVARGDLGVE IPAEEVPFIQ KTMIGKCNVA GKPVITATQM LDSMQRNPRP TRAEASDVAN
AIYDGTDAIM LSGETAAGDY PVDAVKTMFN IAVYTEKTLD NKAITNEIET DLTITDAISH
SAASLSEDLS VKAIITPTES GNTARMVSKY RPKAPIVAVT SHSYVSRQLS LVWGVYAVQG
DRVNTTDEML AHAIDQGLTT NLFNHGDRVV ITAGVPVGES GTTNLIKVHV VGHVVAKGQG
IGQQGAAGKA FVTNDLNKLE NDFQEGDILV TTATDRDMMP YIEKAAGIIT EEGGLTSHAA
VVALNVGIPV VVGVDQAMSK IEHGEEITID PSNGNIYQGR TSVI
//
