ID I0JPN7_HALH3 Unreviewed; 587 AA.
AC I0JPN7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=pykA {ECO:0000313|EMBL:CCG46107.1};
GN OrderedLocusNames=HBHAL_3762 {ECO:0000313|EMBL:CCG46107.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG46107.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG46107.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
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; HE717023; CCG46107.1; -; Genomic_DNA.
DR RefSeq; WP_014643996.1; NC_017668.1.
DR AlphaFoldDB; I0JPN7; -.
DR STRING; 866895.HBHAL_3762; -.
DR KEGG; hhd:HBHAL_3762; -.
DR PATRIC; fig|866895.3.peg.2789; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_9; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000007397; 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 CDD; cd00288; Pyruvate_Kinase; 1.
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:CCG46107.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:CCG46107.1}.
FT DOMAIN 3..326
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 359..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 508..577
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 587 AA; 62611 MW; 60F38BE52A9CD225 CRC64;
MFRKTKIVST IGPASESVEK LSQLIEAGMN VARLNFSHGD FEEHGARIKN IREASASTGK
TVAILLDTKG PEIRTGTLKE EEVYLEKGST VYVSMDDIQG DAERISVTYP GLINDVQPGS
KILLDDGLVE LLVEEIDKKN NEIKTTVLNN GPLKNKKGVN VPNVSVNLPG ITDKDAKDIE
FGIEQGVDFI AASFVRRASD VLEIKELLEK HGALDIQIIP KIENQEGVDN IDEILEVSDG
LMVARGDLGV EIPAEDVPLV QKQLIHKCNK AGKPVITATQ MLDSMQRNPR PTRAEASDVA
NAIFDGTDAI MLSGETAAGD YPVESVQTMH NIASKTETGL NYKAILDERS KHSDMTITDA
ISQSVTHTAI NLDVNAVVTP TESGHTARMI SKYRPRAPIV AITSSEAVNR KLSLVWGVYA
VMGPRAQSTD DMLDVAVERS LASGVATRGD RVIITGGVPV GESGTTNLMK VHVIGDVLVK
GQGVGQKSAY GRAVVAKDPK EAIDRVVDGD ILVTHGTDRD MMPAIEKAAG LVTVEGGLTS
HAAVVGLSLG IPVIVGVKDA LSIISDGNDI TIDSSRGDIY EGHASVL
//
