ID Q2FMN4_METHJ Unreviewed; 500 AA.
AC Q2FMN4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN OrderedLocusNames=Mhun_0465 {ECO:0000313|EMBL:ABD40227.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD40227.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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 -!- 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}.
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DR EMBL; CP000254; ABD40227.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2FMN4; -.
DR STRING; 323259.Mhun_0465; -.
DR EnsemblBacteria; ABD40227; ABD40227; Mhun_0465.
DR KEGG; mhu:Mhun_0465; -.
DR eggNOG; arCOG04120; Archaea.
DR HOGENOM; CLU_015439_0_2_2; -.
DR InParanoid; Q2FMN4; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001941; 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; 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:ABD40227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001941};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:ABD40227.1}.
FT DOMAIN 32..351
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 386..496
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 500 AA; 54554 MW; 77492FA7581AC0A8 CRC64;
MQSLPFIFRK LNISHIMKRR ASPSDPGISC TMRRTKIIAT IGPASSNPRI IREMILSGMD
IARLNLSHGS PPWHEETVQQ IRALADELNR EIGILVDIPG PKLRVLIHSP PRDVVPGDTI
HIAAEHEHAS GAIHVHPPDC IPKVCPGDVV LVGDGAVTLQ VLKPGPPMLT TVISGGTIRE
GMGVVIPGRR PDVPYAGARF IDYIRQGAAL RPDYIALSFV GSAEDIRDAR TLLTREGMGN
IPLIAKIECR RAVEGLDDII RHADAVMVAR GDLGVELPLE EVPYIQKLII TTCSQQGIPV
ITATEMLESM VSRGRPTRAE VTDVANAIVD GTDATMLSAE TSVGRYPGQA VVMMARIAIE
IEQHLPYLRI LNERSDWHEK NVEGIISYRA CYIAEELESP AIVAFTRSGL TAERVSRCRP
RSPVLALTPD PAVARRLLLR WGIQPVVFDP IQSADELFRA AVKIAKVTGI ATSKDQLVII
AGNFSGKEGR TNMIKVEEMP
//
