ID R4U470_9MOLU Unreviewed; 478 AA.
AC R4U470;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 Name=pyk {ECO:0000313|EMBL:AGM26247.1};
GN ORFNames=SSYRP_v1c06570 {ECO:0000313|EMBL:AGM26247.1};
OS Spiroplasma syrphidicola EA-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276229 {ECO:0000313|EMBL:AGM26247.1, ECO:0000313|Proteomes:UP000013963};
RN [1] {ECO:0000313|EMBL:AGM26247.1, ECO:0000313|Proteomes:UP000013963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EA-1 {ECO:0000313|EMBL:AGM26247.1};
RX PubMed=23711669; DOI=10.1093/gbe/evt084;
RA Ku C., Lo W.S., Chen L.L., Kuo C.H.;
RT "Complete genomes of two dipteran-associated spiroplasmas provided insights
RT into the origin, dynamics, and impacts of viral invasion in spiroplasma.";
RL Genome Biol. Evol. 5:1151-1164(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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP005078; AGM26247.1; -; Genomic_DNA.
DR RefSeq; WP_016340891.1; NC_021284.1.
DR AlphaFoldDB; R4U470; -.
DR STRING; 1276229.SSYRP_v1c06570; -.
DR KEGG; ssyr:SSYRP_v1c06570; -.
DR PATRIC; fig|1276229.3.peg.652; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_14; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000013963; 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; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 1.
DR Pfam; PF00224; PK; 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:AGM26247.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013963};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 10..336
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 478 AA; 53239 MW; 460307993FB2BFE1 CRC64;
MDKINLKDKM KRTKIITTIG PSTHSEEGIT KLFDLGMNTI RLNFSHGDYE EQGARIVWTK
EIIKKIGKPI SIMLDTKGPE IRVGKMKDGK QEIVKGTKVT IYSLPAEYAS REGTGSEMTV
SYDMSQDLKV GDVVLVDDGK LQLNVTDVQP GVITTEAFNH HVVKTNKRIN LPGVAFTLPF
LADKDIADIK YGAEQGVDYI AASFVNTKEN VLEIRQLLKE ANAEHIQIIA KIESQIGINN
IDDIIAAADG IMVARGDLGL EIPYYDVPYW EKIIIRKCRE AGKVVIVATQ MLESMTDNPH
PTRAEVTDVY FATELGADAT MLSGESANGD YPFITVDTMA TINKRAEMEF YSKLYYEKQL
ENACQTTTGP RAEIAKKLAE KCKNGEYEYA VVLSNTGTLL KTVSKFRPNV VILGVSPTPE
LYTAFGVWHS IFMNKVDNYN EFKDNDQAII EVAKKWGAKV GSKILFARND VLKELIVE
//
