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Database: UniProt
Entry: A0A4V1Z1S2_9ACTN
LinkDB: A0A4V1Z1S2_9ACTN
Original site: A0A4V1Z1S2_9ACTN 
ID   A0A4V1Z1S2_9ACTN        Unreviewed;       482 AA.
AC   A0A4V1Z1S2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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:RYU11896.1};
GN   ORFNames=ETU37_11595 {ECO:0000313|EMBL:RYU11896.1};
OS   Nocardioides iriomotensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=715784 {ECO:0000313|EMBL:RYU11896.1, ECO:0000313|Proteomes:UP000291189};
RN   [1] {ECO:0000313|EMBL:RYU11896.1, ECO:0000313|Proteomes:UP000291189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105384 {ECO:0000313|EMBL:RYU11896.1,
RC   ECO:0000313|Proteomes:UP000291189};
RA   Fu Y., Cai Y., Lin Z., Chen P.;
RT   "Nocardioides guangzhouensis sp. nov., an actinobacterium isolated from
RT   soil.";
RL   Submitted (JAN-2019) 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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:RYU11896.1}.
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DR   EMBL; SDPU01000022; RYU11896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4V1Z1S2; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000291189; 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; PYRUVATE KINASE; 1.
DR   PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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:RYU11896.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291189};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:RYU11896.1}.
FT   DOMAIN          1..322
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          354..465
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   482 AA;  51998 MW;  14B85C9D820E9B9A CRC64;
     MRRAKIVCTL GPATSSPESI RALVDAGMDV ARMNMSHGSH ADHEKVYRMV REASDATGHA
     IGIFADLQGP KIRLGKVSAG PCQLEEGATF TITTREVPGD TEICSTTYDG LPGDVAKGDQ
     ILIDDGKVRL EVLEVDDTDV TTRVVVPGPV SDNKGINLPG VAVSVPALSE KDKEDLRFAL
     HLTVDFIALS FVRSAKDVED VRMVMHEEGI FLPVIAKIEK PQAIDNIEGI VDAFDGFMVA
     RGDLGVECPL EDVPFLQKHV IDVARRHAKP VIVATQMLES MITNPRPTRA EASDVANAVL
     DGADAVMLSG ETSVGDWPTE TVETMARIIE STEVHGLGRM TAIDWQPRTR GGVIAKAAAE
     VAQRVGAKYL VAFTQSGDSA RRLSRYRGPI PMIAFTPVAA VRSQLALSWG IETFKAPEVE
     HTDEMVRQVD EHLLKINRVV EGDLVVIIAG SPPGLPGSTN ALRIHRMGDA INEVAPAYRR
     FG
//
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